Biology:Protein kinase N1

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Short description: Protein-coding gene in the species Homo sapiens


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
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:


References

  1. "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. 2.0 2.1 "Entrez Gene: PKN1 protein kinase N1". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5585. 
  3. "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. 
  4. "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. 
  5. "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. Bibcode2005Natur.437.1173R. 
  6. "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. 
  7. "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. 
  8. "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. 
  9. "PKN regulates phospholipase D1 through direct interaction". J. Biol. Chem. 276 (21): 18096–101. May 2001. doi:10.1074/jbc.M010646200. PMID 11259428. 
  10. "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. 
  11. "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. 
  12. "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. 
  13. "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. 
  14. "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