ArticleProceedings of the National Academy of Sciences of the United States of America2009
Assembly and dynamics of proteins of the longitudinal and junctional sarcoplasmic reticulum in skeletal muscle cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Development of a protein synthesis network at the sarco/endoplasmic reticulum in adult cardiac myocytes.The Journal of physiology · 2026Article
- Developmental endothelial locus 1: the present and future of an endogenous factor in vessels.Frontiers in physiology · 2024Review
- Histological Methods to Assess Skeletal Muscle Degeneration and Regeneration in Duchenne Muscular Dystrophy.International journal of molecular sciences · 2022Review
- The role of junctophilin proteins in cellular function.Physiological reviews · 2022Review
- Review
- The regulatory role of Myomaker and Myomixer-Myomerger-Minion in muscle development and regeneration.Cellular and molecular life sciences : CMLS · 2020Review
- Dynamics of triadin, a muscle-specific triad protein, within sarcoplasmic reticulum subdomains.Molecular biology of the cell · 2020Article
- Cored in the act: the use of models to understand core myopathies.Disease models & mechanisms · 2019Review
- Molecular determinants of homo- and heteromeric interactions of Junctophilin-1 at triads in adult skeletal muscle fibers.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The relationship between form and function throughout the history of excitation-contraction coupling.The Journal of general physiology · 2018Review
- Transport of the alpha subunit of the voltage gated L-type calcium channel through the sarcoplasmic reticulum occurs prior to localization to triads and requires the beta subunit but not Stac3 in skeletal muscles.Traffic (Copenhagen, Denmark) · 2017Article
- Organization of junctional sarcoplasmic reticulum proteins in skeletal muscle fibers.Journal of muscle research and cell motility · 2015Review
- N-WASP is required for Amphiphysin-2/BIN1-dependent nuclear positioning and triad organization in skeletal muscle and is involved in the pathophysiology of centronuclear myopathy.EMBO molecular medicine · 2014Article
- Obscurin is required for ankyrinB-dependent dystrophin localization and sarcolemma integrity.The Journal of cell biology · 2013Article
- A proteolytic cleavage to separate the sarcolemma/T-tubule from the sarcoplasmic reticulum.The Journal of physiology · 2013Article
- T-tubule biogenesis and triad formation in skeletal muscle and implication in human diseases.Skeletal muscle · 2011Article
- Transient receptor potential canonical type 1 (TRPC1) operates as a sarcoplasmic reticulum calcium leak channel in skeletal muscle.The Journal of biological chemistry · 2009Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The sarcoplasmic reticulum (SR) of skeletal muscle cells is a complex network of tubules and cisternae that share a common lumen delimited by a single continuous membrane. The SR contains longitudinal and junctional domains characterized by distinctive patterns of protein localization, but how SR proteins reach and/or are retained at these sites is not known. Here, we report that the organization of longitudinal SR proteins is a slow process characterized by temporally distinct patterns of protein localization. In contrast, junctional SR proteins rapidly and synchronously assembled into clusters which, however, merged into mature triadic junctions only after completion of longitudinal SR protein organization. Fluorescence recovery after photobleaching experiments indicated that SR organization was accompanied by significant changes in the dynamic properties of longitudinal and junctional proteins. The decrease in mobility that accompanied organization of the longitudinal SR proteins ank1.5-GFP and GFP-InsP3R1 was abrogated by deletion of specific binding sites for myofibrillar or cytoskeletal proteins, respectively. Assembly of junctional SR domains was accompanied by a strong decrease in mobility of junctional proteins that in triadin appeared to be mediated by its intraluminal region. Together, the data suggest that the organization of specific SR domains results from a process of membrane reorganization accompanied by the establishment of multiple protein-protein interactions with intrinsic and extrinsic cues.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.