Ignet

Gene Information

Gene symbol: PKN1

Gene name: protein kinase N1

HGNC ID: 9405

Synonyms: DBK, PRK1, PKN, MGC46204, PAK1

Related Genes

#	Gene Symbol	Number of hits
1	AKT1	1 hits
2	ARF6	1 hits
3	BIRC5	1 hits
4	CASP3	1 hits
5	CCND1	1 hits
6	CD28	1 hits
7	CDC42	1 hits
8	CDKN1A	1 hits
9	CYCS	1 hits
10	DMPK	1 hits
11	INS	1 hits
12	MAPK1	1 hits
13	MAPK3	1 hits
14	MAPK6	1 hits
15	MYC	1 hits
16	PDK1	1 hits
17	PLK3	1 hits
18	PRKAA1	1 hits
19	RAC1	1 hits
20	RAF1	1 hits
21	RPS27A	1 hits
22	RPS6KA1	1 hits
23	SGK1	1 hits
24	SLC2A4	1 hits
25	SPG21	1 hits
26	STK11	1 hits
27	STK38	1 hits
28	TIAM1	1 hits
29	ZAP70	1 hits

Related Sentences

#	PMID	Sentence
1	10395678	TCR and CD28 are coupled via ZAP-70 to the activation of the Vav/Rac-1-/PAK-1/p38 MAPK signaling pathway.
2	10395678	The small GTPase Rac-1 controls the catalytic activity of the mitogen-activated protein kinases (MAPKs) and cell cycle progression through G1.
3	10395678	Rac-1 activation requires the phospho-tyrosine (p-Tyr)-dependent recruitment of the Vav GDP releasing factor (GRF) to the plasma membrane and assembly of GTPase/GRF complexes, an event critical for Ag receptor-triggered T cell activation.
4	10395678	Here, we show that TCR/CD28 costimulation synergistically induces Rac-1 GDP/GTP exchange.
5	10395678	Our findings, obtained by using ZAP-70-negative Jurkat T cells, indicate that CD28 costimulation augments TCR-mediated T cell activation by increasing the ZAP-70-mediated Tyr phosphorylation of Vav.
6	10395678	This event regulates the Rac-1-associated GTP/GDP exchange activity of Vav and downstream pathway(s) leading to PAK-1 and p38 MAPK activation.
7	10395678	CD28 amplifies TCR-induced ZAP-70 activity and association of Vav with ZAP-70 and linker for activation of T cells (LAT).
8	10395678	These results favor a model in which ZAP-70 regulates the intersection of the TCR and CD28 signaling pathways, which elicits the coupling of TCR and CD28 to the Rac-1, PAK-1, and p38 MAPK effector molecules.
9	10395678	TCR and CD28 are coupled via ZAP-70 to the activation of the Vav/Rac-1-/PAK-1/p38 MAPK signaling pathway.
10	10395678	The small GTPase Rac-1 controls the catalytic activity of the mitogen-activated protein kinases (MAPKs) and cell cycle progression through G1.
11	10395678	Rac-1 activation requires the phospho-tyrosine (p-Tyr)-dependent recruitment of the Vav GDP releasing factor (GRF) to the plasma membrane and assembly of GTPase/GRF complexes, an event critical for Ag receptor-triggered T cell activation.
12	10395678	Here, we show that TCR/CD28 costimulation synergistically induces Rac-1 GDP/GTP exchange.
13	10395678	Our findings, obtained by using ZAP-70-negative Jurkat T cells, indicate that CD28 costimulation augments TCR-mediated T cell activation by increasing the ZAP-70-mediated Tyr phosphorylation of Vav.
14	10395678	This event regulates the Rac-1-associated GTP/GDP exchange activity of Vav and downstream pathway(s) leading to PAK-1 and p38 MAPK activation.
15	10395678	CD28 amplifies TCR-induced ZAP-70 activity and association of Vav with ZAP-70 and linker for activation of T cells (LAT).
16	10395678	These results favor a model in which ZAP-70 regulates the intersection of the TCR and CD28 signaling pathways, which elicits the coupling of TCR and CD28 to the Rac-1, PAK-1, and p38 MAPK effector molecules.
17	10395678	TCR and CD28 are coupled via ZAP-70 to the activation of the Vav/Rac-1-/PAK-1/p38 MAPK signaling pathway.
