From Wikipedia, the free encyclopedia

The Raf kinase inhibitor protein (RKIP) is a kinase inhibitor protein, that regulates many signaling pathways within the cell. [1] RKIP is a member of the phosphatidylethanolamine-binding protein family and has displayed disruptive regulation on the Raf-1- MEK1/2, ERK1/2 and NF-kappaB signalling pathways, by interaction with the Raf-1 kinase. [1]

RKIP has also been shown to inhibit G protein coupled receptor kinases (GRK) when phosphorylated by protein kinase C. [2] Via this mechanism it has been shown to exert beneficial effects on cardiac structure and function. [3]

References

  1. ^ a b Odabaei, Golaun; Chatterjee, Devasis; Jazirehi, Ali R.; Goodglick, Lee; Yeung, Kam; Bonavida, Benjamin (2004). "Raf-1 Kinase Inhibitor Protein: Structure, Function, Regulation of Cell Signaling, and Pivotal Role in Apoptosis". In Vande Woude, George F.; Klein, George (eds.). Advances in Cancer Research. Vol. 91. Elsevier. pp. 169–200. doi: 10.1016/S0065-230X(04)91005-6. ISBN  978-0-12-006691-9. ISSN  0065-230X. PMID  15327891. S2CID  21758249.
  2. ^ Lorenz, Kristina; Lohse, Martin J.; Quitterer, Ursula (4 December 2003). "Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2". Nature. 426 (6966): 574–579. doi: 10.1038/nature02158. ISSN  1476-4687. PMID  14654844. S2CID  4431750. EBSCOhost  11581735.
  3. ^ Schmid, Evelyn; Neef, Stefan; Berlin, Christopher; Tomasovic, Angela; Kahlert, Katrin; Nordbeck, Peter; Deiss, Katharina; Denzinger, Sabrina; Herrmann, Sebastian; Wettwer, Erich; Weidendorfer, Markus; Becker, Daniel; Schäfer, Florian; Wagner, Nicole; Ergün, Süleyman (19 October 2015). "Cardiac RKIP induces a beneficial β-adrenoceptor-dependent positive inotropy". Nature Medicine. 21 (11): 1298–1306. doi: 10.1038/nm.3972. ISSN  1546-170X. PMID  26479924. S2CID  11418537. EBSCOhost  110747403.
From Wikipedia, the free encyclopedia

The Raf kinase inhibitor protein (RKIP) is a kinase inhibitor protein, that regulates many signaling pathways within the cell. [1] RKIP is a member of the phosphatidylethanolamine-binding protein family and has displayed disruptive regulation on the Raf-1- MEK1/2, ERK1/2 and NF-kappaB signalling pathways, by interaction with the Raf-1 kinase. [1]

RKIP has also been shown to inhibit G protein coupled receptor kinases (GRK) when phosphorylated by protein kinase C. [2] Via this mechanism it has been shown to exert beneficial effects on cardiac structure and function. [3]

References

  1. ^ a b Odabaei, Golaun; Chatterjee, Devasis; Jazirehi, Ali R.; Goodglick, Lee; Yeung, Kam; Bonavida, Benjamin (2004). "Raf-1 Kinase Inhibitor Protein: Structure, Function, Regulation of Cell Signaling, and Pivotal Role in Apoptosis". In Vande Woude, George F.; Klein, George (eds.). Advances in Cancer Research. Vol. 91. Elsevier. pp. 169–200. doi: 10.1016/S0065-230X(04)91005-6. ISBN  978-0-12-006691-9. ISSN  0065-230X. PMID  15327891. S2CID  21758249.
  2. ^ Lorenz, Kristina; Lohse, Martin J.; Quitterer, Ursula (4 December 2003). "Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2". Nature. 426 (6966): 574–579. doi: 10.1038/nature02158. ISSN  1476-4687. PMID  14654844. S2CID  4431750. EBSCOhost  11581735.
  3. ^ Schmid, Evelyn; Neef, Stefan; Berlin, Christopher; Tomasovic, Angela; Kahlert, Katrin; Nordbeck, Peter; Deiss, Katharina; Denzinger, Sabrina; Herrmann, Sebastian; Wettwer, Erich; Weidendorfer, Markus; Becker, Daniel; Schäfer, Florian; Wagner, Nicole; Ergün, Süleyman (19 October 2015). "Cardiac RKIP induces a beneficial β-adrenoceptor-dependent positive inotropy". Nature Medicine. 21 (11): 1298–1306. doi: 10.1038/nm.3972. ISSN  1546-170X. PMID  26479924. S2CID  11418537. EBSCOhost  110747403.

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