JBC Transcription and Nuclear Factor Monoclonals

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Originally published In Press as doi:10.1074/jbc.M204607200 on June 24, 2002

J. Biol. Chem., Vol. 277, Issue 36, 33032-33040, September 6, 2002
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Mass Spectrometric Analysis of GAP-43/Neuromodulin Reveals the Presence of a Variety of Fatty Acylated Species*

Xiquan LiangDagger , Yun Lu§, Thomas A. Neubert§, and Marilyn D. ReshDagger

From the Dagger  Cell Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021 and § Skirball Institute of Biomolecular Medicine and Department of Pharmacology, School of Medicine, New York University, New York, New York 10016

GAP-43 (neuromodulin) is a protein kinase C substrate that is abundant in developing and regenerating neurons. Thioester-linked palmitoylation at two cysteines near the GAP-43 N terminus has been implicated in directing membrane binding. Here, we use mass spectrometry to examine the stoichiometry of palmitoylation and the molecular identity of the fatty acid(s) attached to GAP-43 in vivo. GAP-43 expressed in either PC12 or COS-1 cells was acetylated at the N-terminal methionine. Approximately 35% of the N-terminal GAP-43 peptides were also modified by palmitate and/or stearate on Cys residues. Interestingly, a variety of acylated species was detected, in which one of the Cys residues was acylated by either palmitate or stearate, or both Cys residues were acylated by palmitates or stearates or a combination of palmitate and stearate. Depalmitoylation of membrane-bound GAP-43 did not release the protein from the membrane, implying that additional forces function to maintain membrane binding. Indeed, mutation of four basic residues within the N-terminal domain of GAP-43 dramatically reduced membrane localization of GAP-43 without affecting palmitoylation. These data reveal the heterogeneous nature of S-acylation in vivo and illustrate the power of mass spectrometry for identification of key regulatory protein modifications.

* This work was supported by National Institutes of Health (NIH) Grant GM/CA 57966, Grant A046 from the American Institute for Cancer Research, and NIH Shared Instrumentation Grant 1 S10 RR14662-01 (to T. A. N.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Cell Biology and Genetics Program, Sloan-Kettering Institute for Cancer Research, 1275 York Ave., Box 143, New York, NY 10021. Tel.: 212-639-2514; Fax: 212-717-3317; E-mail: m-resh@ski.mskcc.org.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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