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(Received for publication, August 5, 1996, and in revised form, August 30, 1996)
From the Department of Molecular Pharmacology and Biological
Chemistry, Northwestern University Medical School, Chicago, Illinois
60611 and the § Department of Physiology, Rush University,
Chicago, Illinois 60612
The hydrophilic
Volume 271, Number 43,
Issue of October 25, 1996
pp. 26465-26468
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
COMMUNICATION:
2a Subunit and Effects on Channel Function
2a subunit of the
L-type calcium channel was recently shown to be a membrane-localized,
post-translationally modified protein (Chien, A. J., Zhao, X. L.,
Shirokov, R. E., Puri, T. S., Chang, C. F., Sun, D. D., Rios, E., and
Hosey, M. M. (1995) J. Biol. Chem. 270, 30036-30044).
In this study, we demonstrate that the rat 2a subunit
was palmitoylated through a hydroxylamine-sensitive thioester linkage.
Palmitoylation required a pair of cysteines in the N terminus,
Cys3 and Cys4; mutation of these residues to
serines resulted in mutant 2a subunits that were unable
to incorporate palmitic acid. Interestingly, a palmitoylation-deficient
2a mutant still localized to membrane particulate
fractions and was still able to target functional channel complexes to
the plasma membrane similar to wild-type 2a. However,
channels formed with a palmitoylation-deficient 2a
subunit exhibited a dramatic decrease in ionic current per channel,
indicating that although mutations eliminating palmitoylation did not
affect channel targeting by the 2a subunit, they were
important determinants of channel modulation by the 2a
subunit. Three other known subunits that were analyzed were not
palmitoylated, suggesting that palmitoylation could provide a basis for
the regulation of L-type channels through modification of a specific
isoform.
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