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Difference between revisions of "Wilson 2021 Mol Metab"

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(Created page with "{{Publication |title=Wilson RJ, Lyons SP, Koves TR, Bryson VG, Zhang H, Li T, Crown SB, Ding JD, Grimsrud PA, Rosenberg PB, Muoio DM (2021) Disruption of STIM1-mediated Ca2+ s...")
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{{Publication
{{Publication
|title=Wilson RJ, Lyons SP, Koves TR, Bryson VG, Zhang H, Li T, Crown SB, Ding JD, Grimsrud PA, Rosenberg PB, Muoio DM (2021) Disruption of STIM1-mediated Ca2+ sensing and energy metabolism in adult skeletal muscle compromises exercise tolerance, proteostasis and lean mass. Mol Metab [Epub ahead of print].
|title=Wilson RJ, Lyons SP, Koves TR, Bryson VG, Zhang H, Li T, Crown SB, Ding JD, Grimsrud PA, Rosenberg PB, Muoio DM (2021) Disruption of STIM1-mediated Ca<sup>2+</sup> sensing and energy metabolism in adult skeletal muscle compromises exercise tolerance, proteostasis and lean mass. Mol Metab [Epub ahead of print].
|info=[https://www.ncbi.nlm.nih.gov/pubmed/34979330 PMID: 34979330 Open Access]
|info=[https://www.ncbi.nlm.nih.gov/pubmed/34979330 PMID: 34979330 Open Access]
|authors=Wilson RJ, Lyons SP, Koves TR, Bryson VG, Zhang H, Li T, Crown SB, Ding JD, Grimsrud PA, Rosenberg PB, Muoio DM
|authors=Wilson RJ, Lyons SP, Koves TR, Bryson VG, Zhang H, Li T, Crown SB, Ding JD, Grimsrud PA, Rosenberg PB, Muoio DM
|year=2021
|year=2021
|journal=Mol Metab
|journal=Mol Metab
|abstract=STIM1 is a single-pass transmembrane endoplasmic/sarcoplasmic reticulum (E/SR) protein recognized for its role in store operated Ca2+ entry (SOCE), an ancient and ubiquitous signaling pathway. Whereas STIM1 is indispensable during development, its biological and metabolic functions in mature muscle were unclear. Shown here, STIM1 is abundant in adult skeletal muscle, upregulated by exercise, and present at SR-mitochondria interfaces. Among its multifaceted roles, STIM1 regulates Ca2+ signaling, mitochondrial Ca2+ loading, energy metabolism and protein homeostasis. Thus, inducible tissue-specific deletion of STIM1 (iSTIM1 KO) in adult muscle leads to diminished lean mass, reduced exercise capacity, and perturbed fuel selection in settings of energetic stress, without affecting whole-body glucose tolerance. Proteomics and phospho-proteomics analyses of iSTIM1 KO muscles revealed molecular signatures of low-grade E/SR stress and broad activation of processes and signaling networks involved in proteostasis. The findings provide insight into the pathophysiology of muscle diseases linked to disturbances in STIM1-dependent calcium handling.
|abstract=STIM1 is a single-pass transmembrane endoplasmic/sarcoplasmic reticulum (E/SR) protein recognized for its role in store operated Ca<sup>2+</sup> entry (SOCE), an ancient and ubiquitous signaling pathway. Whereas STIM1 is indispensable during development, its biological and metabolic functions in mature muscle were unclear. Shown here, STIM1 is abundant in adult skeletal muscle, upregulated by exercise, and present at SR-mitochondria interfaces. Among its multifaceted roles, STIM1 regulates Ca<sup>2+</sup> signaling, mitochondrial Ca<sup>2+</sup> loading, energy metabolism and protein homeostasis. Thus, inducible tissue-specific deletion of STIM1 (iSTIM1 KO) in adult muscle leads to diminished lean mass, reduced exercise capacity, and perturbed fuel selection in settings of energetic stress, without affecting whole-body glucose tolerance. Proteomics and phospho-proteomics analyses of iSTIM1 KO muscles revealed molecular signatures of low-grade E/SR stress and broad activation of processes and signaling networks involved in proteostasis. The findings provide insight into the pathophysiology of muscle diseases linked to disturbances in STIM1-dependent calcium handling.
|editor=[[Plangger M]]
|editor=[[Plangger M]]
}}
}}

Revision as of 18:17, 5 January 2022

Publications in the MiPMap
Wilson RJ, Lyons SP, Koves TR, Bryson VG, Zhang H, Li T, Crown SB, Ding JD, Grimsrud PA, Rosenberg PB, Muoio DM (2021) Disruption of STIM1-mediated Ca2+ sensing and energy metabolism in adult skeletal muscle compromises exercise tolerance, proteostasis and lean mass. Mol Metab [Epub ahead of print].

Β» PMID: 34979330 Open Access

Wilson RJ, Lyons SP, Koves TR, Bryson VG, Zhang H, Li T, Crown SB, Ding JD, Grimsrud PA, Rosenberg PB, Muoio DM (2021) Mol Metab

Abstract: STIM1 is a single-pass transmembrane endoplasmic/sarcoplasmic reticulum (E/SR) protein recognized for its role in store operated Ca2+ entry (SOCE), an ancient and ubiquitous signaling pathway. Whereas STIM1 is indispensable during development, its biological and metabolic functions in mature muscle were unclear. Shown here, STIM1 is abundant in adult skeletal muscle, upregulated by exercise, and present at SR-mitochondria interfaces. Among its multifaceted roles, STIM1 regulates Ca2+ signaling, mitochondrial Ca2+ loading, energy metabolism and protein homeostasis. Thus, inducible tissue-specific deletion of STIM1 (iSTIM1 KO) in adult muscle leads to diminished lean mass, reduced exercise capacity, and perturbed fuel selection in settings of energetic stress, without affecting whole-body glucose tolerance. Proteomics and phospho-proteomics analyses of iSTIM1 KO muscles revealed molecular signatures of low-grade E/SR stress and broad activation of processes and signaling networks involved in proteostasis. The findings provide insight into the pathophysiology of muscle diseases linked to disturbances in STIM1-dependent calcium handling.

β€’ Bioblast editor: Plangger M


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2022-01