ArticleMolecular biology of the cell2012
MyRIP interaction with MyoVa on secretory granules is controlled by the cAMP-PKA pathway.
Article in Molecular biology of the cell, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 26 citations in OpenAlex.
- A novel membrane complex is required for docking and regulated exocytosis of lysosome-related organelles in Tetrahymena thermophila.PLoS genetics · 2022Article
- In vivo Roles of Rab27 and Its Effectors in Exocytosis.Cell structure and function · 2021Review
- Regulation of insulin exocytosis by calcium-dependent protein kinase C in beta cells.Cell calcium · 2017Review
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- Interaction between MyRIP and the actin cytoskeleton regulates Weibel-Palade body trafficking and exocytosis.Journal of cell science · 2016Article
- Rabphilin 3A retains NMDA receptors at synaptic sites through interaction with GluN2A/PSD-95 complex.Nature communications · 2015Article
- Synaptotagmin-7 phosphorylation mediates GLP-1-dependent potentiation of insulin secretion from β-cells.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- The circular RNA Cdr1as, via miR-7 and its targets, regulates insulin transcription and secretion in islet cells.Scientific reports · 2015Article
- Interplay between Rab27a effectors in pancreatic β-cells.World journal of diabetes · 2015Review
- Glutamate acts as a key signal linking glucose metabolism to incretin/cAMP action to amplify insulin secretion.Cell reports · 2014Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Myosin- and Rab-interacting protein (MyRIP), which belongs to the protein kinase A (PKA)-anchoring family, is implicated in hormone secretion. However, its mechanism of action is not fully elucidated. Here we investigate the role of MyRIP in myosin Va (MyoVa)-dependent secretory granule (SG) transport and secretion in pancreatic beta cells. These cells solely express the brain isoform of MyoVa (BR-MyoVa), which is a key motor protein in SG transport. In vitro pull-down, coimmunoprecipitation, and colocalization studies revealed that MyRIP does not interact with BR-MyoVa in glucose-stimulated pancreatic beta cells, suggesting that, contrary to previous notions, MyRIP does not link this motor protein to SGs. Glucose-stimulated insulin secretion is augmented by incretin hormones, which increase cAMP levels and leads to MyRIP phosphorylation, its interaction with BR-MyoVa, and phosphorylation of the BR-MyoVa receptor rabphilin-3A (Rph-3A). Rph-3A phosphorylation on Ser-234 was inhibited by small interfering RNA knockdown of MyRIP, which also reduced cAMP-mediated hormone secretion. Demonstrating the importance of this phosphorylation, nonphosphorylatable and phosphomimic Rph-3A mutants significantly altered hormone release when PKA was activated. These data suggest that MyRIP only forms a functional protein complex with BR-MyoVa on SGs when cAMP is elevated and under this condition facilitates phosphorylation of SG-associated proteins, which in turn can enhance secretion.
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