You are not currently logged in.
Access JSTOR through your library or other institution:
Myristoylated and Nonmyristoylated Forms of a Protein are Phosphorylated by Protein Kinase C
Jonathan M. Graff, Jeffrey I. Gordon and Perry J. Blackshear
New Series, Vol. 246, No. 4929 (Oct. 27, 1989), pp. 503-506
Published by: American Association for the Advancement of Science
Stable URL: http://www.jstor.org/stable/1704590
Page Count: 4
You can always find the topics here!Topics: COS cells, Cell membranes, Gels, Phosphorylation, Chickens, P branes, Radioactive decay, String theory, Particulate matter, Autoradiography
Were these topics helpful?See something inaccurate? Let us know!
Select the topics that are inaccurate.
Preview not available
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.
Science © 1989 American Association for the Advancement of Science