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Publication : Cloning and characterization of mPAL, a novel Shc SH2 domain-binding protein expressed in proliferating cells.

First Author  Schmandt R Year  1999
Journal  Oncogene Volume  18
Issue  10 Pages  1867-79
PubMed ID  10086341 Mgi Jnum  J:53892
Mgi Id  MGI:1333605 Doi  10.1038/sj.onc.1202507
Citation  Schmandt R, et al. (1999) Cloning and characterization of mPAL, a novel Shc SH2 domain-binding protein expressed in proliferating cells. Oncogene 18(10):1867-79
abstractText  Shc adaptor proteins play a role in linking activated cell surface receptors to the Ras signaling pathway in response to receptor mediated tyrosine kinase activation. While the function of Shc in the activation of the Ras pathway via binding to Grb2 has been well characterized, it is becoming increasingly apparent that Shc participates in additional signaling pathways through interactions with other cytoplasmic proteins. Using the yeast two-hybrid system, we have identified a unique Shc binding protein designated PAL (Protein expressed in Activated Lymphocytes) with no similarity to other known proteins. mPAL binds specifically to the Shc SH2 domain and unlike previously described Shc SH2 domain-protein interactions, the association of mPAL and Shc is phospho-tyrosine-independent. Both mPAL RNA and protein expression are restricted to tissues containing actively dividing cells and proliferating cells in culture. mPAL expression is induced upon growth factor stimulation and is down-regulated upon growth inhibition. This pattern, and timing of mPAL expression and its association with the Shc adaptor molecule suggests a role for this protein in signaling pathways governing cell cycle progression.
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