Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

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...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cells, Cultured
Share to Mice

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mice, Knockout

Share to Microscopy, Confocal

Share to Mutation

Share to Protein Binding

Share to Time Factors

Share to 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 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to regulate Ca2+ store release-induced Ca2+ entry in endothelial cells.PMID 19052258Read ↗

Dissecting the functions of protein-protein interactions: caveolin as a promiscuous partner. Focus on "Caveolin-1 scaffold domain interacts with TRPC1 and IP3R3 to regulate Ca2+ store release-induced Ca2+ entry in endothelial cells".Semantic proximity Read ↗

Heteromeric TRPV4-C1 channels contribute to store-operated Ca(2+) entry in vascular endothelial cells.Semantic proximity Read ↗

TRPC3 controls agonist-stimulated intracellular Ca2+ release by mediating the interaction between inositol 1,4,5-trisphosphate receptor and RACK1.Semantic proximity Read ↗

The Interaction of Caveolin 3 Protein with the Potassium Inward Rectifier Channel Kir2.1Semantic proximity Read ↗

Ligand sensitivity of type-1 inositol 1,4,5-trisphosphate receptor is enhanced by the D2594K mutation.Semantic proximity Read ↗

Caveolin-3 and SAP97 form a scaffolding protein complex that regulates the voltage-gated potassium channel Kv1.5.Semantic proximity Read ↗

TRPC1 participates in the HSV-1 infection process by facilitating viral entry.Semantic proximity Read ↗

Critical regions for activation gating of the inositol 1,4,5-trisphosphate receptor.Semantic proximity Read ↗

Impairment of store-operated Ca2+ entry in TRPC4(-/-) mice interferes with increase in lung microvascular permeability.Semantic proximity Read ↗

TRPC3 mediates T-cell receptor-dependent calcium entry in human T-lymphocytes.Semantic proximity Read ↗

Functional interaction of the two-pore domain potassium channel TASK-1 and caveolin-3.Semantic proximity Read ↗

Disruption of Ca2+/calmodulin:KSR1 interaction lowers ERK activation.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.