ArticleHistochemistry and cell biology2009
Localization of ank1.5 in the sarcoplasmic reticulum precedes that of SERCA and RyR: relationship with the organization of obscurin in developing sarcomeres.
Article in Histochemistry and cell biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 21 citations in OpenAlex.
- The Sarcoplasmic Reticulum of Skeletal Muscle Cells: A Labyrinth of Membrane Contact Sites.Biomolecules · 2022Review
- Thick Filament Protein Network, Functions, and Disease Association.Comprehensive Physiology · 2018Review
- Exercise-induced alterations and loss of sarcomeric M-line organization in the diaphragm muscle of obscurin knockout mice.American journal of physiology. Cell physiology · 2017Article
- A novel type 2 diabetes risk allele increases the promoter activity of the muscle-specific small ankyrin 1 gene.Scientific reports · 2016Article
- Organization of junctional sarcoplasmic reticulum proteins in skeletal muscle fibers.Journal of muscle research and cell motility · 2015Review
- Obscurins: Goliaths and Davids take over non-muscle tissues.PloS one · 2014Article
- Obscurin is required for ankyrinB-dependent dystrophin localization and sarcolemma integrity.The Journal of cell biology · 2013Article
- Hydrophobic residues in small ankyrin 1 participate in binding to obscurin.Molecular membrane biology · 2012Article
- Integrity of the network sarcoplasmic reticulum in skeletal muscle requires small ankyrin 1.Journal of cell science · 2011Article
- Regulation of DMD pathology by an ankyrin-encoded miRNA.Skeletal muscle · 2011Article
- Extending the knowledge in histochemistry and cell biology.Histochemistry and cell biology · 2010Review
- Muscle giants: molecular scaffolds in sarcomerogenesis.Physiological reviews · 2009Review
- Assembly and dynamics of proteins of the longitudinal and junctional sarcoplasmic reticulum in skeletal muscle cells.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Ank1.5 is a muscle-specific isoform of ankyrin1 localized on the sarcoplasmic reticulum (SR) membrane that has been shown to interact with obscurin, a sarcomeric protein. We report here studies on the localization of obscurin and ank1.5 in embryonic and postnatal rodent skeletal muscles. Using two antibodies against epitopes in the N- and C-terminus of obscurin, two distinct patterns of localization were observed. Before birth, the antibodies against the N- and the C-terminus of obscurin stained the Z-disk and M-band, respectively. At the same time, ank1.5 was detected at the Z-disk, rising the possibility that obscurin molecules at M-band may not be able to interact with ank1.5. Localization of ank1.5 at Z-disks in E14 muscle fibers revealed that ank1.5 is among the earliest SR proteins to assemble, since its organization preceded that of other SR proteins, like SERCA and RyR. After birth, the antibody against the N-terminus of obscurin stained the M-band while that against the C-terminus stained both M-bands and the Z-disks. Starting from postnatal day 1, ank1.5 was found at the level of both M-bands and Z-disks. Altogether, from these results we infer that exposure of some obscurin epitopes changes during skeletal muscle development, resulting in distinct, antibody-specific, localization pattern. Why this occurs is not clear, yet these data indicate that the organization of obscurin at different locations in the sarcomere changes during muscle development and that this might affect the interaction with ank1.5.
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