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

Identification of a novel endoplasmic reticulum export motif within the eighth α-helical domain (α-H8) of the human prostacyclin receptor.

Biochimica et biophysica acta - 1 Apr 2011

Donnellan Peter D, Kimbembe Cisca C, Reid Helen M, Kinsella B Therese

Abstract excerpt

The human prostacyclin receptor (hIP) undergoes agonist-dependent trafficking involving a direct interaction with Rab11a GTPase. The region of interaction was localised to a 14 residue Rab11a binding domain (RBD) within the proximal carboxyl-terminal (C)-tail domain of the hIP, consisting of Val(299)-Val(307) within the eighth helical domain (α-H8) adjacent to the palmitoylated residues at Cys(308)-Cys(311)....

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Motifs
Share to Arginine

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

Share to Calnexin

Share to Endoplasmic Reticulum

Share to Lysine

Share to Microscopy, Confocal

Share to Protein Structure, Secondary

Share to Radioligand Assay

Source

Identifiers

PMID: 21223948
DOI: 10.1016/j.bbamem.2011.01.003

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

Identification of a novel endoplasmic reticulum export motif within the eighth α-helical domain (α-H8) of the human prostacyclin receptor.PMID 21223948Read ↗

Palmitoylation of the human prostacyclin receptor. Functional implications of palmitoylation and isoprenylation.Semantic proximity Read ↗

Identification of a Ser/Thr cluster in the C-terminal domain of the human prostaglandin receptor EP4 that is essential for agonist-induced beta-arrestin1 recruitment but differs from the apparent principal phosphorylation site.Semantic proximity Read ↗

Internalization and recycling of the human prostacyclin receptor is modulated through its isoprenylation-dependent interaction with the delta subunit of cGMP phosphodiesterase 6.Semantic proximity Read ↗

Versatility and differential roles of cysteine residues in human prostacyclin receptor structure and function.Semantic proximity Read ↗

Role of the ERC motif in the proximal part of the second intracellular loop and the C-terminal domain of the human prostaglandin F2alpha receptor (hFP-R) in G-protein coupling control.Semantic proximity Read ↗

A conserved motif for the transport of G protein-coupled receptors from the endoplasmic reticulum to the cell surface.Semantic proximity Read ↗

New insights into human prostacyclin receptor structure and function through natural and synthetic mutations of transmembrane charged residues.Semantic proximity Read ↗

The key residue within the second extracellular loop of human EP3 involved in selectively turning down PGE2- and retaining PGE1-mediated signaling in live cells.Semantic proximity Read ↗

A single lys residue on the first intracellular loop modulates the endoplasmic reticulum export and cell-surface expression of α2A-adrenergic receptor.Semantic proximity Read ↗

Human prostacyclin receptor structure and function from naturally-occurring and synthetic mutations.Semantic proximity Read ↗

Identification of the N-linked glycosylation sites of the human relaxin receptor and effect of glycosylation on receptor function.Semantic proximity Read ↗

Internalization and sequestration of the human prostacyclin receptor.Semantic proximity Read ↗

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