18	10395678	The small GTPase Rac-1 controls the catalytic activity of the mitogen-activated protein kinases (MAPKs) and cell cycle progression through G1.
19	10395678	Rac-1 activation requires the phospho-tyrosine (p-Tyr)-dependent recruitment of the Vav GDP releasing factor (GRF) to the plasma membrane and assembly of GTPase/GRF complexes, an event critical for Ag receptor-triggered T cell activation.
20	10395678	Here, we show that TCR/CD28 costimulation synergistically induces Rac-1 GDP/GTP exchange.
21	10395678	Our findings, obtained by using ZAP-70-negative Jurkat T cells, indicate that CD28 costimulation augments TCR-mediated T cell activation by increasing the ZAP-70-mediated Tyr phosphorylation of Vav.
22	10395678	This event regulates the Rac-1-associated GTP/GDP exchange activity of Vav and downstream pathway(s) leading to PAK-1 and p38 MAPK activation.
23	10395678	CD28 amplifies TCR-induced ZAP-70 activity and association of Vav with ZAP-70 and linker for activation of T cells (LAT).
24	10395678	These results favor a model in which ZAP-70 regulates the intersection of the TCR and CD28 signaling pathways, which elicits the coupling of TCR and CD28 to the Rac-1, PAK-1, and p38 MAPK effector molecules.
25	11733498	Interaction between active Pak1 and Raf-1 is necessary for phosphorylation and activation of Raf-1.
26	11733498	Previous studies have shown that Pak1/2 is implicated in both Ras-dependent and -independent activation of Raf-1 by phosphorylating Raf Ser(338).
27	11733498	The present study explores the structural basis of Raf-1 phosphorylation by Pak1.
28	11733498	Interaction between active Pak1 and Raf-1 is necessary for phosphorylation and activation of Raf-1.
29	11733498	Previous studies have shown that Pak1/2 is implicated in both Ras-dependent and -independent activation of Raf-1 by phosphorylating Raf Ser(338).
30	11733498	The present study explores the structural basis of Raf-1 phosphorylation by Pak1.
31	11733498	Interaction between active Pak1 and Raf-1 is necessary for phosphorylation and activation of Raf-1.
32	11733498	Previous studies have shown that Pak1/2 is implicated in both Ras-dependent and -independent activation of Raf-1 by phosphorylating Raf Ser(338).
33	11733498	The present study explores the structural basis of Raf-1 phosphorylation by Pak1.
34	14614828	LKB1 is the upstream kinase in the AMP-activated protein kinase cascade.
35	14614828	We previously reported the identification of three protein kinases (Elm1, Pak1, and Tos3 [9]) that lie upstream of Snf1, the yeast homologue of AMPK.
36	14614828	LKB1 shares sequence similarity with Elm1, Pak1, and Tos3, and we demonstrated that LKB1 phosphorylates AMPK on the activation loop threonine (Thr172) within the catalytic subunit and activates AMPK in vitro [9].
37	14614828	AMPKK purified from rat liver corresponds to LKB1, and blocking LKB1 activity in cells abolishes AMPK activation in response to different stimuli.
38	14614828	LKB1 is the upstream kinase in the AMP-activated protein kinase cascade.
39	14614828	We previously reported the identification of three protein kinases (Elm1, Pak1, and Tos3 [9]) that lie upstream of Snf1, the yeast homologue of AMPK.
40	14614828	LKB1 shares sequence similarity with Elm1, Pak1, and Tos3, and we demonstrated that LKB1 phosphorylates AMPK on the activation loop threonine (Thr172) within the catalytic subunit and activates AMPK in vitro [9].
41	14614828	AMPKK purified from rat liver corresponds to LKB1, and blocking LKB1 activity in cells abolishes AMPK activation in response to different stimuli.
42	19581924	We found previously that in intestinal cells, insulin or insulin-like growth factor-1 stimulates c-Myc and cyclin D1 protein expression through both Akt-dependent and Akt-independent mechanisms.
43	19581924	The effect of Akt is attributed to the stimulation of c-Myc translation by mammalian target of rapamycin.
44	19581924	However, Akt-independent stimulation was, associated with an increase in beta-catenin (beta-cat) in the nucleus and an increased association between beta-cat and T-cell factor binding sites on the c-Myc promoter, detected by chromatin immunoprecipitation.
