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Molecular and Cellular Biology, February 1999, p. 1539-1546, Vol. 19, No. 2
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

SH3P7 Is a Cytoskeleton Adapter Protein and Is Coupled to Signal Transduction from Lymphocyte Antigen Receptors

Oliver Larbolette, Bernd Wollscheid, Jutta Schweikert, Peter J. Nielsen, and Jürgen Wienands*

Abteilung für Molekulare Immunologie, Institut für Biologie III, Albert-Ludwigs-Universität Freiburg, and Max-Planck-Institut für Immunbiologie, D-79108 Freiburg, Germany

Received 3 September 1998/Accepted 26 October 1998

Lymphocytes respond to antigen receptor engagement with tyrosine phosphorylation of many cellular proteins, some of which have been identified and functionally characterized. Here we describe SH3P7, a novel substrate protein for Src and Syk family kinases. SH3P7 migrates in sodium dodecyl sulfate-polyacrylamide gel electrophoresis as a 55-kDa protein that is preferentially expressed in brain, thymus, and spleen. It contains multiple amino acid sequence motifs, including two consensus tyrosine phosphorylation sites of the YXXP type and one SH3 domain. A region of sequence similarity, which we named SCAD, was found in SH3P7 and three actin-binding proteins. The SCAD region may represent a new type of protein-protein interaction domain that mediates binding to actin. Consistent with this possibility, SH3P7 colocalizes with actin filaments of the cytoskeleton. Altogether, our data implicate SH3P7 as an adapter protein which links antigen receptor signaling to components of the cytoskeleton.

* Corresponding author. Mailing address: Max-Planck-Institut für Immunbiologie, Stübeweg 51, 79108 Freiburg, Germany. Phone: 49-761-5108-438. Fax: 49-761-5108-423. E-mail: wienands{at}immunbio.mpg.de.

Molecular and Cellular Biology, February 1999, p. 1539-1546, Vol. 19, No. 2
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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