Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin-deficient muscle.

Utrophin binds laterally along actin filaments and can couple costameric actin with sarcolemma when overexpressed in dystrophin-deficient muscle.

Dystrophin is widely thought to mechanically link the cortical cytoskeleton with the muscle sarcolemma. Although the dystrophin homolog utrophin can functionally compensate for dystrophin in mice, recent studies question whether utrophin can bind laterally along actin filaments and anchor filaments...

Disgrifiad llawn

Manylion Llyfryddiaeth
Prif Awduron:	Rybakova, I, Patel, JR, Davies, K, Yurchenco, P, Ervasti, J
Fformat:	Journal article
Iaith:	English
Cyhoeddwyd:	2002

Eitemau Tebyg

Dystrophin and utrophin are functionally homologous actin binding proteins but act through distinct modes of filament association
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Cyhoeddwyd: (2001)

Biomechanical Properties of the Sarcolemma and Costameres of Skeletal Muscle Lacking Desmin
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Functional substitution by TAT-utrophin in dystrophin-deficient mice.
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Nitric Oxide and l-Arginine Cause an Accumulation of Utrophin at the Sarcolemma: A Possible Compensation for Dystrophin Loss in Duchenne Muscular Dystrophy
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Cyhoeddwyd: (2000)

The utrophin and dystrophin genes share similarities in genomic structure.
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Immunogold confirmation that utrophin is localized to the normal position of dystrophin in dystrophin-negative transgenic mouse muscle.
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Cyhoeddwyd: (2001)

The potential of utrophin and dystrophin combination therapies for Duchenne muscular dystrophy
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Cyhoeddwyd: (2019)

Histones bundle F-actin filaments and affect actin structure.
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Biased localization of actin binding proteins by actin filament conformation
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Cyhoeddwyd: (2020-11-01)

Confirmation by immunogold labeling that utrophin is localised to the normal position of dystrophin in dystrophin-negative transgenic mouse muscle
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Expression of dystrophin-glycoprotein complex at the skeletal muscle sarcolemma in Duchenne muscular dystrophy
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MODELING ACTIN FILAMENT ALIGNMENT
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Generation of clusters of dystrophin revertant fibers requires muscle regeneration and tests the function of dystrophin/utrophin transgenes
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Utrophin Compensates dystrophin Loss during Mouse Spermatogenesis
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Direct Visualization of Actin Filaments and Actin-Binding Proteins in Neuronal Cells
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Formin DAAM1 Organizes Actin Filaments in the Cytoplasmic Nodal Actin Network.
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ZZ domain is essentially required for the physiological binding of dystrophin and utrophin to beta-dystroglycan.
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Material properties of actin filament bundles
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Cytochalasans and Their Impact on Actin Filament Remodeling
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Visualizing Filamentous Actin in Chlamydomonas reinhardtii
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Dystrophin and utrophin influence fiber type composition and post-synaptic membrane structure.
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Piperazine Derivative Stabilizes Actin Filaments in Primary Fibroblasts and Binds G-Actin In Silico
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Cytokinesis requires localized β-actin filament production by an actin isoform specific nucleator
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Tissue-Specificity of Dystrophin–Actin Interactions: Isoform-Specific Thermodynamic Stability and Actin-Binding Function of Tandem Calponin-Homology Domains
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Alternative utrophin mRNAs contribute to phenotypic differences between dystrophin-deficient mice and Duchenne muscular dystrophy
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Nuclear actin filaments – a historical perspective
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Observation of Chloroplast-actin Filaments in Leaves of Arabidopsis
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Sarcolemmal nNOS anchoring reveals a qualitative difference between dystrophin and utrophin.
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Cyhoeddwyd: (2010)

Sarcolemmal nNOS anchoring reveals a qualitative difference between dystrophin and utrophin
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Marginal level dystrophin expression improves clinical outcome in a strain of dystrophin/utrophin double knockout mice.
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Cyhoeddwyd: (2010-12-01)