Integrin-linked kinase regulates phosphorylation of serine 473 of protein kinase B by an indirect mechanism View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

1999-12

AUTHORS

Danielle K Lynch, Christine A Ellis, Paul AW Edwards, Ian D Hiles

ABSTRACT

The serine threonine kinase protein kinase B regulates cellular activities as diverse as glycogen metabolism and apoptosis. Full activation of protein kinase B requires 3-phosphoinositides and dual phosphorylation on threonine-308 and serine-473. CaM-K kinase and 3-phosphoinositide dependent-kinase-1 phosphorylate threonine-308. Integrin-linked kinase reportedly phophorylates serine-473. Consistent with this, in a model COS cell system we show that expression of wild-type integrin-linked kinase promotes the wortmannin sensitive phosphorylation of serine-473 of protein kinase B and its downstream substrates, and inhibits C2-ceramide induced apoptosis. In contrast, integrin-linked kinase mutated in a lysine residue critical for function in protein kinases is inactive in these experiments, and furthermore, acts dominantly to block serine-473 phosphorylation induced by ErbB4. However, alignment of analogous sequences from different species demonstrates that integrin-linked kinase is not a typical protein kinase and identifies a conserved serine residue which potentially regulates kinase activity in a phosphorylation dependent manner. Mutation of this serine to aspartate or glutamate, but not alanine, in combination with the inactivating lysine mutation restores integrin-linked kinase dependent phosphorylation of serine-473 of protein kinase B. These data strongly suggest that integrin-linked kinase does not possess serine-473 kinase activity but functions as an adaptor to recruit a serine-473 kinase or phosphatase. More... »

PAGES

1203258

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/sj.onc.1203258

DOI

http://dx.doi.org/10.1038/sj.onc.1203258

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1043845856

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10637513


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