Biology:Protein kinase N1
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Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
Serine/threonine-protein kinase N1 is an enzyme that in humans is encoded by the PKN1 gene.[1][2]
Function
The protein encoded by this gene belongs to the protein kinase C superfamily. This kinase is activated by Rho family of small G proteins and may mediate the Rho-dependent signaling pathway. This kinase can be activated by phospholipids and by limited proteolysis. The 3-phosphoinositide dependent protein kinase-1 (PDPK1/PDK1) is reported to phosphorylate this kinase, which may mediate insulin signals to the actin cytoskeleton. The proteolytic activation of this kinase by caspase-3 or related proteases during apoptosis suggests its role in signal transduction related to apoptosis. Alternatively spliced transcript variants encoding distinct isoforms have been observed.[2]
Interactions
Protein kinase N1 has been shown to interact with:
- AKAP9,[3]
- Actinin, alpha 1,[4]
- CCDC85B,[5]
- NEFL,[6]
- NEUROD2[7]
- Phosphoinositide-dependent kinase-1,[8]
- Phospholipase D1,[9]
- RHOA,[10][11][12] and
- Vimentin.[13]
- TRAF1.[14]
References
- ↑ "The protein kinase N (PKN) gene PRKCL1/Prkcl1 maps to human chromosome 19p12-p13.1 and mouse chromosome 8 with close linkage to the myodystrophy (myd) mutation". Genomics 49 (1): 129–32. June 1998. doi:10.1006/geno.1997.5208. PMID 9570957.
- ↑ 2.0 2.1 "Entrez Gene: PKN1 protein kinase N1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5585.
- ↑ "Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the golgi apparatus". J. Biol. Chem. 274 (24): 17267–74. June 1999. doi:10.1074/jbc.274.24.17267. PMID 10358086.
- ↑ "Pathological shear stress stimulates the tyrosine phosphorylation of alpha-actinin associated with the glycoprotein Ib-IX complex". Biochemistry 41 (4): 1100–8. January 2002. doi:10.1021/bi0156005. PMID 11802708.
- ↑ "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. October 2005. doi:10.1038/nature04209. PMID 16189514. Bibcode: 2005Natur.437.1173R.
- ↑ "PKN associates and phosphorylates the head-rod domain of neurofilament protein". J. Biol. Chem. 271 (16): 9816–22. April 1996. doi:10.1074/jbc.271.16.9816. PMID 8621664.
- ↑ "Interaction of PKN with a neuron-specific basic helix-loop-helix transcription factor, NDRF/NeuroD2". Brain Res. Mol. Brain Res. 74 (1–2): 126–34. December 1999. doi:10.1016/s0169-328x(99)00273-9. PMID 10640683.
- ↑ "A 3-phosphoinositide-dependent protein kinase-1 (PDK1) docking site is required for the phosphorylation of protein kinase Czeta (PKCzeta ) and PKC-related kinase 2 by PDK1". J. Biol. Chem. 275 (27): 20806–13. July 2000. doi:10.1074/jbc.M000421200. PMID 10764742.
- ↑ "PKN regulates phospholipase D1 through direct interaction". J. Biol. Chem. 276 (21): 18096–101. May 2001. doi:10.1074/jbc.M010646200. PMID 11259428.
- ↑ "RhoE binds to ROCK I and inhibits downstream signaling". Mol. Cell. Biol. 23 (12): 4219–29. June 2003. doi:10.1128/mcb.23.12.4219-4229.2003. PMID 12773565.
- ↑ "Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7". J. Biol. Chem. 273 (15): 8616–22. April 1998. doi:10.1074/jbc.273.15.8616. PMID 9535835.
- ↑ "Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif". J. Biol. Chem. 273 (5): 2698–705. January 1998. doi:10.1074/jbc.273.5.2698. PMID 9446575.
- ↑ "Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN". Biochem. Biophys. Res. Commun. 234 (3): 621–5. May 1997. doi:10.1006/bbrc.1997.6669. PMID 9175763.
- ↑ "Negative regulation of constitutive NF-kappaB and JNK signaling by PKN1-mediated phosphorylation of TRAF1". Genes Cells 13 (5): 509–20. May 2008. doi:10.1111/j.1365-2443.2008.01182.x. PMID 18429822.
