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

Agonist-induced up-regulation of human somatostatin receptor type 1 is regulated by beta-arrestin-1 and requires an essential serine residue in the receptor C-tail.

Biochimica et biophysica acta - 20 May 2005

Ramírez José L, Watt Heather L, Rocheville Magalie, Kumar Ujendra

Abstract excerpt

We have previously shown that the human somatostatin receptor type 1 (hSSTR1) does not undergo agonist-induced internalization, but is instead up-regulated at the membrane upon prolonged somatostatin (SST) exposure. The deletion of the carboxyterminal C-tail of the receptor completely abolishes up-regulation. To identify molecular signals that mediate hSSTR1 up-regulation, we created mutant receptors with...

Read the complete abstract on PubMed

Topics

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

Share to Adenylyl Cyclases
Share to Arrestins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to beta-Arrestins

Share to Calcium-Calmodulin-Dependent Protein Kinases

Share to Protein Structure, Secondary

Share to Receptors, Somatostatin

Share to Serine

Share to Up-Regulation

Source

Identifiers

PMID: 15893521
DOI: 10.1016/j.bbamem.2005.02.004

Genes

SST

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Agonist-induced up-regulation of human somatostatin receptor type 1 is regulated by beta-arrestin-1 and requires an essential serine residue in the receptor C-tail.PMID 15893521Read ↗

Agonist-dependent up-regulation of human somatostatin receptor type 1 requires molecular signals in the cytoplasmic C-tail.Semantic proximity Read ↗

Agonist-independent internalization and activity of a C-terminally truncated somatostatin receptor subtype 2 (delta349).Semantic proximity Read ↗

Somatostatin receptor-3 mediated intracellular signaling and apoptosis is regulated by its cytoplasmic terminal.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 ↗

Involvement of a cytoplasmic-tail serine cluster in urotensin II receptor internalization.Semantic proximity Read ↗

Importance of constitutive activity and arrestin-independent mechanisms for intracellular trafficking of the ghrelin receptor.Semantic proximity Read ↗

Replacement of threonine 394 by alanine facilitates internalization and resensitization of the rat mu opioid receptor.Semantic proximity Read ↗

Internalization-defective mutants of somatostatin receptor subtype 2 exert normal signaling functions in hematopoietic cells.Semantic proximity Read ↗

Desensitization and internalization of the human motilin receptor is independent of the C-terminal tail.Semantic proximity Read ↗

The human vasoactive intestinal Peptide/Pituitary adenylate cyclase activating peptide receptor 1 (VPAC1): constitutive activation by mutations at threonine 343.Semantic proximity Read ↗

Deciphering the specific role of G(αi/o) isoforms: functional selective oxytocin ligands and somatostatin SST5 receptor mutants.Semantic proximity Read ↗

Identification of a short linear sequence present in the C-terminal tail of the rat follitropin receptor that modulates arrestin-3 binding in a phosphorylation-independent fashion.Semantic proximity Read ↗

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