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Mutation of the hydrophobic motif in a phosphorylation-deficient mutant renders protein kinase C delta more apoptotically active.
- Source :
-
Archives of biochemistry and biophysics [Arch Biochem Biophys] 2010 Jan 15; Vol. 493 (2), pp. 242-8. Date of Electronic Publication: 2009 Nov 13. - Publication Year :
- 2010
-
Abstract
- Protein kinase C delta (PKCdelta) is one of the important isoforms of PKCs that regulate various cellular processes, including cell survival and apoptosis. Studies have shown that activation of PKCdelta is correlated with apoptosis in various cell types, depending upon various stimuli. Phosphorylation of Thr505, Ser643 and Ser662 is crucial in activation of PKCdelta. Furthermore, phosphorylation of tyrosine residues, in particular that of Tyr311, is associated with PKCdelta activation and induction of apoptosis. Here, we generated a hydrophobic motif phosphorylation-deficient mutant of PKCdelta (PKCdelta-S662A) by mutating Ser662 to Ala, and studied the effect of this mutation in inducing apoptosis in L929 murine fibroblasts. We report that this mutation renders PKCdelta apoptotically more active. Furthermore, we found that the mutant PKCdelta-S662A is tyrosine-phosphorylated and translocated to the membrane faster than its wild-type counterpart.<br /> (Copyright (c) 2009 Elsevier Inc. All rights reserved.)
- Subjects :
- Amino Acid Motifs physiology
Amino Acid Substitution
Animals
Cell Line
Cell Membrane genetics
Enzyme Activation genetics
Fibroblasts cytology
Hydrophobic and Hydrophilic Interactions
Isoenzymes genetics
Isoenzymes metabolism
Mice
Phosphorylation genetics
Protein Kinase C-delta genetics
Protein Transport physiology
Apoptosis physiology
Cell Membrane enzymology
Fibroblasts enzymology
Mutation, Missense
Protein Kinase C-delta metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1096-0384
- Volume :
- 493
- Issue :
- 2
- Database :
- MEDLINE
- Journal :
- Archives of biochemistry and biophysics
- Publication Type :
- Academic Journal
- Accession number :
- 19914197
- Full Text :
- https://doi.org/10.1016/j.abb.2009.11.007