2l5y
From Proteopedia
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== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/STIM2_HUMAN STIM2_HUMAN] Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Functions as a highly sensitive Ca(2+) sensor in the endoplasmic reticulum which activates both store-operated and store-independent Ca(2+)-influx. Regulates basal cytosolic and endoplasmic reticulum Ca(2+) concentrations. Upon mild variations of the endoplasmic reticulum Ca(2+) concentration, translocates from the endoplasmic reticulum to the plasma membrane where it probably activates the Ca(2+) release-activated Ca(2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca(2+) influx.<ref>PMID:16005298</ref> <ref>PMID:16860747</ref> <ref>PMID:17905723</ref> <ref>PMID:18160041</ref> <ref>PMID:21217057</ref> <ref>PMID:22464749</ref> <ref>PMID:23359669</ref> | [https://www.uniprot.org/uniprot/STIM2_HUMAN STIM2_HUMAN] Plays a role in mediating store-operated Ca(2+) entry (SOCE), a Ca(2+) influx following depletion of intracellular Ca(2+) stores. Functions as a highly sensitive Ca(2+) sensor in the endoplasmic reticulum which activates both store-operated and store-independent Ca(2+)-influx. Regulates basal cytosolic and endoplasmic reticulum Ca(2+) concentrations. Upon mild variations of the endoplasmic reticulum Ca(2+) concentration, translocates from the endoplasmic reticulum to the plasma membrane where it probably activates the Ca(2+) release-activated Ca(2+) (CRAC) channels ORAI1, ORAI2 and ORAI3. May inhibit STIM1-mediated Ca(2+) influx.<ref>PMID:16005298</ref> <ref>PMID:16860747</ref> <ref>PMID:17905723</ref> <ref>PMID:18160041</ref> <ref>PMID:21217057</ref> <ref>PMID:22464749</ref> <ref>PMID:23359669</ref> | ||
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| - | == Publication Abstract from PubMed == | ||
| - | Stromal interaction molecules (STIM)s function as endoplasmic reticulum calcium (Ca(2+)) sensors that differentially regulate plasma membrane Ca(2+) release activated Ca(2+) channels in various cells. To probe the structural basis for the functional differences between STIM1 and STIM2 we engineered a series of EF-hand and sterile alpha motif (SAM) domain (EF-SAM) chimeras, demonstrating that the STIM1 Ca(2+)-binding EF-hand and the STIM2 SAM domain are major contributors to the autoinhibition of oligomerization in each respective isoform. Our nuclear magnetic resonance (NMR) derived STIM2 EF-SAM structure provides a rationale for an augmented stability, which involves a 54 degrees pivot in the EF-hand:SAM domain orientation permissible by an expanded nonpolar cleft, ionic interactions, and an enhanced hydrophobic SAM core, unique to STIM2. Live cells expressing "super-unstable" or "super-stable" STIM1/STIM2 EF-SAM chimeras in the full-length context show a remarkable correlation with the in vitro data. Together, our data suggest that divergent Ca(2+)- and SAM-dependent stabilization of the EF-SAM fold contributes to the disparate regulation of store-operated Ca(2+) entry by STIM1 and STIM2. | ||
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| - | Auto-inhibitory role of the EF-SAM domain of STIM proteins in store-operated calcium entry.,Zheng L, Stathopulos PB, Schindl R, Li GY, Romanin C, Ikura M Proc Natl Acad Sci U S A. 2011 Jan 25;108(4):1337-42. Epub 2011 Jan 7. PMID:21217057<ref>PMID:21217057</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 2l5y" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
NMR structure of calcium-loaded STIM2 EF-SAM.
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