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(Received for publication, August 7, 1996, and in revised form, November 11, 1996)
From the Departments of The Crk-associated substrate p130Cas
(Cas) and the recently described human enhancer of filamentation 1 (HEF1) are two proteins with similar structure (64% amino acid
homology), which are thought to act as "docking" molecules in
intracellular signaling cascades. Both proteins contain an N-terminal
Src homology (SH), three domain and a cluster of SH2 binding motifs.
Here we show that ligation of either
Volume 272, Number 7,
Issue of February 14, 1997
pp. 4230-4236
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
§
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,§
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,¶¶
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Medicine and
¶ Pathology, Harvard Medical School, Boston, Massachusetts 02115, the ** Institute for Cancer Research, Fox Chase Cancer Center,
Philadelphia, Pennsylvania 19111, the Third
Department of Internal Medicine, University of Tokyo, Hongo, Tokyo 113, Japan, the §§ Division of Hematology and Medical
Oncology, Oregon Health Sciences University, Portland, Oregon 97201, the ¶¶ Division of Hematology/Oncology, Deaconess
Hospital, Boston, Massachusetts 02115, and the Divisions of
§ Hematologic Malignancies and 
Tumor Immunology,
Dana-Farber Cancer Institute, Boston, Massachusetts 02115
1 integrin or B cell antigen
receptor (BCR) on human tonsillar B cells and B cell lines promoted
tyrosine phosphorylation of HEF1. In contrast, Cas tyrosine
phosphorylation was observed in certain B cell lines but not in
tonsillar B cells, indicating a more general role for HEF1 in B cell
signaling. Interestingly, pretreatment of tonsillar B cells with
cytochalasin B dramatically reduced both integrin- and BCR-induced HEF1
phosphorylation, suggesting that some component of the BCR-mediated
signaling pathway is closely linked with a cytoskeletal reorganization.
Both HEF1 and Cas were found to complex with the related adhesion focal
tyrosine kinase (RAFTK), and when tyrosine phosphorylated, with the
adapter molecule CrkL. In addition, the two molecules were detected in
p53/56Lyn immunoprecipitates, and Lyn kinase was found to
specifically bind the C-terminal proline-rich sequence of Cas in an
in vitro binding assay. These associations implicate HEF1
and Cas as important components in a cytoskeleton-linked signaling
pathway initiated by ligation of 1 integrin or BCR on human B cells.
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