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J Biol Chem, Vol. 274, Issue 9, 5263-5266, February 26, 1999
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From the The ErbB2 receptor tyrosine kinase plays a
critical role in a variety of developmental processes, and its aberrant
activation may contribute to the progression of some breast and ovarian
tumors. ASGP2, a transmembrane glycoprotein found on the surface of the highly metastatic ascites 13762 rat mammary adenocarcinoma cell line,
is constitutively associated with ErbB2 in these cells and in mammary
tissue from pregnant rats. Expression studies indicate that ASGP2
interacts directly and specifically with ErbB2 through one of its
epidermal growth factor-like domains and that the co-expression of the
two proteins in the same cell dramatically facilitates their direct
stable interaction. Ectopic expression of ASGP2 in human melanoma tumor
cells potentiates the response of endogenous ErbB2 to the neuregulin-1
growth factor. These observations point to a novel intramembrane
mechanism for the modulation of receptor tyrosine kinase activity.
Department of Cell Biology, Harvard Medical
School, and Division of Signal Transduction, Beth Israel Hospital,
Boston, Massachusetts 02215, the ¶ Department of Cell Biology and
Anatomy and the ** Department of Biochemistry and Molecular Biology,
University of Miami School of Medicine, Miami, Florida 33101, and the
Department of Medicine, University of California, San Diego, La
Jolla, California 92093
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