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J. Exp. Med.,
Volume 187, Number 7, April 6, 1998 1157-1161
By
From the * Department of Medicine and Rosalind Russell Arthritis Center, University of California,
San Francisco, California 94143; the Activation of T and natural killer (NK) cells leads to the tyrosine phosphorylation of pp36 and
to its association with several signaling molecules, including phospholipase C Institute of Medical Biochemistry and § Department of
Anatomy, University of Oslo, N-0317 Oslo, Norway; and the Veterans Administration Medical
Center, University of California, San Francisco, California 94122
-1 and Grb2.
Microsequencing of peptides derived from purified rat pp36 protein led to the cloning, in rat
and man, of cDNA encoding a T- and NK cell-specific protein with several putative Src homology 2 domain-binding motifs. A rabbit antiserum directed against a peptide sequence from
the cloned rat molecule recognized tyrosine phosphorylated pp36 from pervanadate-treated rat
thymocytes. When expressed in 293T human fibroblast cells and tyrosine-phosphorylated,
pp36 associated with phospholipase C-1 and Grb2. Studies with GST-Grb2 fusion proteins
demonstrated that the association was specific for the Src homology 2 domain of Grb-2. Molecular cloning of the gene encoding pp36 should facilitate studies examining the role of this
adaptor protein in proximal signaling events during T and NK cell activation.
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