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

The endoplasmic reticulum-associated protein, OS-9, behaves as a lectin in targeting the immature calcium-sensing receptor.

Journal of cellular physiology - 1 Jan 2018

Ward Bryan K, Rea Sarah L, Magno Aaron L, Pedersen Bernadette, Brown Suzanne J, Mullin Shelby, Arulpragasam Ajanthy, Ingley Evan, Conigrave Arthur D, Ratajczak Thomas

Abstract excerpt

The mechanisms responsible for the processing and quality control of the calcium-sensing receptor (CaSR) in the endoplasmic reticulum (ER) are largely unknown. In a yeast two-hybrid screen of the CaSR C-terminal tail (residues 865-1078), we identified osteosarcoma-9 (OS-9) protein as a binding partner. OS-9 is an ER-resident lectin that targets misfolded glycoproteins to the ER-associated degradation (ERAD)...

Read the complete abstract on PubMed

Topics

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

Share to Endoplasmic Reticulum-Associated Degradation
Share to Immunoprecipitation

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

Share to Lectins

Share to Mitogen-Activated Protein Kinase 1

Share to Mitogen-Activated Protein Kinase 3

Share to Protein Interaction Domains and Motifs

Share to Proteolysis

Share to Receptors, Calcium-Sensing

Source

Identifiers

PMID: 28419469
DOI: 10.1002/jcp.25957

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

The endoplasmic reticulum-associated protein, OS-9, behaves as a lectin in targeting the immature calcium-sensing receptor.PMID 28419469Read ↗

Unraveling the function of Arabidopsis thaliana OS9 in the endoplasmic reticulum-associated degradation of glycoproteins.Semantic proximity Read ↗

The C-terminal tail of tetraspanin protein CD9 contributes to its function and molecular organization.Semantic proximity Read ↗

OS9 Protein Interacts with Na-K-2Cl Co-transporter (NKCC2) and Targets Its Immature Form for the Endoplasmic Reticulum-associated Degradation Pathway.Semantic proximity Read ↗

ER residential chaperone GRP78 unconventionally relocalizes to the cell surface via endosomal transport.Semantic proximity Read ↗

Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation.Semantic proximity Read ↗

Immunosuppression by Mutated Calreticulin Released from Malignant Cells.Semantic proximity Read ↗

Calcium-sensing receptor ubiquitination and degradation mediated by the E3 ubiquitin ligase dorfin.Semantic proximity Read ↗

Characterization of the sterol and phosphatidylinositol 4-phosphate binding properties of Golgi-associated OSBP-related protein 9 (ORP9).Semantic proximity Read ↗

mu-Opioid receptor cell surface expression is regulated by its direct interaction with Ribophorin I.Semantic proximity Read ↗

OS-9 and GRP94 deliver mutant alpha1-antitrypsin to the Hrd1-SEL1L ubiquitin ligase complex for ERAD.Semantic proximity Read ↗

Transient dimerization and interaction with ERGIC-53 occur in the fibroblast growth factor receptor 3 early secretory pathway.Semantic proximity Read ↗

The mammalian endoplasmic reticulum stress response element consists of an evolutionarily conserved tripartite structure and interacts with a novel stress-inducible complexSemantic proximity Read ↗

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