ArticleMolecular biology of the cell2000
A nonerythroid isoform of protein 4.1R interacts with components of the contractile apparatus in skeletal myofibers.
Article in Molecular biology of the cell, 2000. 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.
- MYH7 in cardiomyopathy and skeletal muscle myopathy.Molecular and cellular biochemistry · 2024Review
- Epithelial-specific isoforms of protein 4.1R promote adherens junction assembly in maturing epithelia.The Journal of biological chemistry · 2020Article
- Thick Filament Protein Network, Functions, and Disease Association.Comprehensive Physiology · 2018Review
- Protein 4.1R Exon 16 3' Splice Site Activation Requires Coordination among TIA1, Pcbp1, and RBM39 during Terminal Erythropoiesis.Molecular and cellular biology · 2017Article
- Protein 4.1R Influences Myogenin Protein Stability and Skeletal Muscle Differentiation.The Journal of biological chemistry · 2016Article
- Identification of Small Ankyrin 1 as a Novel Sarco(endo)plasmic Reticulum Ca2+-ATPase 1 (SERCA1) Regulatory Protein in Skeletal Muscle.The Journal of biological chemistry · 2015Article
- Giant axon formation in mice lacking Kell, XK, or Kell and XK: animal models of McLeod neuroacanthocytosis syndrome.The American journal of pathology · 2014Article
- Structural protein 4.1R is integrally involved in nuclear envelope protein localization, centrosome-nucleus association and transcriptional signaling.Journal of cell science · 2011Article
- An internal ribosome entry site element directs the synthesis of the 80 kDa isoforms of protein 4.1R.BMC biology · 2008Article
- Protein 4.1R self-association: identification of the binding domain.The Biochemical journal · 2006Article
- Cardiac muscle cell cytoskeletal protein 4.1: analysis of transcripts and subcellular location--relevance to membrane integrity, microstructure, and possible role in heart failure.Mammalian genome : official journal of the International Mammalian Genome Society · 2005Article
- Mitotic regulation of protein 4.1R involves phosphorylation by cdc2 kinase.Molecular biology of the cell · 2005Article
- Obscurin is a ligand for small ankyrin 1 in skeletal muscle.Molecular biology of the cell · 2003Article
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Authors and funding
3 authors.
Funding
Abstract
The approximately 80-kDa erythroid 4.1R protein is a major component of the erythrocyte cytoskeleton, where it links transmembrane proteins to the underlying spectrin/actin complexes. A diverse collection of 4.1R isoforms has been described in nonerythroid cells, ranging from approximately 30 to approximately 210 kDa. In the current study, we identified the number and primary structure of 4.1R isoforms expressed in adult skeletal muscle and characterized the localization patterns of 4.1R message and protein. Skeletal muscle 4.1R appears to originate solely from the upstream translation initiation codon (AUG-1) residing in exon 2'. Combinations of alternatively spliced downstream exons generate an array of distinct 4.1R spliceoforms. Two major isoform classes of approximately 105/110 and approximately 135 kDa are present in muscle homogenates. 4.1R transcripts are distributed in highly ordered signal stripes, whereas 4.1R protein(s) decorate the sarcoplasm in transverse striations that are in register with A-bands. An approximately 105/110-kDa 4.1R isoform appears to occur in vivo in a supramolecular complex with major sarcomeric proteins, including myosin, alpha-actin, and alpha-tropomyosin. In vitro binding assays showed that 4.1R may interact directly with the aforementioned contractile proteins through its 10-kDa domain. All of these observations suggest a topological model whereby 4.1R may play a scaffolding role by anchoring the actomyosin myofilaments and possibly modulating their displacements during contraction/relaxation.
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