45	19581924	In this study, we show that insulin stimulated the phosphorylation/activation of p-21-activated protein kinase-1 (PAK-1) in an Akt-independent manner in vitro and in an in vivo hyperinsulinemic mouse model.
46	19581924	Significantly, shRNA (small hairpin RNA)-mediated PAK-1 knockdown attenuated both basal and insulin-stimulated c-Myc and cyclin D1 expression, associated with a marked reduction in extracellular signal-regulated kinase activation and beta-cat phosphorylation at Ser675.
47	19581924	Furthermore, PAK-1 silencing led to a complete blockade of insulin-stimulated beta-cat binding to the c-Myc promoter and cellular growth.
48	19581924	Finally, inhibition of MEK, a downstream target of PAK-1, blocked insulin-stimulated nuclear beta-cat accumulation and c-Myc expression.
49	19581924	Our observations suggest that PAK-1 serves as an important linker between insulin and Wnt signaling pathways.
50	19581924	We found previously that in intestinal cells, insulin or insulin-like growth factor-1 stimulates c-Myc and cyclin D1 protein expression through both Akt-dependent and Akt-independent mechanisms.
51	19581924	The effect of Akt is attributed to the stimulation of c-Myc translation by mammalian target of rapamycin.
52	19581924	However, Akt-independent stimulation was, associated with an increase in beta-catenin (beta-cat) in the nucleus and an increased association between beta-cat and T-cell factor binding sites on the c-Myc promoter, detected by chromatin immunoprecipitation.
53	19581924	In this study, we show that insulin stimulated the phosphorylation/activation of p-21-activated protein kinase-1 (PAK-1) in an Akt-independent manner in vitro and in an in vivo hyperinsulinemic mouse model.
54	19581924	Significantly, shRNA (small hairpin RNA)-mediated PAK-1 knockdown attenuated both basal and insulin-stimulated c-Myc and cyclin D1 expression, associated with a marked reduction in extracellular signal-regulated kinase activation and beta-cat phosphorylation at Ser675.
55	19581924	Furthermore, PAK-1 silencing led to a complete blockade of insulin-stimulated beta-cat binding to the c-Myc promoter and cellular growth.
56	19581924	Finally, inhibition of MEK, a downstream target of PAK-1, blocked insulin-stimulated nuclear beta-cat accumulation and c-Myc expression.
57	19581924	Our observations suggest that PAK-1 serves as an important linker between insulin and Wnt signaling pathways.
58	19581924	We found previously that in intestinal cells, insulin or insulin-like growth factor-1 stimulates c-Myc and cyclin D1 protein expression through both Akt-dependent and Akt-independent mechanisms.
59	19581924	The effect of Akt is attributed to the stimulation of c-Myc translation by mammalian target of rapamycin.
60	19581924	However, Akt-independent stimulation was, associated with an increase in beta-catenin (beta-cat) in the nucleus and an increased association between beta-cat and T-cell factor binding sites on the c-Myc promoter, detected by chromatin immunoprecipitation.
61	19581924	In this study, we show that insulin stimulated the phosphorylation/activation of p-21-activated protein kinase-1 (PAK-1) in an Akt-independent manner in vitro and in an in vivo hyperinsulinemic mouse model.
62	19581924	Significantly, shRNA (small hairpin RNA)-mediated PAK-1 knockdown attenuated both basal and insulin-stimulated c-Myc and cyclin D1 expression, associated with a marked reduction in extracellular signal-regulated kinase activation and beta-cat phosphorylation at Ser675.
63	19581924	Furthermore, PAK-1 silencing led to a complete blockade of insulin-stimulated beta-cat binding to the c-Myc promoter and cellular growth.
64	19581924	Finally, inhibition of MEK, a downstream target of PAK-1, blocked insulin-stimulated nuclear beta-cat accumulation and c-Myc expression.
65	19581924	Our observations suggest that PAK-1 serves as an important linker between insulin and Wnt signaling pathways.
66	19581924	We found previously that in intestinal cells, insulin or insulin-like growth factor-1 stimulates c-Myc and cyclin D1 protein expression through both Akt-dependent and Akt-independent mechanisms.
67	19581924	The effect of Akt is attributed to the stimulation of c-Myc translation by mammalian target of rapamycin.
