TRPP2 and STIM1 form a microdomain to regulate store-operated Ca²⁺ entry and blood vessel tone.

ABSTRACT:

Background

Polycystin-2 (TRPP2) is a Ca²⁺ permeable nonselective cationic channel essential for maintaining physiological function in live cells. Stromal interaction molecule 1 (STIM1) is an important Ca²⁺ sensor in store-operated Ca²⁺ entry (SOCE). Both TRPP2 and STIM1 are expressed in endoplasmic reticular membrane and participate in Ca²⁺ signaling, suggesting a physical interaction and functional synergism.

Methods

We performed co-localization, co-immunoprecipitation, and fluorescence resonance energy transfer assay to identify the interactions of TRPP2 and STIM1 in transfected HEK293 cells and native vascular smooth muscle cells (VSMCs). The function of the TRPP2-STIM1 complex in thapsigargin (TG) or adenosine triphosphate (ATP

SUBMITTER: Guo J 

PROVIDER: S-EPMC7457527 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature