Protein kinase C autophosphorylates by an intrapeptide reaction
- PMID: 3611058
Protein kinase C autophosphorylates by an intrapeptide reaction
Abstract
The Ca2+-activated, phospholipid-dependent protein kinase C autophosphorylates by an intrapeptide reaction in a mixed micelle system in which the enzyme is a monomer. The rate of autophosphorylation in the micellar system is comparable to that observed in bilayer systems, where the enzyme may exist as an oligomer. Trypsinolysis of the enzyme reveals that both the regulatory and catalytic domains of the molecule are modified by the intrapeptide phosphorylation. Proteolysis of the enzyme to separate the two domains results in loss of ability to autophosphorylate. Furthermore, intact protein kinase C cannot phosphorylate either the cleaved regulatory or catalytic domains. Kinetic and proteolytic analyses suggest that intrapeptide phosphorylation is the predominant, and perhaps only, mechanism by which protein kinase C autophosphorylates. The intrapeptide modification of protein kinase C has intriguing implications for protein structure and regulation.
Similar articles
-
Domain structure and phosphorylation of protein kinase C.J Biol Chem. 1987 Feb 15;262(5):2291-7. J Biol Chem. 1987. PMID: 3818597
-
Autophosphorylation of rat brain Ca2+-activated and phospholipid-dependent protein kinase.J Biol Chem. 1986 Sep 15;261(26):12134-40. J Biol Chem. 1986. PMID: 3462187
-
Autophosphorylation of protein kinase C at three separated regions of its primary sequence.Science. 1990 Jul 27;249(4967):408-11. doi: 10.1126/science.2377895. Science. 1990. PMID: 2377895
-
Protease-activated protein kinase C in rat liver.Int J Biochem. 1991;23(5-6):507-12. Int J Biochem. 1991. PMID: 2065812 Review.
-
A historical overview of protein kinases and their _targeted small molecule inhibitors.Pharmacol Res. 2015 Oct;100:1-23. doi: 10.1016/j.phrs.2015.07.010. Epub 2015 Jul 21. Pharmacol Res. 2015. PMID: 26207888 Review.
Cited by
-
mTORC2 controls the activity of PKC and Akt by phosphorylating a conserved TOR interaction motif.Sci Signal. 2021 Apr 13;14(678):eabe4509. doi: 10.1126/scisignal.abe4509. Sci Signal. 2021. PMID: 33850054 Free PMC article.
-
Regulatory autophosphorylation sites on protein kinase C-delta at threonine-141 and threonine-295.Biochemistry. 2009 Jun 2;48(21):4642-51. doi: 10.1021/bi802171c. Biochemistry. 2009. PMID: 19366211 Free PMC article.
-
Atrial natriuretic factor inhibits autophosphorylation of protein kinase C and A 240-kDa protein in plasma membranes of bovine adrenal glomerulosa cells: involvement of cGMP-dependent and independent signal transduction mechanisms.Mol Cell Biochem. 1994 Dec 21;141(2):103-11. doi: 10.1007/BF00926173. Mol Cell Biochem. 1994. PMID: 7891667
-
Automethylation of protein (D-aspartyl/L-isoaspartyl) carboxyl methyltransferase, a response to enzyme aging.J Protein Chem. 1994 Jan;13(1):23-30. doi: 10.1007/BF01891989. J Protein Chem. 1994. PMID: 8011068
-
PAK1 and aPKCzeta regulate myosin II-B phosphorylation: a novel signaling pathway regulating filament assembly.Mol Biol Cell. 2006 Jul;17(7):2869-81. doi: 10.1091/mbc.e05-11-1001. Epub 2006 Apr 12. Mol Biol Cell. 2006. PMID: 16611744 Free PMC article.
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Miscellaneous
