KANK1 regulates the positioning of liprin-α1 and the spatial organization of insulin granule fusion in pancreatic β cells.

ABSTRACT: In β cells, insulin granule fusion is enriched at the capillary interface, which targets insulin secretion directly into the bloodstream. The cues and molecular mechanisms used to target granule fusion to this area remain unknown. The capillary interface is characterized by local activation of focal adhesions and an enrichment of presynaptic scaffold proteins, including liprin-α1, the latter suggesting that a presynaptic-like mechanism might control the targeting of insulin granules to this region. Here, we show that the focal adhesion-associated adaptor protein KANK1 is locally enriched at the β-cell capillary interface and its knockdown disrupts the subcellular localization of liprin-α1. Moreover, KANK1 knockdown reduced glucose-induced insulin secretion and led to the mistargeting of in

SUBMITTER: Deng K 

PROVIDER: S-EPMC12803835 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature