Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to regulate Ca2+ store release-induced Ca2+ entry in endothelial cells.

doi:10.1152/ajpcell.00470.2008

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Article

Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to regulate Ca2+ store release-induced Ca2+ entry in endothelial cells.

American journal of physiology. Cell physiology - 1 Mar 2009

Sundivakkam Premanand C, Kwiatek Angela M, Sharma Tiffany T, Minshall Richard D, Malik Asrar B, Tiruppathi Chinnaswamy

Abstract excerpt

Caveolin-1 (Cav-1) regulates agonist-induced Ca(2+) entry in endothelial cells; however, how Cav-1 regulates this process is poorly understood. Here, we describe that Cav-1 scaffold domain (NH(2)-terminal residues 82-101; CSD) interacts with transient receptor potential canonical channel 1 (TRPC1) and inositol 1,4,5-trisphosphate receptor 3 (IP(3)R3) to regulate Ca(2+) entry. We have shown previously that the...

Topics

Animals
Calcium Signaling
Caveolin 1
Cells, Cultured
Endothelial Cells
Humans
Inositol 1,4,5-Trisphosphate Receptors
Mice
Mice, Knockout
Microscopy, Confocal

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mutation

Protein Binding

Protein Interaction Domains and Motifs

Protein Interaction Mapping

TRPC Cation Channels

Thrombin

Time Factors

Transfection

Source

Open in PubMed Open full text

Identifiers

PMID: 19052258
DOI: 10.1152/ajpcell.00470.2008
PMCID: PMC2660268

Genes

TRPC1

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-19052258-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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