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(Received for publication, May 14, 1996, and in revised form, June 24, 1996)
From the Mitsubishi Kasei Institute of Life Sciences, 11 Minamiooya, Machida, Tokyo 194, Japan
BIT (a
Volume 271, Number 41,
Issue of October 11, 1996
pp. 25569-25574
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
rain
mmunoglobulin-like molecule with
yrosine-based activation motifs) is a brain-specific
membrane protein which has two cytoplasmic TAMs
(yrosine-based 
ctivation 
otifs).
Using the Far Western blotting technique, we detected association of a
70-kDa protein with the tyrosine-phosphorylated TAMs of BIT. A mouse
brain cDNA library in 
gt11 was screened for this association,
and two positive clones encoding tyrosine phosphatase SH-PTP2 were
isolated. SH-PTP2 has two SH2 domains and is believed to function as a
positive mediator in receptor tyrosine kinase signaling. SH-PTP2 and
BIT were coimmunoprecipitated from phosphorylated rat brain lysate, and
BIT was a major tyrosine-phosphorylated protein associated with SH-PTP2
in this lysate. This interaction was also observed in Jurkat T cells
transfected with BIT cDNA depending on tyrosine phosphorylation of
BIT. Bisphosphotyrosyl peptides corresponding to BIT-TAMs stimulated
SH-PTP2 activity 33-35-fold in vitro, indicating that two
SH2 domains of SH-PTP2 simultaneously interact with two
phosphotyrosines of BIT-TAM. Our findings suggest that the tyrosine
phosphorylation of BIT results in stimulation of the signal
transduction pathway promoted by SH-PTP2 and that BIT is probably a
major receptor molecule in the brain located just upstream of
SH-PTP2.
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