Comparison of the signaling abilities of the drosophila and human insulin receptors in mammalian cells Journal Article

  


Authors: Yamaguchi, T.; Fernandez, R.; Roth, R. A.
Article Title: Comparison of the signaling abilities of the drosophila and human insulin receptors in mammalian cells
Abstract: Chimeric receptors encoding either the whole or a portion of the cytoplasmic domain of the drosophila insulin receptor (IR) with the extracellular domain of the human IR were expressed either transiently in COS cells or stably in Chinese hamster ovary cells and compared with the wild-type human IR. All three receptors bound insulin equally and exhibited an insulin-activated tyrosine kinase activity. The ability of the drosophila cytoplasmic domain to mediate the tyrosine phosphorylation of insulin receptor substrate 1, stimulate cell proliferation, and activate MAP kinase was found to be indistinguishable from that of the human IR. The chimeric drosophila receptors did not bind more phosphatidylinositol 3-kinase than the human IR, despite containing a C-terminal extension with potential tyrosine phosphorylation sites in the motif recognized by the SH2 domain of this enzyme. Thus, the essential signal-transducing abilities of the IR appear to have been conserved from invertebrates to mammals, despite the considerable differences in the sequences of these receptors. © 1995, American Chemical Society. All rights reserved.
Keywords: signal transduction; mitogen activated protein kinase; protein phosphorylation; human cell; nonhuman; comparative study; animal cell; animal; cell line; drosophila; enzyme activation; tyrosine; chimera; molecular sequence data; species specificity; immunoblotting; base sequence; drosophila melanogaster; dna, complementary; cho cell; cho cells; cricetulus; insulin receptor; phosphatidylinositol kinase; radioligand assay; precipitin tests; human; priority journal; article; support, u.s. gov't, p.h.s.; hamsters; receptor, insulin; chimeric proteins
Journal Title: Biochemistry
Volume: 34
Issue: 15
ISSN: 0006-2960
Publisher: American Chemical Society  
Date Published: 1995-04-18
Start Page: 4962
End Page: 4968
Language: English
DOI: 10.1021/bi00015a007
PUBMED: 7711018
PROVIDER: scopus
DOI/URL:

https://www.scopus.com/inward/record.uri?eid=2-s2.0-0028949153&doi=10.1021%2fbi00015a007&partnerID=40&md5=97239b09de1b97437ef53c600d557257
Notes: Article -- Export Date: 28 August 2018 -- Source: Scopus
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