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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Li, Guang-yao Romanin, Christoph Ikura, Mitsuhiko Zheng, Le Schindl, Rainer Stathopulos, Peter B. |
| Description | Author Affiliation: Zheng L ( Division of Signaling Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, Toronto, ON, Canada M5G 1L7.); |
| Abstract | 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 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° 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. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 4 |
| Volume Number | 108 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2011-01-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Calcium Metabolism Cell Adhesion Molecules EF Hand Motifs Membrane Proteins Neoplasm Proteins Amino Acid Sequence Binding Sites Calcium Channels Chemistry Genetics Endoplasmic Reticulum HEK293 Cells HeLa Cells Hydrophobic And Hydrophilic Interactions Luminescent Proteins Magnetic Resonance Spectroscopy Membrane Potentials Microscopy, Fluorescence Models, Molecular Molecular Sequence Data Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Sequence Homology, Amino Acid Transfection Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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