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J Biol Chem, Vol. 274, Issue 9, 5542-5549, February 26, 1999
, a Src Homology 2 and 3 Domain-containing Adapter Protein Having Similar Binding and Biological
Properties to Nck
From the Department of Biochemistry and Molocular Biology and
Walther Oncology Center, Indiana University School of Medicine,
Indianapolis, Indiana 46202
Adapter proteins made up of Src homology (SH)
domains mediate multiple cellular signaling events initiated by
receptor protein tyrosine kinases. Here we report that Grb4 is an
adapter protein closely related to but distinct from Nck that is made
up of three SH3 domains and one SH2 domain. Northern analysis indicated
that both genes are expressed in multiple tissues. Both Nck and Grb4 proteins could associate with receptor tyrosine kinases and the SH3-binding proteins PAK, Sos1, and PRK2, and they synergized with
v-Abl and Sos to induce gene expression via the transcription factor
Elk-1. Although neither protein was transforming on its own, both Nck
and Grb4 cooperated with v-Abl to transform NIH 3T3 cells and
influenced the morphology and anchorage-dependent growth of
wild type Ras-transformed cells. Nck and Grb4 therefore appear to be
functionally redundant.
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