PKN2
From Wikipedia, the free encyclopedia
Serine/threonine-protein kinase N2 is an enzyme that in humans is encoded by the PKN2 gene.[1][2][3]
Interactions
PKN2 has been shown to interact with Phosphoinositide-dependent kinase-1,[4][5] AKT1,[6] NCK1,[7][8] PTPN13[9] and RHOA.[7][10]
References
- ↑ Palmer RH, Ridden J, Parker PJ (January 1995). "Identification of multiple, novel, protein kinase C-related gene products". FEBS Lett 356 (1): 5–8. doi:10.1016/0014-5793(94)01202-4. PMID 7988719.
- ↑ Palmer RH, Ridden J, Parker PJ (March 1995). "Cloning and expression patterns of two members of a novel protein-kinase-C-related kinase family". Eur J Biochem 227 (1–2): 344–351. doi:10.1111/j.1432-1033.1995.tb20395.x. PMID 7851406.
- ↑ "Entrez Gene: PKN2 protein kinase N2".
- ↑ Hodgkinson, Conrad P; Sale Graham J (January 2002). "Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment". Biochemistry (United States) 41 (2): 561–569. doi:10.1021/bi010719z. ISSN 0006-2960. PMID 11781095.
- ↑ Balendran, A; Biondi R M, Cheung P C, Casamayor A, Deak M, Alessi D R (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. (UNITED STATES) 275 (27): 20806–20813. doi:10.1074/jbc.M000421200. ISSN 0021-9258. PMID 10764742.
- ↑ Koh, H; Lee K H, Kim D, Kim S, Kim J W, Chung J (November 2000). "Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage". J. Biol. Chem. (UNITED STATES) 275 (44): 34451–34458. doi:10.1074/jbc.M001753200. ISSN 0021-9258. PMID 10926925.
- ↑ 7.0 7.1 Quilliam, L A; Lambert Q T, Mickelson-Young L A, Westwick J K, Sparks A B, Kay B K, Jenkins N A, Gilbert D J, Copeland N G, Der C J (November 1996). "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling". J. Biol. Chem. (UNITED STATES) 271 (46): 28772–28776. doi:10.1074/jbc.271.46.28772. ISSN 0021-9258. PMID 8910519.
- ↑ Braverman, L E; Quilliam L A (February 1999). "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck". J. Biol. Chem. (UNITED STATES) 274 (9): 5542–5549. doi:10.1074/jbc.274.9.5542. ISSN 0021-9258. PMID 10026169.
- ↑ Gross, C; Heumann R, Erdmann K S (May 2001). "The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif". FEBS Lett. (Netherlands) 496 (2–3): 101–104. doi:10.1016/S0014-5793(01)02401-2. ISSN 0014-5793. PMID 11356191.
- ↑ Flynn, P; Mellor H, Palmer R, Panayotou G, Parker P J (January 1998). "Multiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motif". J. Biol. Chem. (UNITED STATES) 273 (5): 2698–2705. doi:10.1074/jbc.273.5.2698. ISSN 0021-9258. PMID 9446575.
Further reading
- Quilliam LA, Lambert QT, Mickelson-Young LA et al. (1997). "Isolation of a NCK-associated kinase, PRK2, an SH3-binding protein and potential effector of Rho protein signaling". J. Biol. Chem. 271 (46): 28772–28776. doi:10.1074/jbc.271.46.28772. PMID 8910519.
- Yu W, Liu J, Morrice NA, Wettenhall RE (1997). "Isolation and characterization of a structural homologue of human PRK2 from rat liver. Distinguishing substrate and lipid activator specificities". J. Biol. Chem. 272 (15): 10030–10034. doi:10.1074/jbc.272.15.10030. PMID 9092545.
- Vincent S, Settleman J (1997). "The PRK2 kinase is a potential effector target of both Rho and Rac GTPases and regulates actin cytoskeletal organization". Mol. Cell. Biol. 17 (4): 2247–56. PMC 232074. PMID 9121475.
- Cryns VL, Byun Y, Rana A et al. (1997). "Specific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategy". J. Biol. Chem. 272 (47): 29449–29453. doi:10.1074/jbc.272.47.29449. PMID 9368003.
- Braverman LE, Quilliam LA (1999). "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck". J. Biol. Chem. 274 (9): 5542–5549. doi:10.1074/jbc.274.9.5542. PMID 10026169.
- Flynn P, Mellor H, Casamassima A, Parker PJ (2000). "Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinase". J. Biol. Chem. 275 (15): 11064–11070. doi:10.1074/jbc.275.15.11064. PMID 10753910.
- Sun W, Vincent S, Settleman J, Johnson GL (2000). "MEK kinase 2 binds and activates protein kinase C-related kinase 2. Bifurcation of kinase regulatory pathways at the level of an MAPK kinase kinase". J. Biol. Chem. 275 (32): 24421–24428. doi:10.1074/jbc.M003148200. PMID 10818102.
- Koh H, Lee KH, Kim D et al. (2000). "Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage". J. Biol. Chem. 275 (44): 34451–34458. doi:10.1074/jbc.M001753200. PMID 10926925.
- Gross C, Heumann R, Erdmann KS (2001). "The protein kinase C-related kinase PRK2 interacts with the protein tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif". FEBS Lett. 496 (2–3): 101–104. doi:10.1016/S0014-5793(01)02401-2. PMID 11356191.
- Hodgkinson CP, Sale GJ (2002). "Regulation of both PDK1 and the phosphorylation of PKC-zeta and -delta by a C-terminal PRK2 fragment". Biochemistry 41 (2): 561–569. doi:10.1021/bi010719z. PMID 11781095.
- Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–16903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- McDonald C, Vacratsis PO, Bliska JB, Dixon JE (2003). "The yersinia virulence factor YopM forms a novel protein complex with two cellular kinases". J. Biol. Chem. 278 (20): 18514–18523. doi:10.1074/jbc.M301226200. PMID 12626518.
- Anderson NL, Polanski M, Pieper R et al. (2004). "The human plasma proteome: a nonredundant list developed by combination of four separate sources". Mol. Cell Proteomics 3 (4): 311–326. doi:10.1074/mcp.M300127-MCP200. PMID 14718574.
- Beausoleil SA, Jedrychowski M, Schwartz D et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–12135. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
- Yarrow JC, Totsukawa G, Charras GT, Mitchison TJ (2005). "Screening for cell migration inhibitors via automated microscopy reveals a Rho-kinase inhibitor". Chem. Biol. 12 (3): 385–395. doi:10.1016/j.chembiol.2005.01.015. PMID 15797222.
- DeGiorgis JA, Jaffe H, Moreira JE et al. (2005). "Phosphoproteomic analysis of synaptosomes from human cerebral cortex". J. Proteome Res. 4 (2): 306–315. doi:10.1021/pr0498436. PMID 15822905.
- Kimura K, Wakamatsu A, Suzuki Y et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
- Gregory SG, Barlow KF, McLay KE et al. (2006). "The DNA sequence and biological annotation of human chromosome 1". Nature 441 (7091): 315–321. doi:10.1038/nature04727. PMID 16710414.
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