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Open Access Articles- Top Results for Protein kinase N1

Protein kinase N1

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Identifiers
SymbolsPKN1 ; DBK; PAK-1; PAK1; PKN; PKN-ALPHA; PRK1; PRKCL1
External IDsOMIM601032 MGI108022 HomoloGene48130 IUPHAR: 1520 ChEMBL: 3384 GeneCards: PKN1 Gene
EC number2.7.11.13
RNA expression pattern
File:PBB GE PKN1 202161 at tn.png
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez5585320795
EnsemblENSG00000123143ENSMUSG00000057672
UniProtQ16512P70268
RefSeq (mRNA)NM_002741NM_001199593
RefSeq (protein)NP_002732NP_001186522
Location (UCSC)Chr 19:
14.54 – 14.58 Mb
Chr 8:
83.67 – 83.7 Mb
PubMed search[1][2]

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. ^ Bartsch JW, Mukai H, Takahashi N, Ronsiek M, Fuchs S, Jockusch H et al. (June 1998). "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. PMID 9570957. doi:10.1006/geno.1997.5208. 
  2. ^ a b "Entrez Gene: PKN1 protein kinase N1". 
  3. ^ Takahashi M, Shibata H, Shimakawa M, Miyamoto M, Mukai H, Ono Y (June 1999). "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. PMID 10358086. doi:10.1074/jbc.274.24.17267. 
  4. ^ Feng S, Reséndiz JC, Christodoulides N, Lu X, Arboleda D, Berndt MC et al. (January 2002). "Pathological shear stress stimulates the tyrosine phosphorylation of alpha-actinin associated with the glycoprotein Ib-IX complex". Biochemistry 41 (4): 1100–8. PMID 11802708. doi:10.1021/bi0156005. 
  5. ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N et al. (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature 437 (7062): 1173–8. PMID 16189514. doi:10.1038/nature04209. 
  6. ^ Mukai H, Toshimori M, Shibata H, Kitagawa M, Shimakawa M, Miyahara M et al. (April 1996). "PKN associates and phosphorylates the head-rod domain of neurofilament protein". J. Biol. Chem. 271 (16): 9816–22. PMID 8621664. doi:10.1074/jbc.271.16.9816. 
  7. ^ Shibata H, Oda H, Mukai H, Oishi K, Misaki K, Ohkubo H et al. (December 1999). "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. PMID 10640683. doi:10.1016/s0169-328x(99)00273-9. 
  8. ^ Balendran A, Biondi RM, Cheung PC, Casamayor A, Deak M, Alessi DR (July 2000). "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. PMID 10764742. doi:10.1074/jbc.M000421200. 
  9. ^ Oishi K, Takahashi M, Mukai H, Banno Y, Nakashima S, Kanaho Y et al. (May 2001). "PKN regulates phospholipase D1 through direct interaction". J. Biol. Chem. 276 (21): 18096–101. PMID 11259428. doi:10.1074/jbc.M010646200. 
  10. ^ Riento K, Guasch RM, Garg R, Jin B, Ridley AJ (June 2003). "RhoE binds to ROCK I and inhibits downstream signaling". Mol. Cell. Biol. 23 (12): 4219–29. PMC 156133. PMID 12773565. doi:10.1128/mcb.23.12.4219-4229.2003. 
  11. ^ Alberts AS, Bouquin N, Johnston LH, Treisman R (April 1998). "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. PMID 9535835. doi:10.1074/jbc.273.15.8616. 
  12. ^ Flynn P, Mellor H, Palmer R, Panayotou G, Parker PJ (January 1998). "Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif". J. Biol. Chem. 273 (5): 2698–705. PMID 9446575. doi:10.1074/jbc.273.5.2698. 
  13. ^ Matsuzawa K, Kosako H, Inagaki N, Shibata H, Mukai H, Ono Y et al. (May 1997). "Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN". Biochem. Biophys. Res. Commun. 234 (3): 621–5. PMID 9175763. doi:10.1006/bbrc.1997.6669. 

