Ignet

Gene Information

Gene symbol: PRKD1

Gene name: protein kinase D1

HGNC ID: 9407

Synonyms: PKCM, PKD, PKC-mu

Related Genes

#	Gene Symbol	Number of hits
1	ANKS3	1 hits
2	ANKS6	1 hits
3	BICC1	1 hits
4	DDHD2	1 hits
5	KIRREL	1 hits
6	LAMA5	1 hits
7	PKD1	1 hits
8	PRKAA1	1 hits
9	PRKAR1A	1 hits
10	VASP	1 hits

Related Sentences

#	PMID	Sentence
1	12660326	Homodimerization and heterodimerization of the glomerular podocyte proteins nephrin and NEPH1.
2	12660326	Nephrin and NEPH1, the gene products of NPHS1 and NEPH1, are podocyte membrane proteins of the Ig superfamily.
3	12660326	Similar to the nephrin knockout, mice lacking NEPH1 show severe proteinuria leading to perinatal death.
4	12660326	This NEPH1-Ig fusion protein labeled the glomerular capillary wall of mouse kidneys in a staining pattern identical to NEPH1 and nephrin, prompting speculation that that NEPH1 might form homodimers and/or heterodimers with nephrin.
5	12660326	Fusion proteins containing two Ig domains of NEPH1 were sufficient to immobilize NEPH1, but they failed to interact with control protein containing the phylogenetically related PKD repeats of polycystin-1.
6	12660326	NEPH1 also precipitated nephrin, a protein with eight Ig domains and a fibronectin-like domain.
7	12660326	Truncational analysis of nephrin revealed a very similar mode of interaction, i.e., two nephrin Ig domains fused to human IgG precipitated either nephrin or NEPH1, but not the control protein.
8	12660326	Both NEPH1 and nephrin interactions were strictly dependent upon posttranslational glycosylation, and bacterially expressed protein failed to bind NEPH1.
9	12660326	These findings demonstrate that the Ig domains of NEPH1 and nephrin form promiscuous homodimeric and heterodimeric interactions that may facilitate cis- and trans- homodimerizations and heterodimerizations of these molecules at the glomerular slit diaphragm.
10	20150535	Whereas the total absence of laminin alpha5 results in breakdown of the glomerular basement membrane (GBM) and failed glomerular vascularization, a hypomorphic Lama5 mutation (the Lama5(neo) allele) results in proteinuria, hematuria, polycystic kidney disease (PKD), and death 3 to 4 weeks after birth.
11	20150535	Podocyte-specific restoration of laminin alpha5 production using two distinct strategies in Lama5(neo/neo) mice resulted in the resolution of proteinuria, hematuria, and PKD.
12	20150535	These results suggest that the development of normal GBM structure and function requires podocyte-derived laminin alpha5 during and after glomerulogenesis and present a unique mechanism for the pathogenesis of PKD in these mice.
13	20150535	Whereas the total absence of laminin alpha5 results in breakdown of the glomerular basement membrane (GBM) and failed glomerular vascularization, a hypomorphic Lama5 mutation (the Lama5(neo) allele) results in proteinuria, hematuria, polycystic kidney disease (PKD), and death 3 to 4 weeks after birth.
14	20150535	Podocyte-specific restoration of laminin alpha5 production using two distinct strategies in Lama5(neo/neo) mice resulted in the resolution of proteinuria, hematuria, and PKD.
15	20150535	These results suggest that the development of normal GBM structure and function requires podocyte-derived laminin alpha5 during and after glomerulogenesis and present a unique mechanism for the pathogenesis of PKD in these mice.
16	20150535	Whereas the total absence of laminin alpha5 results in breakdown of the glomerular basement membrane (GBM) and failed glomerular vascularization, a hypomorphic Lama5 mutation (the Lama5(neo) allele) results in proteinuria, hematuria, polycystic kidney disease (PKD), and death 3 to 4 weeks after birth.
17	20150535	Podocyte-specific restoration of laminin alpha5 production using two distinct strategies in Lama5(neo/neo) mice resulted in the resolution of proteinuria, hematuria, and PKD.
18	20150535	These results suggest that the development of normal GBM structure and function requires podocyte-derived laminin alpha5 during and after glomerulogenesis and present a unique mechanism for the pathogenesis of PKD in these mice.
19	21085109	Polycystin 1 regulates mTOR activity through different pathways, and TSC intersects with the primary cilium, a crucial cell organelle in the pathogenesis of PKD.
20	26039630	The SAM domain of ANKS6 has different interacting partners and mutations can induce different cystic phenotypes.
