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      Comparison of the signaling abilities of the cytoplasmic domains of the insulin receptor and the insulin receptor-related receptor in 3T3-L1 adipocytes.

      1 , , ,
      Endocrinology
      The Endocrine Society

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          Abstract

          In the present work a chimeric receptor containing the intracellular domain of the insulin receptor-related receptor (IRR) and the extracellular domain of the colony stimulating factor-1 (CSF-1) receptor was expressed in 3T3-L1 adipocytes and compared with the parallel chimeric receptor containing the cytoplasmic domain of the insulin receptor (IR). Both chimeric receptors exhibited CSF-stimulated tyrosine kinase activity when assayed in vitro after in vivo activation comparable to that of the endogenous IR present in these cells. No cross-activation of the expressed chimeric and endogenous receptors was observed. The cytoplasmic domain of the IRR was found to 1) mediate activation of the Ser/Thr kinase Akt/PKB, 2) stimulate glucose uptake, 3) inhibit lipolysis, and 4) stimulate glycogen synthase, all with a potency comparable to those of the expressed CSF-1R/IR chimera and the endogenous insulin receptors. These results indicate that despite the extensive differences in sequence between the cytoplasmic domains of the IRR and IR, the elements required for insulin-specific responses have been conserved in this distinct member of the insulin receptor family.

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          Author and article information

          Journal
          Endocrinology
          Endocrinology
          The Endocrine Society
          0013-7227
          0013-7227
          Aug 1998
          : 139
          : 8
          Affiliations
          [1 ] Department of Molecular Pharmacology, Stanford University School of Medicine, California 94305, USA.
          Article
          10.1210/endo.139.8.6165
          9681510
          60461566-c603-49c7-bfd0-c1af146c73df
          History

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