68	19581924	However, Akt-independent stimulation was, associated with an increase in beta-catenin (beta-cat) in the nucleus and an increased association between beta-cat and T-cell factor binding sites on the c-Myc promoter, detected by chromatin immunoprecipitation.
69	19581924	In this study, we show that insulin stimulated the phosphorylation/activation of p-21-activated protein kinase-1 (PAK-1) in an Akt-independent manner in vitro and in an in vivo hyperinsulinemic mouse model.
70	19581924	Significantly, shRNA (small hairpin RNA)-mediated PAK-1 knockdown attenuated both basal and insulin-stimulated c-Myc and cyclin D1 expression, associated with a marked reduction in extracellular signal-regulated kinase activation and beta-cat phosphorylation at Ser675.
71	19581924	Furthermore, PAK-1 silencing led to a complete blockade of insulin-stimulated beta-cat binding to the c-Myc promoter and cellular growth.
72	19581924	Finally, inhibition of MEK, a downstream target of PAK-1, blocked insulin-stimulated nuclear beta-cat accumulation and c-Myc expression.
73	19581924	Our observations suggest that PAK-1 serves as an important linker between insulin and Wnt signaling pathways.
74	19581924	We found previously that in intestinal cells, insulin or insulin-like growth factor-1 stimulates c-Myc and cyclin D1 protein expression through both Akt-dependent and Akt-independent mechanisms.
75	19581924	The effect of Akt is attributed to the stimulation of c-Myc translation by mammalian target of rapamycin.
76	19581924	However, Akt-independent stimulation was, associated with an increase in beta-catenin (beta-cat) in the nucleus and an increased association between beta-cat and T-cell factor binding sites on the c-Myc promoter, detected by chromatin immunoprecipitation.
77	19581924	In this study, we show that insulin stimulated the phosphorylation/activation of p-21-activated protein kinase-1 (PAK-1) in an Akt-independent manner in vitro and in an in vivo hyperinsulinemic mouse model.
78	19581924	Significantly, shRNA (small hairpin RNA)-mediated PAK-1 knockdown attenuated both basal and insulin-stimulated c-Myc and cyclin D1 expression, associated with a marked reduction in extracellular signal-regulated kinase activation and beta-cat phosphorylation at Ser675.
79	19581924	Furthermore, PAK-1 silencing led to a complete blockade of insulin-stimulated beta-cat binding to the c-Myc promoter and cellular growth.
80	19581924	Finally, inhibition of MEK, a downstream target of PAK-1, blocked insulin-stimulated nuclear beta-cat accumulation and c-Myc expression.
81	19581924	Our observations suggest that PAK-1 serves as an important linker between insulin and Wnt signaling pathways.
82	21969371	Inhibition or ablation of p21-activated kinase (PAK1) disrupts glucose homeostatic mechanisms in vivo.
83	21969371	The p21-activated kinase PAK1 is implicated in tumorigenesis, and efforts to inhibit PAK1 signaling as a means to induce tumor cell apoptosis are underway.
84	21969371	Mimicking this, islets from PAK1(-/-) knock-out mice exhibited profound defects in the second/sustained-phase of insulin secretion.
85	21969371	Analyses of human and mouse islet beta cell signaling revealed PAK1 activation to be 1) dependent upon Cdc42 abundance, 2) crucial for signaling downstream to activate ERK1/2, but 3) dispensable for cofilin phosphorylation.
86	21969371	Exacerbating this, the PAK1(-/-) knock-out mice also exhibited peripheral insulin resistance.
87	21969371	Insulin resistance was coupled to ablation of insulin-stimulated GLUT4 translocation in skeletal muscle from PAK1(-/-) knock-out mice, and in sharp contrast to islet beta cells, skeletal muscle PAK1 loss was underscored by defective cofilin phosphorylation but normal ERK1/2 activation.
88	21969371	Inhibition or ablation of p21-activated kinase (PAK1) disrupts glucose homeostatic mechanisms in vivo.
89	21969371	The p21-activated kinase PAK1 is implicated in tumorigenesis, and efforts to inhibit PAK1 signaling as a means to induce tumor cell apoptosis are underway.
90	21969371	Mimicking this, islets from PAK1(-/-) knock-out mice exhibited profound defects in the second/sustained-phase of insulin secretion.
