STIM1 signalling controls store-operated calcium entry required for development and contractile function in skeletal muscle

It is now well established that stromal interaction molecule 1 (STIM1) is the calcium sensor of endoplasmic reticulum stores required to activate store-operated calcium entry (SOC) channels at the surface of non-excitable cells. However, little is known about STIM1 in excitable cells, such as striat...

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Published in	Nature Cell Biology Vol. 10; no. 6; pp. 688 - 697
Main Authors	Hawkins, April, Seth, Malini, Zhang, Zhu-Shan, Stiber, Jonathan, Finch, Elizabeth, Rosenberg, Paul, Williams, R. Sanders, Burch, Jarrett, Malouf, Nadia, Wang, Sunny, Graham, Victoria, Ward, Cary C, Eu, Jerry P
Format	Journal Article
Language	English
Published	London Nature Publishing Group UK 01.06.2008 Nature Publishing Group
Subjects	Animals Biomedical and Life Sciences Calcium Calcium - metabolism Calcium channels Calcium Channels - metabolism Calcium Signaling Cancer Research Cell Biology Cell Line Developmental Biology Endoplasmic reticulum Fatigue Gene Silencing Life Sciences Membrane Glycoproteins - metabolism Membrane Glycoproteins - physiology Membrane proteins Mice Models, Biological Models, Genetic Muscle Contraction Muscles Muscles - metabolism Musculoskeletal system Patch-Clamp Techniques Physiological aspects Plasma Sarcoplasmic Reticulum - metabolism Sensors Signal Transduction Stem Cells Stromal Interaction Molecule 1 United States
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Abstract	It is now well established that stromal interaction molecule 1 (STIM1) is the calcium sensor of endoplasmic reticulum stores required to activate store-operated calcium entry (SOC) channels at the surface of non-excitable cells. However, little is known about STIM1 in excitable cells, such as striated muscle, where the complement of calcium regulatory molecules is rather disparate from that of non-excitable cells. Here, we show that STIM1 is expressed in both myotubes and adult skeletal muscle. Myotubes lacking functional STIM1 fail to show SOC and fatigue rapidly. Moreover, mice lacking functional STIM1 die perinatally from a skeletal myopathy. In addition, STIM1 haploinsufficiency confers a contractile defect only under conditions where rapid refilling of stores would be needed. These findings provide insight into the role of STIM1 in skeletal muscle and suggest that STIM1 has a universal role as an ER/SR calcium sensor in both excitable and non-excitable cells.
AbstractList	It is now well established that stromal interaction molecule 1 (STIM1) is the calcium sensor of endoplasmic reticulum stores required to activate store-operated calcium entry (SOC) channels at the surface of non-excitable cells. However, little is known about STIM1 in excitable cells, such as striated muscle, where the complement of calcium regulatory molecules is rather disparate from that of non-excitable cells. Here, we show that STIM1 is expressed in both myotubes and adult skeletal muscle. Myotubes lacking functional STIM1 fail to show SOC and fatigue rapidly. Moreover, mice lacking functional STIM1 die perinatally from a skeletal myopathy. In addition, STIM1 haploinsufficiency confers a contractile defect only under conditions where rapid refilling of stores would be needed. These findings provide insight into the role of STIM1 in skeletal muscle and suggest that STIM1 has a universal role as an ER/SR calcium sensor in both excitable and non-excitable cells. It is now well established that stromal interaction molecule 1 (STIM1) is the calcium sensor of endoplasmic reticulum (ER) stores required to activate store-operated calcium entry (SOC) channels at the surface of non-excitable cells. Yet little is known about STIM1 in excitable cells such as striated muscle where the complement of calcium regulatory molecules is rather disparate from that of non-excitable cells. Here, we show that STIM1 is expressed in both myotubes and adult skeletal muscle. Myotubes lacking functional STIM1 fail to exhibit SOC and fatigue rapidly. Moreover, mice lacking functional STIM1 die perinatally from a skeletal myopathy. In addition, STIM1 haploinsufficiency confers a contractile defect only under conditions where rapid refilling of stores would be needed. These findings provide novel insight to the role of STIM1 in skeletal muscle and suggest that STIM1 has a universal role as an ER/SR calcium sensor in both excitable and non-excitable cells.
