Insulin signal transduction through protein kinase cascades View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1998

AUTHORS

Joseph Avruch

ABSTRACT

This review summarizes the evolution of ideas concerning insulin signal transduction, the current information on protein ser/thr kinase cascades as signalling intermediates, and their status as participants in insulin regulation of energy metabolism. Best characterized is the Ras-MAPK pathway, whose input is crucial to cell fate decisions, but relatively dispensable in metabolic regulation. By contrast the effectors downstream of PI-3 kinase, although less well elucidated, include elements indispensable for the insulin regulation of glucose transport, glycogen and cAMP metabolism. Considerable information has accrued on PKB/cAkt, a protein kinase that interacts directly with Ptd Ins 3′OH phosphorylated lipids, as well as some of the elements further downstream, such as glycogen synthase kinase-3 and the p70 S6 kinase. Finally, some information implicates other erk pathways (e.g. such as the SAPK/JNK pathway) and Nck/cdc42-regulated PAKs (homologs of the yeast Ste 20) as participants in the cellular response to insulin. Thus insulin recruits a broad array of protein (ser/thr) kinases in its target cells to effectuate its characteristic anabolic and anticatabolic programs. (Mol Cell Biochem 182: 31-48, 1998) More... »

PAGES

31-48

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4615-5647-3_4

DOI

http://dx.doi.org/10.1007/978-1-4615-5647-3_4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1048057053


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