<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>283(42)</volume><submitter>Wu Z</submitter><pubmed_abstract>Sigma-1 receptor (sigma-1R) agonists enhance inositol 1,4,5-trisphosphate (IP3)-dependent calcium release from endoplasmic reticulum by inducing dissociation of ankyrin B 220 (ANK 220) from the IP3 receptor (IP3R-3), releasing it from inhibition. MCF-7 breast tumor cells express little or no sigma-1R and were used here to investigate the effect of receptor overexpression and the role of its N- and C-terminal segments in function. We stably expressed intact sigma-1R (amino acids (aa) 1-223; lines 11 and 41), N-fragment (aa 1-100; line K3), or C-fragment (aa 102-223; line sg101). C-fragment expressed as a peripheral membrane-bound protein that was removable from the endoplasmic reticulum membrane by chaotropic salt wash, consistent with lack of a putative transmembrane domain. The expressed </pubmed_abstract><journal>The Journal of biological chemistry</journal><pagination>28198-215</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC2661391</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Role of sigma-1 receptor C-terminal segment in inositol 1,4,5-trisphosphate receptor activation: constitutive enhancement of calcium signaling in MCF-7 tumor cells.</pubmed_title><pmcid>PMC2661391</pmcid><pubmed_authors>Wu Z</pubmed_authors><pubmed_authors>Bowen WD</pubmed_authors></additional><is_claimable>false</is_claimable><name>Role of sigma-1 receptor C-terminal segment in inositol 1,4,5-trisphosphate receptor activation: constitutive enhancement of calcium signaling in MCF-7 tumor cells.</name><description>Sigma-1 receptor (sigma-1R) agonists enhance inositol 1,4,5-trisphosphate (IP3)-dependent calcium release from endoplasmic reticulum by inducing dissociation of ankyrin B 220 (ANK 220) from the IP3 receptor (IP3R-3), releasing it from inhibition. MCF-7 breast tumor cells express little or no sigma-1R and were used here to investigate the effect of receptor overexpression and the role of its N- and C-terminal segments in function. We stably expressed intact sigma-1R (amino acids (aa) 1-223; lines 11 and 41), N-fragment (aa 1-100; line K3), or C-fragment (aa 102-223; line sg101). C-fragment expressed as a peripheral membrane-bound protein that was removable from the endoplasmic reticulum membrane by chaotropic salt wash, consistent with lack of a putative transmembrane domain. The expressed </description><dates><release>2008-01-01T00:00:00Z</release><publication>2008 Oct</publication><modification>2025-04-21T17:59:30.593Z</modification><creation>2019-03-27T00:21:26Z</creation></dates><accession>S-EPMC2661391</accession><cross_references><pubmed>18539593</pubmed><doi>10.1074/jbc.m802099200</doi><doi>10.1074/jbc.M802099200</doi></cross_references></HashMap>