Audience	Academic
Author	Wang, Sunny Hawkins, April Finch, Elizabeth Ward, Cary C Eu, Jerry P Stiber, Jonathan Zhang, Zhu-Shan Graham, Victoria Williams, R. Sanders Seth, Malini Burch, Jarrett Malouf, Nadia Rosenberg, Paul
AuthorAffiliation	1 Department of Medicine, Duke University School of Medicine, Durham, NC 2 Department of Pathology, University of North Carolina, Chapel Hill, NC
AuthorAffiliation_xml	– name: 2 Department of Pathology, University of North Carolina, Chapel Hill, NC – name: 1 Department of Medicine, Duke University School of Medicine, Durham, NC
Author_xml	– givenname: April surname: Hawkins fullname: Hawkins, April organization: Department of Medicine, Duke University School of Medicine – givenname: Malini surname: Seth fullname: Seth, Malini organization: Department of Medicine, Duke University School of Medicine – givenname: Zhu-Shan surname: Zhang fullname: Zhang, Zhu-Shan organization: Department of Medicine, Duke University School of Medicine – givenname: Jonathan surname: Stiber fullname: Stiber, Jonathan organization: Department of Medicine, Duke University School of Medicine – givenname: Elizabeth surname: Finch fullname: Finch, Elizabeth organization: Department of Medicine, Duke University School of Medicine – givenname: Paul surname: Rosenberg fullname: Rosenberg, Paul organization: Department of Medicine, Duke University School of Medicine – givenname: R. Sanders surname: Williams fullname: Williams, R. Sanders organization: Department of Medicine, Duke University School of Medicine – givenname: Jarrett surname: Burch fullname: Burch, Jarrett organization: Department of Medicine, Duke University School of Medicine – givenname: Nadia surname: Malouf fullname: Malouf, Nadia organization: Department of Pathology, University of North Carolina – givenname: Sunny surname: Wang fullname: Wang, Sunny organization: Department of Medicine, Duke University School of Medicine – givenname: Victoria surname: Graham fullname: Graham, Victoria organization: Department of Medicine, Duke University School of Medicine – givenname: Cary C surname: Ward fullname: Ward, Cary C organization: Department of Medicine, Duke University School of Medicine – givenname: Jerry P surname: Eu fullname: Eu, Jerry P organization: Department of Medicine, Duke University School of Medicine
BackLink	https://www.ncbi.nlm.nih.gov/pubmed/18488020$$D View this record in MEDLINE/PubMed
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Snippet	It is now well established that stromal interaction molecule 1 (STIM1) is the calcium sensor of endoplasmic reticulum stores required to activate... It is now well established that stromal interaction molecule 1 (STIM1) is the calcium sensor of endoplasmic reticulum (ER) stores required to activate...
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SubjectTerms	Animals Biomedical and Life Sciences Calcium Calcium - metabolism Calcium channels Calcium Channels - metabolism Calcium Signaling Cancer Research Cell Biology Cell Line Developmental Biology Endoplasmic reticulum Fatigue Gene Silencing Life Sciences Membrane Glycoproteins - metabolism Membrane Glycoproteins - physiology Membrane proteins Mice Models, Biological Models, Genetic Muscle Contraction Muscles Muscles - metabolism Musculoskeletal system Patch-Clamp Techniques Physiological aspects Plasma Sarcoplasmic Reticulum - metabolism Sensors Signal Transduction Stem Cells Stromal Interaction Molecule 1
Title	STIM1 signalling controls store-operated calcium entry required for development and contractile function in skeletal muscle
URI	http://dx.doi.org/10.1038/ncb1731 https://link.springer.com/article/10.1038/ncb1731 https://www.ncbi.nlm.nih.gov/pubmed/18488020 https://www.proquest.com/docview/222296754 https://search.proquest.com/docview/20693984 https://search.proquest.com/docview/71630990 https://search.proquest.com/docview/856763563 https://pubmed.ncbi.nlm.nih.gov/PMC2694045
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