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Phospho-dephospho-control by insulin is mimicked by a phospho-oligosaccharide in adipocytes

Nature volume 330, pages 77–79 (1987)Cite this article

Abstract

The mechanism of insulin action is only partly understood1,2. At one end of the signalling chain, the structure of the insulin receptor is known in detail3, and at the other end, insulin controls cellular metabolism by regulating the phosphorylation of serine and threonine residues in key target enzymes4,5. The molecular events linking the occupied receptor to changes in target enzyme phosphorylation have remained obscure. Recently, insulin was shown to promote the hydrolysis of a phosphatidylinositol glycan with release of its polar head-group6,7. The head group was reported to activate a high-affinity cyclic AMP-phosphodiesterase6 and pyruvate dehydrogenase8, to inhibit catecholamine-stimulated lipolysis9, and also to inhibit phospholipid methyltransferase10 and adenylate cyclase8. We report here that in intact adipocytes this head-group faithfully copies the insulin-directed effects on the phosphorylation and dephosphorylation of target proteins of the hormone.

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References

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  1. Peter Strålfors: To whom correspondence should be addressed.

Authors and Affiliations

  1. Departmento de Metabolismo, Nutrition y Hormonas, Fundacion Jiménez Diaz, Avenida Reyes Catolicos 2, 28040, Madrid, Spain

    Susana Alemany & Jose M. Mato

  2. Department of Physiological Chemistry, University of Lund, Box 94, S-22100, Lund, Sweden

    Peter Strålfors

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  1. Susana Alemany
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  2. Jose M. Mato
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Alemany, S., Mato, J. & Strålfors, P. Phospho-dephospho-control by insulin is mimicked by a phospho-oligosaccharide in adipocytes. Nature 330, 77–79 (1987). https://doi.org/10.1038/330077a0

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