91	21969371	Analyses of human and mouse islet beta cell signaling revealed PAK1 activation to be 1) dependent upon Cdc42 abundance, 2) crucial for signaling downstream to activate ERK1/2, but 3) dispensable for cofilin phosphorylation.
92	21969371	Exacerbating this, the PAK1(-/-) knock-out mice also exhibited peripheral insulin resistance.
93	21969371	Insulin resistance was coupled to ablation of insulin-stimulated GLUT4 translocation in skeletal muscle from PAK1(-/-) knock-out mice, and in sharp contrast to islet beta cells, skeletal muscle PAK1 loss was underscored by defective cofilin phosphorylation but normal ERK1/2 activation.
94	21969371	Inhibition or ablation of p21-activated kinase (PAK1) disrupts glucose homeostatic mechanisms in vivo.
95	21969371	The p21-activated kinase PAK1 is implicated in tumorigenesis, and efforts to inhibit PAK1 signaling as a means to induce tumor cell apoptosis are underway.
96	21969371	Mimicking this, islets from PAK1(-/-) knock-out mice exhibited profound defects in the second/sustained-phase of insulin secretion.
97	21969371	Analyses of human and mouse islet beta cell signaling revealed PAK1 activation to be 1) dependent upon Cdc42 abundance, 2) crucial for signaling downstream to activate ERK1/2, but 3) dispensable for cofilin phosphorylation.
98	21969371	Exacerbating this, the PAK1(-/-) knock-out mice also exhibited peripheral insulin resistance.
99	21969371	Insulin resistance was coupled to ablation of insulin-stimulated GLUT4 translocation in skeletal muscle from PAK1(-/-) knock-out mice, and in sharp contrast to islet beta cells, skeletal muscle PAK1 loss was underscored by defective cofilin phosphorylation but normal ERK1/2 activation.
100	21969371	Inhibition or ablation of p21-activated kinase (PAK1) disrupts glucose homeostatic mechanisms in vivo.
101	21969371	The p21-activated kinase PAK1 is implicated in tumorigenesis, and efforts to inhibit PAK1 signaling as a means to induce tumor cell apoptosis are underway.
102	21969371	Mimicking this, islets from PAK1(-/-) knock-out mice exhibited profound defects in the second/sustained-phase of insulin secretion.
103	21969371	Analyses of human and mouse islet beta cell signaling revealed PAK1 activation to be 1) dependent upon Cdc42 abundance, 2) crucial for signaling downstream to activate ERK1/2, but 3) dispensable for cofilin phosphorylation.
104	21969371	Exacerbating this, the PAK1(-/-) knock-out mice also exhibited peripheral insulin resistance.
105	21969371	Insulin resistance was coupled to ablation of insulin-stimulated GLUT4 translocation in skeletal muscle from PAK1(-/-) knock-out mice, and in sharp contrast to islet beta cells, skeletal muscle PAK1 loss was underscored by defective cofilin phosphorylation but normal ERK1/2 activation.
106	21969371	Inhibition or ablation of p21-activated kinase (PAK1) disrupts glucose homeostatic mechanisms in vivo.
107	21969371	The p21-activated kinase PAK1 is implicated in tumorigenesis, and efforts to inhibit PAK1 signaling as a means to induce tumor cell apoptosis are underway.
108	21969371	Mimicking this, islets from PAK1(-/-) knock-out mice exhibited profound defects in the second/sustained-phase of insulin secretion.
109	21969371	Analyses of human and mouse islet beta cell signaling revealed PAK1 activation to be 1) dependent upon Cdc42 abundance, 2) crucial for signaling downstream to activate ERK1/2, but 3) dispensable for cofilin phosphorylation.
110	21969371	Exacerbating this, the PAK1(-/-) knock-out mice also exhibited peripheral insulin resistance.
111	21969371	Insulin resistance was coupled to ablation of insulin-stimulated GLUT4 translocation in skeletal muscle from PAK1(-/-) knock-out mice, and in sharp contrast to islet beta cells, skeletal muscle PAK1 loss was underscored by defective cofilin phosphorylation but normal ERK1/2 activation.
112	21969371	Inhibition or ablation of p21-activated kinase (PAK1) disrupts glucose homeostatic mechanisms in vivo.
113	21969371	The p21-activated kinase PAK1 is implicated in tumorigenesis, and efforts to inhibit PAK1 signaling as a means to induce tumor cell apoptosis are underway.
