Association of diacylglycerol kinase ζ with protein kinase C α

Content Provider	Scilit
Author	Luo, Bai Prescott, Stephen M. Topham, Matthew K.
Copyright Year	2003
Description	Activation of PKC depends on the availability of DAG, a signaling lipid that is tightly and dynamically regulated. DAG kinase (DGK) terminates DAG signaling by converting it to phosphatidic acid. Here, we demonstrate that DGKζ inhibits PKCα activity and that DGK activity is required for this inhibition. We also show that DGKζ directly interacts with PKCα in a signaling complex and that the binding site in DGKζ is located within the catalytic domain. Because PKCα can phosphorylate the myristoylated alanine-rich C-kinase substrate (MARCKS) motif of DGKζ, we tested whether this modification could affect their interaction. Phosphorylation of this motif significantly attenuated coimmunoprecipitation of DGKζ and PKCα and abolished their colocalization in cells, indicating that it negatively regulates binding. Expression of a phosphorylation-mimicking DGKζ mutant that was unable to bind PKCα did not inhibit PKCα activity. Together, our results suggest that DGKζ spatially regulates PKCα activity by attenuating local accumulation of signaling DAG. This regulation is impaired by PKCα-mediated DGKζ phosphorylation.
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2173768/pdf http://jcb.rupress.org/content/160/6/929.full.pdf
Ending Page	937
Page Count	9
Starting Page	929
DOI	10.1083/jcb.200208120
Journal	Journal of Cell Biology
Issue Number	6
Volume Number	160
Language	English
Publisher	Rockefeller University Press
Publisher Date	2003-03-10
Access Restriction	Open
Subject Keyword	Biochemistry and Molecular Biology Cell Biology Membrane Proteins Mutation Signal Transduction Protein Kinase C Protein Binding Phosphorylation Diacylglycerol Kinase Journal: Journal of Cell Biology (Vol- 160, Issue- 6)
Content Type	Text