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

Kappel, Sven; Borgström, Anna; Stoklosa, Paulina; Dörr, Kathrin; Peinelt, Christine (2019). Store-operated calcium entry in disease: Beyond STIM/Orai expression levels. Seminars in cell & developmental biology, 94, pp. 66-73. Elsevier 10.1016/j.semcdb.2019.01.003

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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.

Item Type:

Journal Article (Review Article)

Division/Institute:

04 Faculty of Medicine > Faculty Institutions > NCCR TransCure
04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine

UniBE Contributor:

Kappel, Sven, Borgström, Anna, Stoklosa, Paulina Agnieszka, Peinelt, Christine

Subjects:

500 Science > 570 Life sciences; biology
600 Technology > 610 Medicine & health

ISSN:

1096-3634

Publisher:

Elsevier

Language:

English

Submitter:

Barbara Franziska Järmann-Bangerter

Date Deposited:

26 Sep 2019 15:16

Last Modified:

05 Dec 2022 15:30

Publisher DOI:

10.1016/j.semcdb.2019.01.003

PubMed ID:

30630032

Uncontrolled Keywords:

CRAC channels Glycosylation Orai regulatory proteins pH

BORIS DOI:

10.7892/boris.133497

URI:

https://boris.unibe.ch/id/eprint/133497

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