114	21969371	Mimicking this, islets from PAK1(-/-) knock-out mice exhibited profound defects in the second/sustained-phase of insulin secretion.
115	21969371	Analyses of human and mouse islet beta cell signaling revealed PAK1 activation to be 1) dependent upon Cdc42 abundance, 2) crucial for signaling downstream to activate ERK1/2, but 3) dispensable for cofilin phosphorylation.
116	21969371	Exacerbating this, the PAK1(-/-) knock-out mice also exhibited peripheral insulin resistance.
117	21969371	Insulin resistance was coupled to ablation of insulin-stimulated GLUT4 translocation in skeletal muscle from PAK1(-/-) knock-out mice, and in sharp contrast to islet beta cells, skeletal muscle PAK1 loss was underscored by defective cofilin phosphorylation but normal ERK1/2 activation.
118	23423567	Rac1 signaling is required for insulin-stimulated glucose uptake and is dysregulated in insulin-resistant murine and human skeletal muscle.
119	23423567	The actin cytoskeleton-regulating GTPase Rac1 is required for insulin-stimulated GLUT4 translocation in cultured muscle cells.
120	23423567	However, involvement of Rac1 and its downstream signaling in glucose transport in insulin-sensitive and insulin-resistant mature skeletal muscle has not previously been investigated.
121	23423567	We hypothesized that Rac1 and its downstream target, p21-activated kinase (PAK), are regulators of insulin-stimulated glucose uptake in mouse and human skeletal muscle and are dysregulated in insulin-resistant states.
122	23423567	Muscle-specific inducible Rac1 knockout (KO) mice and pharmacological inhibition of Rac1 were used to determine whether Rac1 regulates insulin-stimulated glucose transport in mature skeletal muscle.
123	23423567	Furthermore, Rac1 and PAK1 expression and signaling were investigated in muscle of insulin-resistant mice and humans.
124	23423567	Inhibition and KO of Rac1 decreased insulin-stimulated glucose transport in mouse soleus and extensor digitorum longus muscles ex vivo.
125	23423567	Rac1 KO mice showed decreased insulin and glucose tolerance and trended toward higher plasma insulin concentrations after intraperitoneal glucose injection.
126	23423567	Rac1 protein expression and insulin-stimulated PAK(Thr423) phosphorylation were decreased in muscles of high fat-fed mice.
127	23423567	These findings show that Rac1 is a regulator of insulin-stimulated glucose uptake and a novel candidate involved in skeletal muscle insulin resistance.
128	23514967	Depletion of PAK1 enhances ubiquitin-mediated survivin degradation in pancreatic β-cells.
129	23514967	Here, we aim to address the linkage between PAK1 and Survivin, a protein essential for β-cell replication.
130	23514967	PAK1 knockout (KO) mouse islets exhibited decreased expression of Survivin protein.
131	23514967	MIN6 β-cells with siRNA-mediated suppression of PAK1 also had decreased Survivin protein and exhibited an increased level of ubiquitinated-Survivin.
132	23514967	However, no significant changes in Survivin mRNA were found in islets from PAK1 KO mice and PAK1-depleted MIN6 β-cells.
133	23514967	The decreased Survivin level in MIN6 cells subjected to hyperglycemic stress was prevented by expression of exogenous PAK1.
134	23514967	Moreover, overexpressing Survivin restored proliferation of β-cells that was impaired by the loss of PAK1.
135	23514967	These data implicate a role for PAK1 in regulating Survivin protein stability in the β-cell and suggest PAK1 as a potential molecular target for the restoration of β-cell mass.
136	23514967	Depletion of PAK1 enhances ubiquitin-mediated survivin degradation in pancreatic β-cells.
137	23514967	Here, we aim to address the linkage between PAK1 and Survivin, a protein essential for β-cell replication.
138	23514967	PAK1 knockout (KO) mouse islets exhibited decreased expression of Survivin protein.
139	23514967	MIN6 β-cells with siRNA-mediated suppression of PAK1 also had decreased Survivin protein and exhibited an increased level of ubiquitinated-Survivin.
140	23514967	However, no significant changes in Survivin mRNA were found in islets from PAK1 KO mice and PAK1-depleted MIN6 β-cells.
141	23514967	The decreased Survivin level in MIN6 cells subjected to hyperglycemic stress was prevented by expression of exogenous PAK1.
