Activation of protein kinase C results in the displacement of its myristoylated, alanine-rich substrate from punctate structures in macrophage filopodia

Antony Rosen, Karen F. Keenan, Marcus Thelen, Angus C. Nairn, Alan Aderem

Research output: Contribution to journalArticlepeer-review

Abstract

The myristoylated, alanine-rich C kinase substrate (MARCKS) is a prominent substrate for protein kinase C (PKC) in a variety of cells, and has been implicated in diverse cellular processes including neurosecretion, fibroblast mitogenesis, and macrophage activation. In macrophages that have spread on the substratum, MARCKS has a punctate distribution at the cell-substratum interface of pseudopodia and filopodia. At these points, MARCKS co-localizes with vinculin and talin. Activation of PKC with phorbol esters results in the rapid disappearance of punctate staining of MARCKS, but not vinculin or talin, and is accompanied by cell spreading and loss of filopodia. The morphological changes and disappearance of punctate staining follow a time-course that closely approximates both the PKC-dependent phosphorylation of MARCKS, and its phos-phorylation-dependent release from the plasma membrane. Our results suggest a role for PKC-dependent phosphorylation of MARCKS in the regulation of the membrane cytoskeleton.

Original languageEnglish (US)
Pages (from-to)1211-1215
Number of pages5
JournalJournal of Experimental Medicine
Volume172
Issue number4
DOIs
StatePublished - Oct 1 1990
Externally publishedYes

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology

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