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Myristoylation and the post-translational acquisition of hydrophobicity by the membrane immunoglobulin heavy-chain polypeptide in B lymphocytes

Pillai, Shiv and Baltimore, David (1987) Myristoylation and the post-translational acquisition of hydrophobicity by the membrane immunoglobulin heavy-chain polypeptide in B lymphocytes. Proceedings of the National Academy of Sciences of the United States of America, 84 (21). pp. 7654-7658. ISSN 0027-8424. http://resolver.caltech.edu/CaltechAUTHORS:PILpnas87

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Abstract

Membrane immunoglobulin heavy chain in pre-B and in B cells is initially synthesized as a relatively hydrophilic protein that is nonetheless stably anchored in the endoplasmic reticulum membrane. In B cells, but not in pre-B cells, the membrane immunoglobulin heavy chain is post-translationally converted to a relatively hydrophobic form that partitions into the oil phase when solubilized with the phase-separating detergent Triton X-114. Covalent myristoylation of the membrane and secretory forms of immunoglobulin heavy chains as well as of light chains was observed in B cells. Myristoylation of the membrane immunoglobulin heavy chain correlates with its transport to the cell surface and its post-translational conversion to a relatively hydrophobic form. This post-translational modification is hydroxylamine resistant and may be responsible for the assembly and transport of membrane immunoglobulin to the cell surface in B cells.


Item Type:Article
Additional Information:© 1987 by the National Academy of Sciences. Contributed by David Baltimore, July 20, 1987. S.P. was supported by the International Union Against Cancer and the Arthritis Foundation. This work was supported by a grant to D.B. from the American Cancer Society. The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indicate this fact.
Subject Keywords:membrane immunoglobulin; acylation
Record Number:CaltechAUTHORS:PILpnas87
Persistent URL:http://resolver.caltech.edu/CaltechAUTHORS:PILpnas87
Alternative URL:http://www.pnas.org/cgi/content/abstract/84/21/7654
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:10184
Collection:CaltechAUTHORS
Deposited By: Tony Diaz
Deposited On:16 Apr 2008
Last Modified:26 Dec 2012 09:57

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