Structural elements of stromal interaction molecule function.

Abstract:

:Stromal interaction molecule (STIM)-1 and -2 are multi-domain, single-pass transmembrane proteins involved in sensing changes in compartmentalized calcium (Ca2+) levels and transducing this cellular signal to Orai1 channel proteins. Our understanding of the molecular mechanisms underlying STIM signaling has been dramatically improved through available X-ray crystal and solution NMR structures. This high-resolution structural data has revealed that intricate intramolecular and intermolecular protein-protein interactions are involved in converting STIMs from the quiescent to activation-competent states. This review article summarizes the current high resolution structural data on specific EF-hand, sterile α motif and coiled-coil interactions which drive STIM function in the activation of Orai1 channels. Further, the work discusses the effects of post-translational modifications on the structure and function of STIMs. Future structural studies on larger STIM:Orai complexes will be critical to fully defining the molecular bases for STIM function and how post-translational modifications influence these mechanisms.

journal_name

Cell Calcium

journal_title

Cell calcium

authors

Novello MJ,Zhu J,Feng Q,Ikura M,Stathopulos PB

doi

10.1016/j.ceca.2018.04.006

subject

Has Abstract

pub_date

2018-07-01 00:00:00

pages

88-94

eissn

0143-4160

issn

1532-1991

pii

S0143-4160(18)30059-9

journal_volume

73

pub_type

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