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Conformational surveillance of Orai1 by a rhomboid intramembrane protease prevents inappropriate CRAC channel activation

AG. Grieve, YC. Yeh, YF. Chang, HY. Huang, L. Zarcone, J. Breuning, N. Johnson, K. Stříšovský, MH. Brown, AB. Parekh, M. Freeman

. 2021 ; 81 (23) : 4784-4798.e7. [pub] 20211119

Jazyk angličtina Země Spojené státy americké

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc22011752

Grantová podpora
LO1047CX Medical Research Council - United Kingdom
101035/Z/13/Z Wellcome Trust - United Kingdom
220887/Z/20/Z Wellcome Trust - United Kingdom
Wellcome Trust - United Kingdom
BB/RO16771/1 Biotechnology and Biological Sciences Research Council - United Kingdom

E-zdroje Online Plný text

NLK Cell Press Free Archives od 1997-12-01 do Před 1 rokem
Free Medical Journals od 1997 do Před 1 rokem
Free Medical Journals od 1997 do Před 1 rokem
Open Access Digital Library od 1997-12-01
Elsevier Open Access Journals od 1997-12-01 do 2023-06-15
Elsevier Open Archive Journals od 1997-12-01 do Před 1 rokem

Odkazy

PubMed 34800360
DOI 10.1016/j.molcel.2021.10.025
Knihovny.cz E-zdroje

Calcium influx through plasma membrane calcium release-activated calcium (CRAC) channels, which are formed of hexamers of Orai1, is a potent trigger for many important biological processes, most notably in T cell-mediated immunity. Through a bioinformatics-led cell biological screen, we have identified Orai1 as a substrate for the rhomboid intramembrane protease RHBDL2. We show that RHBDL2 prevents stochastic calcium signaling in unstimulated cells through conformational surveillance and cleavage of inappropriately activated Orai1. A conserved disease-linked proline residue is responsible for RHBDL2's recognizing the active conformation of Orai1, which is required to sharpen switch-like signaling triggered by store-operated calcium entry. Loss of RHBDL2 control of CRAC channel activity causes severe dysregulation of downstream CRAC channel effectors, including transcription factor activation, inflammatory cytokine expression, and T cell activation. We propose that this surveillance function may represent an ancient activity of rhomboid proteases in degrading unwanted signaling proteins.

Citace poskytuje Crossref.org

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