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SHR Neuro Cancer Cardio Lipid Metab Microb

Schindl, R; Muik, M; Fahrner, M; Derler, I; Fritsch, R; Bergsmann, J; Romanin, C.
Recent progress on STIM1 domains controlling Orai activation.
Cell Calcium. 2009; 46(4): 227-232. Doi: 10.1016/j.ceca.2009.08.003
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Leading authors Med Uni Graz: Schindl Rainer
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Abstract:: Ca(2+) entry in non-excitable cells is mainly carried by store-operated channels among which the CRAC channel is best characterized. Its two limiting molecular components are represented by the Ca(2+) sensor protein STIM1 located in the endoplasmic reticulum and Orai1 in the plasma membrane. STIM1 senses a decrease of the Ca(2+) content in internal stores and triggers its accumulation into puncta like structures resulting in coupling to as well as activation of Orai1 channels. The STIM1-Orai coupling process is determined by an interaction via their C-termini. This review highlights recent developments on domains particularly within the cytosolic part of STIM1 that govern this interaction.
Find related publications in this database (using NLM MeSH Indexing): Animals -; Calcium - chemistry; Calcium - metabolism; Calcium Channels - chemistry; Calcium Channels - metabolism; Calcium Channels - ultrastructure; Cell Membrane - metabolism; Cell Membrane - ultrastructure; Endoplasmic Reticulum - metabolism; Endoplasmic Reticulum - ultrastructure; Humans -; Ion Channel Gating -; Membrane Proteins - chemistry; Membrane Proteins - metabolism; Membrane Proteins - ultrastructure; Neoplasm Proteins - chemistry; Neoplasm Proteins - metabolism; Neoplasm Proteins - ultrastructure; ORAI1 Protein -; Protein Binding -; Protein Interaction Domains and Motifs -; Stromal Interaction Molecule 1 -
Find related publications in this database (Keywords): STIM1; Orai; STIM1-Orai coupling; Fast inactivation; CRAC