ArticleThe Journal of cell biology1998
MKBP, a novel member of the small heat shock protein family, binds and activates the myotonic dystrophy protein kinase.
Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 136 citations in OpenAlex.
- Small heat shock proteins and biomolecular condensates.Cellular and molecular life sciences : CMLS · 2026Review
- Differentially Expressed Genes Regulating Glutathione Metabolism, Protein-Folding, and Unfolded Protein Response in Pancreatic β-Cells in Type 2 Diabetes Mellitus.International journal of molecular sciences · 2023Article
- The Role of Small Heat Shock Proteins in Protein Misfolding Associated Motoneuron Diseases.International journal of molecular sciences · 2022Review
- High mRNA Expression Levels of Heat Shock Protein Family B Member 2 (International journal of molecular sciences · 2022Article
- Minimal Yet Powerful: The Role of Archaeal Small Heat Shock Proteins in Maintaining Protein Homeostasis.Frontiers in molecular biosciences · 2022Review
- Insights on Human Small Heat Shock Proteins and Their Alterations in Diseases.Frontiers in molecular biosciences · 2022Review
- Elucidation of Diverse Physico-Chemical Parameters in Mammalian Small Heat Shock Proteins: A Comprehensive Classification and Structural and Functional Exploration Using In Silico Approach.Applied biochemistry and biotechnology · 2021Article
- The Heterooligomerization of Human Small Heat Shock Proteins Is Controlled by Conserved Motif Located in the N-Terminal Domain.International journal of molecular sciences · 2020Article
- Neuromuscular Diseases Due to Chaperone Mutations: A Review and Some New Results.International journal of molecular sciences · 2020Review
- The growing world of small heat shock proteins: from structure to functions.Cell stress & chaperones · 2017Review
- The protective role of small heat shock proteins in cardiac diseases: key role in atrial fibrillation.Cell stress & chaperones · 2017Review
- αB-crystallin and HspB2 deficiency is protective from diet-induced glucose intolerance.Genomics data · 2016Article
- Article
- Muscle wasting in myotonic dystrophies: a model of premature aging.Frontiers in aging neuroscience · 2015Review
- Different anti-aggregation and pro-degradative functions of the members of the mammalian sHSP family in neurological disorders.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Review
- Heterooligomeric complexes of human small heat shock proteins.Cell stress & chaperones · 2012Article
- HspB2/myotonic dystrophy protein kinase binding protein (MKBP) as a novel molecular chaperone: structural and functional aspects.PloS one · 2012Article
- HSPB2 is dispensable for the cardiac hypertrophic response but reduces mitochondrial energetics following pressure overload in mice.PloS one · 2012Article
- The small heat shock protein HspB2 is a novel anti-apoptotic protein that inhibits apical caspase activation in the extrinsic apoptotic pathway.Breast cancer research and treatment · 2010Article
- An examination of alpha B-crystallin as a modifier of SOD1 aggregate pathology and toxicity in models of familial amyotrophic lateral sclerosis.Journal of neurochemistry · 2010Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Muscle cells are frequently subjected to severe conditions caused by heat, oxidative, and mechanical stresses. The small heat shock proteins (sHSPs) such as alphaB-crystallin and HSP27, which are highly expressed in muscle cells, have been suggested to play roles in maintaining myofibrillar integrity against such stresses. Here, we identified a novel member of the sHSP family that associates specifically with myotonic dystrophy protein kinase (DMPK). This DMPK-binding protein, MKBP, shows a unique nature compared with other known sHSPs: (a) In muscle cytosol, MKBP exists as an oligomeric complex separate from the complex formed by alphaB-crystallin and HSP27. (b) The expression of MKBP is not induced by heat shock, although it shows the characteristic early response of redistribution to the insoluble fraction like other sHSPs. Immunohistochemical analysis of skeletal muscle cells shows that MKBP localizes to the cross sections of individual myofibrils at the Z-membrane as well as the neuromuscular junction, where DMPK has been suggested to be concentrated. In vitro, MKBP enhances the kinase activity of DMPK and protects it from heat-induced inactivation. These results suggest that MKBP constitutes a novel stress-responsive system independent of other known sHSPs in muscle cells and that DMPK may be involved in this system by being activated by MKBP. Importantly, since the amount of MKBP protein, but not that of other sHSP family member proteins, is selectively upregulated in skeletal muscle from DM patients, an interaction between DMPK and MKBP may be involved in the pathogenesis of DM.
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