142	23514967	Moreover, overexpressing Survivin restored proliferation of β-cells that was impaired by the loss of PAK1.
143	23514967	These data implicate a role for PAK1 in regulating Survivin protein stability in the β-cell and suggest PAK1 as a potential molecular target for the restoration of β-cell mass.
144	23514967	Depletion of PAK1 enhances ubiquitin-mediated survivin degradation in pancreatic β-cells.
145	23514967	Here, we aim to address the linkage between PAK1 and Survivin, a protein essential for β-cell replication.
146	23514967	PAK1 knockout (KO) mouse islets exhibited decreased expression of Survivin protein.
147	23514967	MIN6 β-cells with siRNA-mediated suppression of PAK1 also had decreased Survivin protein and exhibited an increased level of ubiquitinated-Survivin.
148	23514967	However, no significant changes in Survivin mRNA were found in islets from PAK1 KO mice and PAK1-depleted MIN6 β-cells.
149	23514967	The decreased Survivin level in MIN6 cells subjected to hyperglycemic stress was prevented by expression of exogenous PAK1.
150	23514967	Moreover, overexpressing Survivin restored proliferation of β-cells that was impaired by the loss of PAK1.
151	23514967	These data implicate a role for PAK1 in regulating Survivin protein stability in the β-cell and suggest PAK1 as a potential molecular target for the restoration of β-cell mass.
152	23514967	Depletion of PAK1 enhances ubiquitin-mediated survivin degradation in pancreatic β-cells.
153	23514967	Here, we aim to address the linkage between PAK1 and Survivin, a protein essential for β-cell replication.
154	23514967	PAK1 knockout (KO) mouse islets exhibited decreased expression of Survivin protein.
155	23514967	MIN6 β-cells with siRNA-mediated suppression of PAK1 also had decreased Survivin protein and exhibited an increased level of ubiquitinated-Survivin.
156	23514967	However, no significant changes in Survivin mRNA were found in islets from PAK1 KO mice and PAK1-depleted MIN6 β-cells.
157	23514967	The decreased Survivin level in MIN6 cells subjected to hyperglycemic stress was prevented by expression of exogenous PAK1.
158	23514967	Moreover, overexpressing Survivin restored proliferation of β-cells that was impaired by the loss of PAK1.
159	23514967	These data implicate a role for PAK1 in regulating Survivin protein stability in the β-cell and suggest PAK1 as a potential molecular target for the restoration of β-cell mass.
160	23514967	Depletion of PAK1 enhances ubiquitin-mediated survivin degradation in pancreatic β-cells.
161	23514967	Here, we aim to address the linkage between PAK1 and Survivin, a protein essential for β-cell replication.
162	23514967	PAK1 knockout (KO) mouse islets exhibited decreased expression of Survivin protein.
163	23514967	MIN6 β-cells with siRNA-mediated suppression of PAK1 also had decreased Survivin protein and exhibited an increased level of ubiquitinated-Survivin.
164	23514967	However, no significant changes in Survivin mRNA were found in islets from PAK1 KO mice and PAK1-depleted MIN6 β-cells.
165	23514967	The decreased Survivin level in MIN6 cells subjected to hyperglycemic stress was prevented by expression of exogenous PAK1.
166	23514967	Moreover, overexpressing Survivin restored proliferation of β-cells that was impaired by the loss of PAK1.
167	23514967	These data implicate a role for PAK1 in regulating Survivin protein stability in the β-cell and suggest PAK1 as a potential molecular target for the restoration of β-cell mass.
168	23514967	Depletion of PAK1 enhances ubiquitin-mediated survivin degradation in pancreatic β-cells.
169	23514967	Here, we aim to address the linkage between PAK1 and Survivin, a protein essential for β-cell replication.
170	23514967	PAK1 knockout (KO) mouse islets exhibited decreased expression of Survivin protein.
171	23514967	MIN6 β-cells with siRNA-mediated suppression of PAK1 also had decreased Survivin protein and exhibited an increased level of ubiquitinated-Survivin.
172	23514967	However, no significant changes in Survivin mRNA were found in islets from PAK1 KO mice and PAK1-depleted MIN6 β-cells.
173	23514967	The decreased Survivin level in MIN6 cells subjected to hyperglycemic stress was prevented by expression of exogenous PAK1.