Further reading
- "Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family". Eur. J. Biochem. 227 (1–2): 344–51. 1995. doi:10.1111/j.1432-1033.1995.tb20395.x. PMID 7851406.
- "Identification and characterization of DBK, a novel putative serine/threonine protein kinase from human endothelial cells". Eur. J. Biochem. 225 (2): 695–702. 1994. doi:10.1111/j.1432-1033.1994.00695.x. PMID 7957185.
- "Identification of multiple, novel, protein kinase C-related gene products". FEBS Lett. 356 (1): 5–8. 1994. doi:10.1016/0014-5793(94)01202-4. PMID 7988719.
- "A novel protein kinase with leucine zipper-like sequences: its catalytic domain is highly homologous to that of protein kinase C". Biochem. Biophys. Res. Commun. 199 (2): 897–904. 1994. doi:10.1006/bbrc.1994.1313. PMID 8135837.
- "PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163". FEBS Lett. 378 (3): 281–5. 1996. doi:10.1016/0014-5793(95)01454-3. PMID 8557118.
- "Identification of a putative target for Rho as the serine-threonine kinase protein kinase N". Science 271 (5249): 648–50. 1996. doi:10.1126/science.271.5249.648. PMID 8571127. Bibcode: 1996Sci...271..648A.
- "PKN associates and phosphorylates the head-rod domain of neurofilament protein". J. Biol. Chem. 271 (16): 9816–22. 1996. doi:10.1074/jbc.271.16.9816. PMID 8621664.
- "Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway". Curr. Biol. 6 (5): 598–605. 1996. doi:10.1016/S0960-9822(02)00546-8. PMID 8805275.
- "Translocation of PKN from the cytosol to the nucleus induced by stresses". Proc. Natl. Acad. Sci. U.S.A. 93 (19): 10195–9. 1996. doi:10.1073/pnas.93.19.10195. PMID 8816775. Bibcode: 1996PNAS...9310195M.
- "Interaction of PKN with alpha-actinin". J. Biol. Chem. 272 (8): 4740–6. 1997. doi:10.1074/jbc.272.8.4740. PMID 9030526.
- "Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN". Biochem. Biophys. Res. Commun. 234 (3): 621–5. 1997. doi:10.1006/bbrc.1997.6669. PMID 9175763.
- "Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases". FEBS Lett. 409 (1): 57–62. 1997. doi:10.1016/S0014-5793(97)00483-3. PMID 9199504.
- "Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif". J. Biol. Chem. 273 (5): 2698–705. 1998. doi:10.1074/jbc.273.5.2698. PMID 9446575.
- "Detailed map of a region commonly amplified at 11q13-->q14 in human breast carcinoma". Cytogenet. Cell Genet. 79 (1–2): 125–31. 1997. doi:10.1159/000134699. PMID 9533029.
- "Sequential phosphorylation of Tau by glycogen synthase kinase-3beta and protein kinase A at Thr212 and Ser214 generates the Alzheimer-specific epitope of antibody AT100 and requires a paired-helical-filament-like conformation". Eur. J. Biochem. 252 (3): 542–52. 1998. doi:10.1046/j.1432-1327.1998.2520542.x. PMID 9546672.
- "PKN interacts with a paraneoplastic cerebellar degeneration-associated antigen, which is a potential transcription factor". Exp. Cell Res. 241 (2): 363–72. 1998. doi:10.1006/excr.1998.4060. PMID 9637778.
- "Proteolytic activation of PKN by caspase-3 or related protease during apoptosis". Proc. Natl. Acad. Sci. U.S.A. 95 (20): 11566–71. 1998. doi:10.1073/pnas.95.20.11566. PMID 9751706. Bibcode: 1998PNAS...9511566T.
- "New phosphorylation sites identified in hyperphosphorylated tau (paired helical filament-tau) from Alzheimer's disease brain using nanoelectrospray mass spectrometry". J. Neurochem. 71 (6): 2465–76. 1998. doi:10.1046/j.1471-4159.1998.71062465.x. PMID 9832145.
- "Characterization of a novel giant scaffolding protein, CG-NAP, that anchors multiple signaling enzymes to centrosome and the golgi apparatus". J. Biol. Chem. 274 (24): 17267–74. 1999. doi:10.1074/jbc.274.24.17267. PMID 10358086.
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