X-ray recordings reveal how a human disease-linked skeletal muscle α-actin mutation leads to contractile dysfunction

X-ray recordings reveal how a human disease-linked skeletal muscle α-actin mutation leads to... Journal of Structural Biology 192 (2015) 331–335 Contents lists available at ScienceDirect Journal of Structural Biology journal homepage: www.elsevier.com/locate/yjsbi X-ray recordings reveal how a human disease-linked skeletal muscle a-actin mutation leads to contractile dysfunction a,⇑ b b b c Julien Ochala , Gianina Ravenscroft , Elyshia McNamara , Kristen J. Nowak , Hiroyuki Iwamoto Centre of Human and Aerospace Physiological Sciences, School of Biomedical Sciences, King’s College London, London, United Kingdom Harry Perkins Institute of Medical Research, The University of Western Australia, Nedlands, Australia Japan Synchrotron Radiation Research Institute, SPring8, Hyogo, Japan article i nfo abstract Article history: In humans, mutant skeletal muscle a-actin proteins are associated with contractile dysfunction, skeletal Received 16 May 2015 muscle weakness and a wide range of primarily skeletal muscle diseases. Despite this knowledge, the Received in revised form 13 August 2015 exact molecular mechanisms triggering the contractile dysfunction remain unknown. Here, we aimed Accepted 22 September 2015 to unravel these. Hence, we used a transgenic mouse model expressing a well-described D286G mutant Available online 25 September 2015 skeletal muscle a-actin protein and recapitulating the human condition of contractile deregulation and severe skeletal muscle weakness. We then recorded and analyzed the small-angle X-ray diffraction http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Structural Biology Elsevier

X-ray recordings reveal how a human disease-linked skeletal muscle α-actin mutation leads to contractile dysfunction

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Publisher
Elsevier
Copyright
Copyright © 2015 Elsevier Inc.
ISSN
1047-8477
eISSN
1095-8657
D.O.I.
10.1016/j.jsb.2015.09.008
Publisher site
See Article on Publisher Site

Abstract

Journal of Structural Biology 192 (2015) 331–335 Contents lists available at ScienceDirect Journal of Structural Biology journal homepage: www.elsevier.com/locate/yjsbi X-ray recordings reveal how a human disease-linked skeletal muscle a-actin mutation leads to contractile dysfunction a,⇑ b b b c Julien Ochala , Gianina Ravenscroft , Elyshia McNamara , Kristen J. Nowak , Hiroyuki Iwamoto Centre of Human and Aerospace Physiological Sciences, School of Biomedical Sciences, King’s College London, London, United Kingdom Harry Perkins Institute of Medical Research, The University of Western Australia, Nedlands, Australia Japan Synchrotron Radiation Research Institute, SPring8, Hyogo, Japan article i nfo abstract Article history: In humans, mutant skeletal muscle a-actin proteins are associated with contractile dysfunction, skeletal Received 16 May 2015 muscle weakness and a wide range of primarily skeletal muscle diseases. Despite this knowledge, the Received in revised form 13 August 2015 exact molecular mechanisms triggering the contractile dysfunction remain unknown. Here, we aimed Accepted 22 September 2015 to unravel these. Hence, we used a transgenic mouse model expressing a well-described D286G mutant Available online 25 September 2015 skeletal muscle a-actin protein and recapitulating the human condition of contractile deregulation and severe skeletal muscle weakness. We then recorded and analyzed the small-angle X-ray diffraction

Journal

Journal of Structural BiologyElsevier

Published: Dec 1, 2015

References

  • Radial displacement of myosin cross-bridges in mouse myocardium due to ablation of myosin binding protein-C
    Colson, B.A.; Bekyarova, T.; Fitzsimons, D.P.; Irving, T.C.; Moss, R.L.
  • Actin structure and function
    Dominguez, R.; Holmes, K.C.
  • Evidence for unique structural change of thin filaments upon calcium activation of insect flight muscle
    Iwamoto, H.
  • X-ray diffraction evidence for the lack of stereospecific protein interactions in highly activated actomyosin complex
    Iwamoto, H.; Oiwa, K.; Suzuki, T.; Fujisawa, T.
  • States of thin filament regulatory proteins as revealed by combined cross-linking/X-ray diffraction techniques
    Iwamoto, H.; Oiwa, K.; Suzuki, T.; Fujisawa, T.

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