HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Biemann, H.-P. Articles by Koshland, D. E. Search for Related Content PubMed PubMed Citation Articles by Biemann, H.-P. Articles by Koshland, D. E., Jr. Social Bookmarking                      What's this?

Volume 271, Number 44, Issue of November 1, 1996 pp. 27927-27930
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

---

An Aspartate/Insulin Receptor Chimera Mitogenically Activates Fibroblasts

(Received for publication, April 1, 1996, and in revised form, August 7, 1996)

Hans-Peter Biemann , Stacey L. Harmer ^§ and Daniel E. Koshland Jr.^¶

From the  Department of Cell Biology, Genzyme Corporation, Cambridge, Massachusetts 02139, the ^§ G. W. Hooper Foundation, University of California, San Francisco, California 94143, and the ^¶ Department of Molecular and Cellular Biology, Stanley Hall, University of California, Berkeley, California 94720

A gene encoding the ligand-binding domain of the Escherichia coli aspartate receptor fused to the cytoplasmic domain of the insulin receptor tyrosine kinase to produce the chimeric aspartate insulin receptor (AIR) was expressed in mammalian cells. A murine fibroblast transfectant line designated CA3 was generated that stably expressed the AIR receptor. This 70,000 M_r receptor containing the tyrosine kinase of the insulin receptor was recognized by aspartate receptor-specific antisera. When isolated in cellular membrane preparations, AIR was found to be capable of autophosphorylation and phosphorylation of histone H2B on tyrosine. The receptor was found to be predominately cytoplasmic and to be situated in the endoplasmic reticulum and Golgi membranes by immunofluorescence imaging of CA3 cells. Mitogenic effects of AIR were observed; CA3 cells continued DNA synthesis under serum deprivation conditions that prevented parental cells from cycling. These results demonstrate that a chimeric receptor containing procaryotic transmembrane sequences is expressed by a eucaryotic cell in intracellular membranes and functionally couples to cellular signaling pathways.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				O. J. Murphy III, X. Yi, R. M. Weis, and L. K. Thompson Hydrogen Exchange Reveals a Stable and Expandable Core within the Aspartate Receptor Cytoplasmic Domain J. Biol. Chem., November 9, 2001; 276(46): 43262 - 43269. [Abstract] [Full Text] [PDF]

				R. B. Bass and J. J. Falke Detection of a Conserved alpha -Helix in the Kinase-docking Region of the Aspartate Receptor by Cysteine and Disulfide Scanning J. Biol. Chem., September 25, 1998; 273(39): 25006 - 25014. [Abstract] [Full Text] [PDF]

				M. A. Danielson, R. B. Bass, and J. J. Falke Cysteine and Disulfide Scanning Reveals a Regulatory alpha -Helix in the Cytoplasmic Domain of the Aspartate Receptor J. Biol. Chem., December 26, 1997; 272(52): 32878 - 32888. [Abstract] [Full Text] [PDF]