21	26039630	The ankyrin repeat and sterile α motif (SAM) domain-containing six gene (Anks6) is a candidate for polycystic kidney disease (PKD).
22	26039630	Originally identified in the PKD/Mhm(cy/+) rat model of PKD, the disease is caused by a mutation (R823W) in the SAM domain of the encoded protein.
23	26039630	Recent studies support the etiological role of the ANKS6 SAM domain in human cystic diseases, but its function in kidney remains unknown.
24	26039630	To investigate the role of ANKS6 in cyst formation, we screened an archive of N-ethyl-N-nitrosourea-treated mice and derived a strain carrying a missense mutation (I747N) within the SAM domain of ANKS6.
25	26039630	Evidence of renal cysts in these mice confirmed the crucial role of the SAM domain of ANKS6 in kidney function.
26	26039630	Comparative phenotype analysis in cy/+ rats and our Anks6(I747N) mice further showed that the two models display noticeably different PKD phenotypes and that there is a defective interaction between ANKS6 with ANKS3 in the rat and between ANKS6 and BICC1 (bicaudal C homolog 1) in the mouse.
27	26039630	Thus, our data demonstrate the importance of ANKS6 for kidney structure integrity and the essential mediating role of its SAM domain in the formation of protein complexes.
28	26039630	The SAM domain of ANKS6 has different interacting partners and mutations can induce different cystic phenotypes.
29	26039630	The ankyrin repeat and sterile α motif (SAM) domain-containing six gene (Anks6) is a candidate for polycystic kidney disease (PKD).
30	26039630	Originally identified in the PKD/Mhm(cy/+) rat model of PKD, the disease is caused by a mutation (R823W) in the SAM domain of the encoded protein.
31	26039630	Recent studies support the etiological role of the ANKS6 SAM domain in human cystic diseases, but its function in kidney remains unknown.
32	26039630	To investigate the role of ANKS6 in cyst formation, we screened an archive of N-ethyl-N-nitrosourea-treated mice and derived a strain carrying a missense mutation (I747N) within the SAM domain of ANKS6.
33	26039630	Evidence of renal cysts in these mice confirmed the crucial role of the SAM domain of ANKS6 in kidney function.
34	26039630	Comparative phenotype analysis in cy/+ rats and our Anks6(I747N) mice further showed that the two models display noticeably different PKD phenotypes and that there is a defective interaction between ANKS6 with ANKS3 in the rat and between ANKS6 and BICC1 (bicaudal C homolog 1) in the mouse.
35	26039630	Thus, our data demonstrate the importance of ANKS6 for kidney structure integrity and the essential mediating role of its SAM domain in the formation of protein complexes.
36	26039630	The SAM domain of ANKS6 has different interacting partners and mutations can induce different cystic phenotypes.
37	26039630	The ankyrin repeat and sterile α motif (SAM) domain-containing six gene (Anks6) is a candidate for polycystic kidney disease (PKD).
38	26039630	Originally identified in the PKD/Mhm(cy/+) rat model of PKD, the disease is caused by a mutation (R823W) in the SAM domain of the encoded protein.
39	26039630	Recent studies support the etiological role of the ANKS6 SAM domain in human cystic diseases, but its function in kidney remains unknown.
40	26039630	To investigate the role of ANKS6 in cyst formation, we screened an archive of N-ethyl-N-nitrosourea-treated mice and derived a strain carrying a missense mutation (I747N) within the SAM domain of ANKS6.
41	26039630	Evidence of renal cysts in these mice confirmed the crucial role of the SAM domain of ANKS6 in kidney function.
42	26039630	Comparative phenotype analysis in cy/+ rats and our Anks6(I747N) mice further showed that the two models display noticeably different PKD phenotypes and that there is a defective interaction between ANKS6 with ANKS3 in the rat and between ANKS6 and BICC1 (bicaudal C homolog 1) in the mouse.
43	26039630	Thus, our data demonstrate the importance of ANKS6 for kidney structure integrity and the essential mediating role of its SAM domain in the formation of protein complexes.
44	30968998	Vasodilator-stimulated phosphoprotein (VASP) is a 39-kDa protein belonging to the Ena/VASP protein family, which is involved in adhesion, migration, cell-cell interaction, and regulation of pathways connected with actin cytoskeleton remodeling.
45	30968998	VASP is phosphorylated at Tyr39, Ser157, Ser239, Thr278, and Ser322 mainly by tyrosine kinase Abl, cAMP-dependent protein kinase, protein kinase G, AMP-activated protein kinase, and protein kinase D1, respectively.