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Store-operated calcium entry in disease: Beyond STIM/Orai expression levels.
Journal article

Store-operated calcium entry in disease: Beyond STIM/Orai expression levels.

  • Kappel S Institute of Biochemistry and Molecular Medicine, National Center of Competence in Research NCCR TransCure, University of Bern, Bühlstrasse 28, 3012 Bern, Switzerland.
  • Borgström A Institute of Biochemistry and Molecular Medicine, National Center of Competence in Research NCCR TransCure, University of Bern, Bühlstrasse 28, 3012 Bern, Switzerland.
  • Stokłosa P Institute of Biochemistry and Molecular Medicine, National Center of Competence in Research NCCR TransCure, University of Bern, Bühlstrasse 28, 3012 Bern, Switzerland.
  • Dörr K Burgweg 8, 53424 Remagen, Germany.
  • Peinelt C Institute of Biochemistry and Molecular Medicine, National Center of Competence in Research NCCR TransCure, University of Bern, Bühlstrasse 28, 3012 Bern, Switzerland. Electronic address: christine.peinelt@ibmm.unibe.ch.
  • 2019-01-11
Published in:
  • Seminars in cell & developmental biology. - 2019
CRAC channels
Glycosylation
Orai regulatory proteins
pH
Animals
Calcium
Calcium Signaling
Humans
Inflammation
Neoplasm Proteins
Neoplasms
Neurodegenerative Diseases
ORAI1 Protein
Stromal Interaction Molecule 1
English Precise intracellular calcium signaling is crucial to numerous cellular functions. In non-excitable cells, store-operated calcium entry (SOCE) is a key step in the generation of intracellular calcium signals. Tight regulation of SOCE is important, and dysregulation is involved in several pathophysiological cellular malfunctions. The current underlying SOCE, calcium release-activated calcium current (ICRAC), was first discovered almost three decades ago. Since its discovery, the molecular components of ICRAC, Orai1 and stromal interaction molecule 1 (STIM1), have been extensively investigated. Several regulatory mechanisms and proteins contribute to alterations in SOCE and cellular malfunctions in cancer, immune and neurodegenerative diseases, inflammation, and neuronal disorders. This review summarizes these regulatory mechanisms, including glycosylation, pH sensing, and the regulatory proteins golli, α-SNAP, SARAF, ORMDL3, CRACR2A, and TRPM4 channels.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/185323
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