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• W2011717731 abstract "Elimination of misfolded membrane proteins in the endoplasmic reticulum (ER) affects cell survival and growth and can be triggered by either local physiologic events or disease-associated mutations. Regulation of signaling receptor degradation involves both cytosolic and ER luminal molecular chaperones, but the mechanisms and timing of this process remain uncertain. Here we report that calreticulin (CRT) and Hsp90 exert distinct effects on the stability and cell surface levels of native and misfolded forms of the human insulin receptor (hIR) and a human variant found in type A insulin resistance. CRT was unique in stabilizing the disease variant and in augmenting hIR expression when glycolysis was abrogated. Effects of Hsp90 were independent of receptor tyrosine phosphorylation and did not change levels of downstream signaling kinases. Live cell imaging revealed that movement of the hIR through the ER was accelerated by misfolding or by overexpression of either CRT or Hsp90. Together, our results indicate that both CRT and Hsp90 control expression of hIR at its earliest maturation stages and modulate its movement within the ER before either degradation or cell surface expression." @default.
• W2011717731 created "2016-06-24" @default.
• W2011717731 creator A5023940237 @default.
• W2011717731 creator A5037192863 @default.
• W2011717731 creator A5053445367 @default.
• W2011717731 date "2007-06-19" @default.
• W2011717731 modified "2023-09-26" @default.
• W2011717731 title "Calreticulin and Hsp90 stabilize the human insulin receptor and promote its mobility in the endoplasmic reticulum" @default.
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• W2011717731 doi "https://doi.org/10.1073/pnas.0701114104" @default.
• W2011717731 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1965537" @default.
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• W2011717731 hasPublicationYear "2007" @default.
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