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Polypyrimidine tract-binding protein promotes insulin secretory granule biogenesis.

Authors: Knoch, KP  Bergert, H  Borgonovo, B  Saeger, HD  Altkruger, A  Verkade, P  Solimena, M 
Citation: Knoch KP, etal., Nat Cell Biol. 2004 Mar;6(3):207-14. Epub 2004 Feb 22.
Pubmed: (View Article at PubMed) PMID:15039777
DOI: Full-text: DOI:10.1038/ncb1099

Pancreatic beta-cells store insulin in secretory granules that undergo exocytosis upon glucose stimulation. Sustained stimulation depletes beta-cells of their granule pool, which must be quickly restored. However, the factors promoting rapid granule biogenesis are unknown. Here we show that beta-cell stimulation induces the nucleocytoplasmic translocation of polypyrimidine tract-binding protein (PTB). Activated cytosolic PTB binds and stabilizes mRNAs encoding proteins of secretory granules, thus increasing their translation, whereas knockdown of PTB expression by RNA interference (RNAi) results in the depletion of secretory granules. These findings may provide insight for the understanding and treatment of diabetes, in which insulin secretion is typically impaired.


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CRRD Object Information
CRRD ID: 10045958
Created: 2015-06-25
Species: All species
Last Modified: 2015-06-25
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.