NDLI: A kinase-negative epidermal growth factor receptor that retains the capacity to stimulate DNA synthesis.

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A kinase-negative epidermal growth factor receptor that retains the capacity to stimulate DNA synthesis.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Staros, J. V. Coker, K. J. Guyer, C. A.
Description	Author Affiliation: Coker KJ ( Department of Biochemistry, Vanderbilt University, Nashville, TN 37235.);
Abstract	The residue proposed to serve as the catalytic base for phosphoryl transfer, Asp-813, of the human epidermal growth factor receptor (EGFR) was mutated to Ala, and the mutant receptor (D813A) was expressed in Chinese hamster ovary (CHO) cells. Partially purified D813A exhibited no detectable kinase activity in the absence or presence of EGF. A low level of EGF-stimulable phosphorylation of D813A was detectable in intact cells, apparently due to the activity of an associated Tyr kinase(s). As previously observed for kinase-inactive Lys-721 mutants, EGF binding to D813A stimulates mitogen-activated protein kinase activity. Surprisingly, and unlike results reported for Lys-721 mutants, D813A is capable of stimulating both 86Rb+ uptake and DNA synthesis in response to EGF. These data suggest not only that Asp-813 is critical to the catalytic activity of the EGFR but also that differences may exist in the signaling properties of kinase-negative Lys-721 and kinase-negative Asp-813 EGFR mutants.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	15
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	DNA Biosynthesis Receptor, Epidermal Growth Factor Metabolism 3T3 Cells Alanine Animals Aspartic Acid CHO Cells Catalysis Cricetinae Cricetulus Mice Mutagenesis, Site-Directed Protein Kinases Signal Transduction Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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