4.4 Review

With the greatest care, stromal interaction molecule (STIM) proteins verify what skeletal muscle is doing

Journal

BMB REPORTS
Volume 51, Issue 8, Pages 378-387

Publisher

KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
DOI: 10.5483/BMBRep.2018.51.8.128

Keywords

Dihydropyridine receptors (DHPR); Excitation-contraction (EC) coupling; Sarcoplasmic/endoplasmic reticulum Ca-2(+)-ATPase 1a (SERCA1a); Store-operated Ca-2(+) entry (SOCE); Stromal interaction molecule (STIM)

Funding

  1. National Research Foundation of Korea - Korean government [NRF-2017R1 A2B4005924]

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Skeletal muscle contracts or relaxes to maintain the body position and locomotion. For the contraction and relaxation of skeletal muscle, Ca-2(+) in the cytosol of skeletal muscle fibers ads as a switch to turn on and off a series of contractile proteins. The cytosolic Ca-2(+) level in skeletal muscle fibers is governed mainly by movements of Ca-2(+) between the cytosol and the sarcoplasmic reticulum (SR). Store-operated Ca-2(+) entry (SOCE), a Ca-2(+) entryway from the extracellular space to the cytosol, has gained a significant amount of attention from muscle physiologists. Orai1 and stromal interaction molecule 1 (STIM1) are the main protein identities of SOCE. This mini-review focuses on the roles of STIM proteins and SOCE in the physiological and pathophysiological functions of skeletal muscle and in their correlations with recently identified proteins, as well as historical proteins that are known to mediate skeletal muscle function.

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