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• W2113561514 endingPage "2840" @default.
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• W2113561514 abstract "Insulin resistance is a defining feature of type 2 diabetes and the metabolic syndrome. While the molecular mechanisms of insulin resistance are multiple, recent evidence suggests that attenuation of insulin signaling by c-Jun N-terminal kinase (JNK) may be a central part of the pathobiology of insulin resistance. Here we demonstrate that the p85α regulatory subunit of phosphoinositide 3-kinase (PI3K), a key mediator of insulin's metabolic actions, is also required for the activation of JNK in states of insulin resistance, including high-fat diet-induced obesity and JNK1 overexpression. The requirement of the p85α regulatory subunit for JNK occurs independently of its role as a component of the PI3K heterodimer and occurs only in response to specific stimuli, namely, insulin and tunicamycin, a chemical that induces endoplasmic reticulum stress. We further show that insulin and p85 activate JNK by via cdc42 and MKK4. The activation of this cdc42/JNK pathway requires both an intact N terminus and functional SH2 domains within the C terminus of the p85α regulatory subunit. Thus, p85α plays a dual role in regulating insulin sensitivity and may mediate cross talk between the PI3K and stress kinase pathways." @default.
• W2113561514 created "2016-06-24" @default.
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• W2113561514 date "2007-04-01" @default.
• W2113561514 modified "2023-10-11" @default.
• W2113561514 title "The p85<i>α</i> Regulatory Subunit of Phosphoinositide 3-Kinase Potentiates c-Jun N-Terminal Kinase-Mediated Insulin Resistance" @default.
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• W2113561514 doi "https://doi.org/10.1128/mcb.00079-07" @default.
• W2113561514 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1899914" @default.
• W2113561514 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17283057" @default.
• W2113561514 hasPublicationYear "2007" @default.
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