Ignet

Gene Information

Gene symbol: RIPK2

Gene name: receptor-interacting serine-threonine kinase 2

HGNC ID: 10020

Synonyms: RICK, RIP2, CARDIAK, CARD3

Related Genes

#	Gene Symbol	Number of hits
1	CBL	1 hits
2	CCKAR	1 hits
3	INS	1 hits
4	MAPK1	1 hits
5	PDX1	1 hits
6	PKD1	1 hits
7	PLCB1	1 hits
8	PPP1R13B	1 hits
9	PRKAA1	1 hits
10	PRKD1	1 hits
11	PTK2	1 hits
12	PTK2B	1 hits
13	RBL2	1 hits
14	SEC23IP	1 hits
15	SHC1	1 hits
16	STK11	1 hits

Related Sentences

#	PMID	Sentence
1	16713446	CCK, a physiological regulator of pancreatic function, rapidly activated Lyn.
2	16713446	CCK activation of Lyn required stimulation of high and low affinity CCK(A) receptor states.
3	16713446	CCK stimulated an association of Lyn with PKC-delta, Shc, p125(FAK) and PYK2 as well as with their autophosphorylated forms, but not with Cbl, p85, p130(CAS) or ERK 1/2.
4	16713446	CCK's activation of Lyn is likely an important mediator of its ability to cause tyrosine phosphorylation of numerous important cellular mediators such as p125(FAK), PYK2, PKC-delta and Shc, which play central roles in CCK's effects on acinar cell function.
5	16713446	CCK, a physiological regulator of pancreatic function, rapidly activated Lyn.
6	16713446	CCK activation of Lyn required stimulation of high and low affinity CCK(A) receptor states.
7	16713446	CCK stimulated an association of Lyn with PKC-delta, Shc, p125(FAK) and PYK2 as well as with their autophosphorylated forms, but not with Cbl, p85, p130(CAS) or ERK 1/2.
8	16713446	CCK's activation of Lyn is likely an important mediator of its ability to cause tyrosine phosphorylation of numerous important cellular mediators such as p125(FAK), PYK2, PKC-delta and Shc, which play central roles in CCK's effects on acinar cell function.
9	16713446	CCK, a physiological regulator of pancreatic function, rapidly activated Lyn.
10	16713446	CCK activation of Lyn required stimulation of high and low affinity CCK(A) receptor states.
11	16713446	CCK stimulated an association of Lyn with PKC-delta, Shc, p125(FAK) and PYK2 as well as with their autophosphorylated forms, but not with Cbl, p85, p130(CAS) or ERK 1/2.
12	16713446	CCK's activation of Lyn is likely an important mediator of its ability to cause tyrosine phosphorylation of numerous important cellular mediators such as p125(FAK), PYK2, PKC-delta and Shc, which play central roles in CCK's effects on acinar cell function.
13	17306383	CCK causes PKD1 activation in pancreatic acini by signaling through PKC-delta and PKC-independent pathways.
14	17306383	CCK activated PKD1 and caused a time- and dose-dependent increase in serine phosphorylation by activation of high- and low-affinity CCK(A) receptor states.
15	17306383	Inhibition of CCK-stimulated increases in phospholipase C, PKC activity or intracellular calcium decreased PKD1 S916 phosphorylation by 56%, 62% and 96%, respectively.
16	17306383	Inhibition of Src/PI3K/MAPK/tyrosine phosphorylation had no effect.
17	17306383	These results demonstrate that CCK(A) receptor activation leads to PKD activation by signaling through PKC-dependent and PKC-independent pathways.
18	17306383	CCK causes PKD1 activation in pancreatic acini by signaling through PKC-delta and PKC-independent pathways.
19	17306383	CCK activated PKD1 and caused a time- and dose-dependent increase in serine phosphorylation by activation of high- and low-affinity CCK(A) receptor states.
20	17306383	Inhibition of CCK-stimulated increases in phospholipase C, PKC activity or intracellular calcium decreased PKD1 S916 phosphorylation by 56%, 62% and 96%, respectively.
21	17306383	Inhibition of Src/PI3K/MAPK/tyrosine phosphorylation had no effect.
22	17306383	These results demonstrate that CCK(A) receptor activation leads to PKD activation by signaling through PKC-dependent and PKC-independent pathways.
23	17306383	CCK causes PKD1 activation in pancreatic acini by signaling through PKC-delta and PKC-independent pathways.
24	17306383	CCK activated PKD1 and caused a time- and dose-dependent increase in serine phosphorylation by activation of high- and low-affinity CCK(A) receptor states.
25	17306383	Inhibition of CCK-stimulated increases in phospholipase C, PKC activity or intracellular calcium decreased PKD1 S916 phosphorylation by 56%, 62% and 96%, respectively.
26	17306383	Inhibition of Src/PI3K/MAPK/tyrosine phosphorylation had no effect.
27	17306383	These results demonstrate that CCK(A) receptor activation leads to PKD activation by signaling through PKC-dependent and PKC-independent pathways.
28	17306383	CCK causes PKD1 activation in pancreatic acini by signaling through PKC-delta and PKC-independent pathways.
29	17306383	CCK activated PKD1 and caused a time- and dose-dependent increase in serine phosphorylation by activation of high- and low-affinity CCK(A) receptor states.
30	17306383	Inhibition of CCK-stimulated increases in phospholipase C, PKC activity or intracellular calcium decreased PKD1 S916 phosphorylation by 56%, 62% and 96%, respectively.
31	17306383	Inhibition of Src/PI3K/MAPK/tyrosine phosphorylation had no effect.
32	17306383	These results demonstrate that CCK(A) receptor activation leads to PKD activation by signaling through PKC-dependent and PKC-independent pathways.
33	20354156	LKB1 deletion with the RIP2.Cre transgene modifies pancreatic beta-cell morphology and enhances insulin secretion in vivo.
34	20354156	LKB1 phosphorylates AMP-activated protein kinase (AMPK) and several related protein kinases.
35	20354156	Whereas deletion of both catalytic isoforms of AMPK from the pancreatic beta-cell and hypothalamic neurons using the rat insulin promoter (RIP2).Cre transgene (betaAMPKdKO) diminishes insulin secretion in vivo, deletion of LKB1 in the beta-cell with an inducible Pdx-1.CreER transgene enhances insulin secretion in mice.
36	20354156	In contrast to Pdx1-CreER-mediated deletion, the expression of Glut2, glucose-induced changes in membrane potential and intracellular Ca(2+) were sharply reduced in betaLKB1KO mouse islets and the stimulation of insulin secretion was modestly inhibited.
37	20354156	We conclude that LKB1 and AMPK play distinct roles in the control of insulin secretion and that the timing of LKB1 deletion, and/or its loss from extrapancreatic sites, influences the final impact on beta-cell function.
38	21135058	RIP2-mediated LKB1 deletion causes axon degeneration in the spinal cord and hind-limb paralysis.
39	21135058	Deletion of both PRKAA1 genes, whose products AMPKα1 and AMPKα2 are also downstream targets of LKB1, with the same strategy was without effect.