174	23514967	Moreover, overexpressing Survivin restored proliferation of β-cells that was impaired by the loss of PAK1.
175	23514967	These data implicate a role for PAK1 in regulating Survivin protein stability in the β-cell and suggest PAK1 as a potential molecular target for the restoration of β-cell mass.
176	23514967	Depletion of PAK1 enhances ubiquitin-mediated survivin degradation in pancreatic β-cells.
177	23514967	Here, we aim to address the linkage between PAK1 and Survivin, a protein essential for β-cell replication.
178	23514967	PAK1 knockout (KO) mouse islets exhibited decreased expression of Survivin protein.
179	23514967	MIN6 β-cells with siRNA-mediated suppression of PAK1 also had decreased Survivin protein and exhibited an increased level of ubiquitinated-Survivin.
180	23514967	However, no significant changes in Survivin mRNA were found in islets from PAK1 KO mice and PAK1-depleted MIN6 β-cells.
181	23514967	The decreased Survivin level in MIN6 cells subjected to hyperglycemic stress was prevented by expression of exogenous PAK1.
182	23514967	Moreover, overexpressing Survivin restored proliferation of β-cells that was impaired by the loss of PAK1.
183	23514967	These data implicate a role for PAK1 in regulating Survivin protein stability in the β-cell and suggest PAK1 as a potential molecular target for the restoration of β-cell mass.
184	23514967	Depletion of PAK1 enhances ubiquitin-mediated survivin degradation in pancreatic β-cells.
185	23514967	Here, we aim to address the linkage between PAK1 and Survivin, a protein essential for β-cell replication.
186	23514967	PAK1 knockout (KO) mouse islets exhibited decreased expression of Survivin protein.
187	23514967	MIN6 β-cells with siRNA-mediated suppression of PAK1 also had decreased Survivin protein and exhibited an increased level of ubiquitinated-Survivin.
188	23514967	However, no significant changes in Survivin mRNA were found in islets from PAK1 KO mice and PAK1-depleted MIN6 β-cells.
189	23514967	The decreased Survivin level in MIN6 cells subjected to hyperglycemic stress was prevented by expression of exogenous PAK1.
190	23514967	Moreover, overexpressing Survivin restored proliferation of β-cells that was impaired by the loss of PAK1.
191	23514967	These data implicate a role for PAK1 in regulating Survivin protein stability in the β-cell and suggest PAK1 as a potential molecular target for the restoration of β-cell mass.
192	23524293	The group of AGC protein kinases includes more than 60 protein kinases in the human genome, classified into 14 families: PDK1, AKT/PKB, SGK, PKA, PKG, PKC, PKN/PRK, RSK, NDR, MAST, YANK, DMPK, GRK and SGK494.
193	23524293	This site is also essential to the mechanism of activation of AGC kinases by phosphorylation and is involved in the allosteric regulation of N-terminal domains of several AGC kinases, such as PKN/PRKs and atypical PKCs.
194	23524293	The group of AGC protein kinases includes more than 60 protein kinases in the human genome, classified into 14 families: PDK1, AKT/PKB, SGK, PKA, PKG, PKC, PKN/PRK, RSK, NDR, MAST, YANK, DMPK, GRK and SGK494.
195	23524293	This site is also essential to the mechanism of activation of AGC kinases by phosphorylation and is involved in the allosteric regulation of N-terminal domains of several AGC kinases, such as PKN/PRKs and atypical PKCs.
196	23650610	Toward addressing linkage of PAK1 to β-cell survival, PAK1-siRNA targeted MIN6 pancreatic β-cells were found to exhibit increased caspase-3 cleavage, cytosolic cytochrome-C and the pro-apoptotic protein Bad.
197	23747564	AGE-BSA-FITC uptake was significantly inhibited by amiloride and inhibitors of Arf6, Rac1, racGEF Tiam1, PAK1 and actin polymerisation.
198	23747564	AGE-BSA increased PAK1 kinase activity (212±41% vs control, p<0.05) and protein levels of Tiam1, a Rac1 activator.
199	23747564	AGE-BSA-FITC uptake was significantly inhibited by amiloride and inhibitors of Arf6, Rac1, racGEF Tiam1, PAK1 and actin polymerisation.
200	23747564	AGE-BSA increased PAK1 kinase activity (212±41% vs control, p<0.05) and protein levels of Tiam1, a Rac1 activator.