Further reading

  • Palmer RH, Ridden J, Parker PJ (1995). "Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family". Eur. J. Biochem. 227 (1-2): 344–51. PMID 7851406. doi:10.1111/j.1432-1033.1995.tb20395.x. 
  • Chu W, Presky DH, Danho W, Swerlick RA, Burns DK (1994). "Identification and characterization of DBK, a novel putative serine/threonine protein kinase from human endothelial cells". Eur. J. Biochem. 225 (2): 695–702. PMID 7957185. doi:10.1111/j.1432-1033.1994.00695.x. 
  • Palmer RH, Ridden J, Parker PJ (1994). "Identification of multiple, novel, protein kinase C-related gene products". FEBS Lett. 356 (1): 5–8. PMID 7988719. doi:10.1016/0014-5793(94)01202-4. 
  • Mukai H, Ono Y (1994). "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. PMID 8135837. doi:10.1006/bbrc.1994.1313. 
  • Palmer RH, Schönwasser DC, Rahman D, Pappin DJ, Herget T, Parker PJ (1996). "PRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163". FEBS Lett. 378 (3): 281–5. PMID 8557118. doi:10.1016/0014-5793(95)01454-3. 
  • Amano M, Mukai H, Ono Y, Chihara K, Matsui T, Hamajima Y et al. (1996). "Identification of a putative target for Rho as the serine-threonine kinase protein kinase N". Science 271 (5249): 648–50. PMID 8571127. doi:10.1126/science.271.5249.648. 
  • Mukai H, Toshimori M, Shibata H, Kitagawa M, Shimakawa M, Miyahara M et al. (1996). "PKN associates and phosphorylates the head-rod domain of neurofilament protein". J. Biol. Chem. 271 (16): 9816–22. PMID 8621664. doi:10.1074/jbc.271.16.9816. 
  • Brown JL, Stowers L, Baer M, Trejo J, Coughlin S, Chant J (1996). "Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway". Curr. Biol. 6 (5): 598–605. PMID 8805275. doi:10.1016/S0960-9822(02)00546-8. 
  • Mukai H, Miyahara M, Sunakawa H, Shibata H, Toshimori M, Kitagawa M et al. (1996). "Translocation of PKN from the cytosol to the nucleus induced by stresses". Proc. Natl. Acad. Sci. U.S.A. 93 (19): 10195–9. PMC 38360. PMID 8816775. doi:10.1073/pnas.93.19.10195. 
  • Mukai H, Toshimori M, Shibata H, Takanaga H, Kitagawa M, Miyahara M et al. (1997). "Interaction of PKN with alpha-actinin". J. Biol. Chem. 272 (8): 4740–6. PMID 9030526. doi:10.1074/jbc.272.8.4740. 
  • Matsuzawa K, Kosako H, Inagaki N, Shibata H, Mukai H, Ono Y et al. (1997). "Domain-specific phosphorylation of vimentin and glial fibrillary acidic protein by PKN". Biochem. Biophys. Res. Commun. 234 (3): 621–5. PMID 9175763. doi:10.1006/bbrc.1997.6669. 
  • Goedert M, Hasegawa M, Jakes R, Lawler S, Cuenda A, Cohen P (1997). "Phosphorylation of microtubule-associated protein tau by stress-activated protein kinases". FEBS Lett. 409 (1): 57–62. PMID 9199504. doi:10.1016/S0014-5793(97)00483-3. 
  • Flynn P, Mellor H, Palmer R, Panayotou G, Parker PJ (1998). "Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif". J. Biol. Chem. 273 (5): 2698–705. PMID 9446575. doi:10.1074/jbc.273.5.2698. 
  • Bekri S, Adélaïde J, Merscher S, Grosgeorge J, Caroli-Bosc F, Perucca-Lostanlen D et al. (1997). "Detailed map of a region commonly amplified at 11q13-->q14 in human breast carcinoma". Cytogenet. Cell Genet. 79 (1-2): 125–31. PMID 9533029. doi:10.1159/000134699. 
  • Zheng-Fischhöfer Q, Biernat J, Mandelkow EM, Illenberger S, Godemann R, Mandelkow E (1998). "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. PMID 9546672. doi:10.1046/j.1432-1327.1998.2520542.x. 
  • Takanaga H, Mukai H, Shibata H, Toshimori M, Ono Y (1998). "PKN interacts with a paraneoplastic cerebellar degeneration-associated antigen, which is a potential transcription factor". Exp. Cell Res. 241 (2): 363–72. PMID 9637778. doi:10.1006/excr.1998.4060. 
  • Takahashi M, Mukai H, Toshimori M, Miyamoto M, Ono Y (1998). "Proteolytic activation of PKN by caspase-3 or related protease during apoptosis". Proc. Natl. Acad. Sci. U.S.A. 95 (20): 11566–71. PMC 21681. PMID 9751706. doi:10.1073/pnas.95.20.11566. 
  • Hanger DP, Betts JC, Loviny TL, Blackstock WP, Anderton BH (1998). "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. PMID 9832145. doi:10.1046/j.1471-4159.1998.71062465.x. 
  • Takahashi M, Shibata H, Shimakawa M, Miyamoto M, Mukai H, Ono Y (1999). "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. PMID 10358086. doi:10.1074/jbc.274.24.17267. 
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