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(Received for publication, March 13, 1995; and in revised form, May 9, 1995) Hematopoietic cell phosphatase is a nonreceptor protein tyrosine
phosphatase that is preferentially expressed in hematopoietic cell
lineages. Motheaten mice, which are devoid of (functional)
hematopoietic cell phosphatase, have severe disturbances in the
regulation of B cell activation and differentiation. Because signals
transduced via the B cell antigen receptor are known to guide these
processes, we decided to analyze molecular interactions between the
hematopoietic cell phosphatase and the B cell antigen receptor.
Ligation of the B cell antigen receptor induces moderate tyrosine
phosphorylation of hematopoietic cell phosphatase and the formation of
a multimolecular complex containing additional 68-70- and 135-kDa
phosphoproteins. In resting B cells most of the hematopoietic cell
phosphatase proteins reside in the cytosolic compartment, whereas after
B cell antigen receptor cross-linking, a small fraction translocates
toward the membrane where it specifically binds to the 135-kDa
phosphoprotein. This 135-kDa glycoprotein was identified as CD22, a
transmembrane associate of the B cell antigen receptor complex.
Together these findings provide the first direct evidence that this
cytoplasmic tyrosine phosphatase is involved in antigen
receptor-mediated B cell activation, suggesting that in vivo B
cell antigen receptor constituents or associated molecules may serve as
substrate for its catalytic activity.
Volume 270,
Number 35,
Issue of September 01, pp. 20305-20308, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
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