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.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Animals
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Calcium / chemistry*
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Calcium / metabolism*
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Calcium Channels / chemistry*
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Calcium Channels / metabolism*
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Calcium Channels / ultrastructure*
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Cell Membrane / metabolism
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Cell Membrane / ultrastructure
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Endoplasmic Reticulum / metabolism
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Endoplasmic Reticulum / ultrastructure
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Humans
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Ion Channel Gating*
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Membrane Proteins / chemistry*
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Membrane Proteins / metabolism*
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Membrane Proteins / ultrastructure*
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Neoplasm Proteins / chemistry*
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Neoplasm Proteins / metabolism*
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Neoplasm Proteins / ultrastructure*
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ORAI1 Protein
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Protein Binding
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Protein Interaction Domains and Motifs*
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Stromal Interaction Molecule 1
Substances
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Calcium Channels
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Membrane Proteins
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Neoplasm Proteins
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ORAI1 Protein
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ORAI1 protein, human
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STIM1 protein, human
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Stromal Interaction Molecule 1
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Calcium