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Published on: October 30, 2012

Receptor tyrosine phosphatase R-PTP-alpha is tyrosine-phosphorylated and associated with the adaptor protein Grb2

J Su1, A Batzer, J Sap

  • 1Department of Pharmacology, New York University Medical Center, New York 10016.

The Journal of Biological Chemistry
|July 22, 1994
PubMed

Insights

Receptor tyrosine phosphatases (R-PTPases) are linked to cellular signaling. R-PTP-alpha associates with Grb2, a key protein in signal transduction pathways, requiring tyrosine phosphorylation and Grb2

Area of Science:

  • Cellular biology
  • Molecular signaling
  • Biochemistry

Background:

  • Receptor tyrosine phosphatases (R-PTPases) are implicated in cellular signal transduction.
  • The adaptor protein Grb2 links receptor tyrosine kinases to the Ras pathway.

Purpose of the Study:

  • To investigate the association between R-PTP-alpha and Grb2.
  • To understand the role of R-PTP-alpha in cellular signaling pathways.

Main Methods:

  • In vivo and in vitro association studies.
  • Use of stably and transiently transfected cells.
  • Recombinant Grb2 protein utilized for in vitro assays.

Main Results:

  • A ubiquitous R-PTPase, R-PTP-alpha, was found to be tyrosine-phosphorylated.
  • R-PTP-alpha was associated in vivo with the Grb2 protein.
  • This association was reproducible in transfected cells and in vitro, requiring an intact SH2 domain in Grb2 and tyrosine phosphorylation of R-PTP-alpha.

Conclusions:

  • Establishes a link between a receptor tyrosine phosphatase (R-PTP-alpha) and a key signaling component (Grb2).
  • Provides a foundation for further research into the functional roles of R-PTP-alpha in cellular signaling.

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