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Nature. 1991 May 23;351(6324):320-2.

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

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Rockefeller University, New York, New York.


Protein kinase C (PKC) transduces receptor-mediated signals by phosphorylating membrane-bound substrates which then act as effectors of specific cellular responses. The myristoylated alanine-rich C kinase substrate (MARCKS) is a specific PKC substrate which has been implicated in macrophage activation, neuro-secretion and growth factor-dependent mitogenesis. Myristoylation of MARCKS is required for effective binding to the plasma membrane where it colocalizes with PKC. 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.

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