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Journal Article

Polypyrimidine tract-binding protein promotes insulin secretory granule biogenesis.

MPS-Authors
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Borgonovo,  Barbara
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Verkade,  Paul
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Solimena,  Michele
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Knoch, K.-P., Bergert, H., Borgonovo, B., Saeger, H.-D., Altkruger, A., Verkade, P., et al. (2004). Polypyrimidine tract-binding protein promotes insulin secretory granule biogenesis. Nature Cell Biology, 6(3), 207-214.


Cite as: https://hdl.handle.net/21.11116/0000-0001-1261-D
Abstract
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.