Regulation by phosphorylation of reversible association of a myristoylated protein kinase C substrate with the plasma membrane View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-05

AUTHORS

Marcus Thelen, Antony Rosen, Angus C. Nairn, Alan Aderem

ABSTRACT

PROTEIN kinase C (PKC) transduces receptor-mediated signals by phosphorylating membrane-bound substrates which then act as effectors of specific cellular responses1. The myristoylated alanine-rich C kinase substrate (MARCKS) is a specific PKC substrate which has been implicated in macrophage activation, neurosecretion and growth factor-dependent mitogenesis2–5. Myristoylation of MARCKS is required for effective binding to the plasma membrane6 where it colocalizes with PKC7. Here we report that PKC-dependent phosphorylation displaces MARCKS from the membrane and that its subsequent dephosphorylation is accompanied by its reassociation with the membrane. This cycle of phosphorylation-dependent membrane attachment and detachment of a myristoylated protein represents a novel mechanism of reversible membrane targeting. As MARCKS is a calmodulin- and actin-binding protein (ref. 8, and J. Hartwig et al., manuscript submitted), the cycle of membrane attachment/detachment represents a mechanism through which PKC might reversibly regulate actin–membrane interaction. More... »

PAGES

320-322

Journal

TITLE

Nature

ISSUE

6324

VOLUME

351

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/351320a0

DOI

http://dx.doi.org/10.1038/351320a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1028226670

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/2034276


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