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Volume 271, Number 45, Issue of November 8, 1996 pp. 28502-28508
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Cysteines 153 and 154 of Transmembrane Transforming Growth Factor- Are Palmitoylated and Mediate Cytoplasmic Protein Association

(Received for publication, June 3, 1996, and in revised form, July 19, 1996)

Lillian Shum , Christoph W. Turck and Rik Derynck

From the Department of Growth and Development and Department of Anatomy, Programs in Cell Biology and Developmental Biology, University of California, San Francisco, California 94143-0640 and the  Howard Hughes Medical Institute, Cardiovascular Research Institute and Department of Medicine, University of California, San Francisco, California 94143-0724

Transforming growth factor- (TGF-) is synthesized as a transmembrane protein with a highly conserved, short cytoplasmic domain that is rich in cysteines. TGF- is a prototype of a large family of growth factors involved in cell-cell communication. We have shown previously that transmembrane TGF- associates with a kinase activity and two proteins of 106 and 86 kDa. In this study, we have used site-directed mutagenesis of the cytoplasmic domain of TGF- to define the structural requirements for these protein interactions. Whereas the cytoplasmic domain of TGF- was not essential for association with transmembrane p106, deletion of the C-terminal 8 amino acids, including a cysteine pair, abolished the interaction with p86 and greatly reduced the kinase activity associated with transmembrane TGF-. Replacement of these 2 cysteines by serines similarly reduced the association of p86 with transmembrane TGF-. Using a combination of mutational analysis and direct microsequencing, we have determined that this cysteine pair was palmitoylated. We therefore conclude that these cysteines play a critical role in the interaction of TGF- with associated proteins and in the function of this protein complex. The palmitoylation of these cysteines suggests a possibly dynamic role of fatty acid modification in the integrity and function of the transmembrane TGF- complex.

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