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Science 27 October 1989:
Vol. 246. no. 4929, pp. 503 - 506
DOI: 10.1126/science.2814478
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Articles

Science, Vol 246, Issue 4929, 503-506
Copyright © 1989 by American Association for the Advancement of Science

articles

Myristoylated and nonmyristoylated forms of a protein are phosphorylated by protein kinase C

JM Graff, JI Gordon, and PJ Blackshear

Howard Hughes Medical Institute Laboratories, Durham, NC 27710.

Activation of protein kinase C is thought to require association of the kinase with the cell membrane. It has been assumed that cellular substrates for the kinase must likewise be associated with membranes, and previous studies with membrane-associated myristoylated proteins have supported this view. It is now shown that a mutation that prevents the normal amino-terminal myristoylation of a prominent cellular substrate of protein kinase C, and appears to prevent its membrane association, does not prevent the normal phosphorylation of this protein in intact cells in response to phorbol esters. Thus, membrane association may not be required in order for protein kinase C substrates to undergo phosphorylation.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Phosphorylation-dependent Conformational Changes Induce a Switch in the Actin-binding Function of MARCKS.
M. R. Bubb, R. H. Lenox, and A. S. Edison (1999)
J. Biol. Chem. 274, 36472-36478
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Myristoylation Does Not Modulate the Properties of MARCKS-related Protein (MRP) in Solution.
E. Schleiff, A. Schmitz, R. A.J. McIlhinney, S. Manenti, and G. Vergeres (1996)
J. Biol. Chem. 271, 26794-26802
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Myristoylation-dependent and Electrostatic Interactions Exert Independent Effects on the Membrane Association of the Myristoylated Alanine-rich Protein Kinase C Substrate Protein in Intact Cells.
S. L. Swierczynski and P. J. Blackshear (1996)
J. Biol. Chem. 271, 23424-23430
   Abstract »    Full Text »    PDF »
Molecular Determinants of the Myristoyl-electrostatic Switch of MARCKS.
J. T. Seykora, M. M. Myat, L.-A. H. Allen, J. V. Ravetch, and A. Aderem (1996)
J. Biol. Chem. 271, 18797-18802
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Protein Kinase C beta II Specifically Binds to and Is Activated by F-actin.
G. C. Blobe, D. S. Stribling, D. Fabbro, S. Stabel, and Y. A. Hannun (1996)
J. Biol. Chem. 271, 15823-15830
   Abstract »    Full Text »    PDF »
The Myristoyl Moiety of Myristoylated Alanine-rich C Kinase Substrate (MARCKS) and MARCKS-related Protein Is Embedded in the Membrane.
G. Vergčres, S.ép. Manenti, T. Weber, and C. Stürzinger (1995)
J. Biol. Chem. 270, 19879-19887
   Abstract »    Full Text »    PDF »
MacMARCKS Mutation Blocks Macrophage Phagocytosis of Zymosan.
Z. Zhu, Z. Bao, and J. Li (1995)
J. Biol. Chem. 270, 17652-17655
   Abstract »    Full Text »    PDF »
Membrane Association of the Myristoylated Alanine-rich C Kinase Substrate (MARCKS) Protein.
S. L. Swierczynski and P. J. Blackshear (1995)
J. Biol. Chem. 270, 13436-13445
   Abstract »    Full Text »    PDF »


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