Membrane association of the myristoylated alanine-rich C kinase substrate (MARCKS) protein appears to involve myristate-dependent binding in the absence of a myristoyl protein receptor

The myristoylated alanine-rich C kinase substrate, or MARCKS protein, has been implicated in several cellular processes, yet its physiological function remains unknown. We have studied the molecular basis of its membrane association in a cell-free system in order to help elucidate its regulation and...

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Bibliographic Details
Published in:The Journal of biological chemistry 1992-01, Vol.267 (5), p.24879-24885
Main Authors: George, D J, Blackshear, P J
Format: Article
Language:English
Subjects:
fibroblasts
MARCKS protein
mechanisms
mice
myristolated alanine-rich C kinase substrate
myristoylation
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Summary:The myristoylated alanine-rich C kinase substrate, or MARCKS protein, has been implicated in several cellular processes, yet its physiological function remains unknown. We have studied the molecular basis of its membrane association in a cell-free system in order to help elucidate its regulation and function. We conclude that, at least in this in vitro system, the membrane association of the MARCKS protein is primarily dependent on the amino-terminal myristate moiety and does no appear to involve a specific cytoplasmic-face protein receptor.
ISSN:0021-9258