Interaction of α-Catulin with Dystrobrevin Contributes to Integrity of Dystrophin Complex in Muscle

Oh, Hyun Ju; Abraham, Linu; Hengel, Jolanda van; Stove, Christophe; Prószyński, Tomasz J.; Gevaert, Kris; DiMario, Joseph X.; Sanes, Joshua R.; Roy, Frans van; Kim, Hongkyun

doi:10.1074/jbc.m112.369496

Cited by 19 publications

(20 citation statements)

References 44 publications

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“…S3A). This is in agreement with previous observations for α-catulin (Oh et al, 2012). Similar results were obtained after electroporation of GFP-fusion constructs into muscle tissues.…”

Section: Identification Of α-Dystrobrevin-1-interacting Proteinssupporting

confidence: 82%

“…The one protein from this group that we considered further was the deubiquitinating enzyme Usp9x (Théard et al, 2010), which was highly enriched in α-dystrobrevin-1 complexes (79 peptides recovered) and virtually missing in the control purification. The remaining eight proteins comprised six components of the DGC [three syntrophin isoforms, two dystrobrevin isoforms and utrophin (Sunada and Campbell, 1995)]; α-catulin, which we and others have previously shown to bind to α-dystrobrevin (Lyssand et al, 2010;Oh et al, 2012); and liprin-α1, a scaffold protein previously shown to interact with α-catulin (Lyssand et al, 2010;Spangler and Hoogenraad, 2007;Spangler et al, 2011) (Fig. 3B).…”

Section: Identification Of α-Dystrobrevin-1-interacting Proteinsmentioning

confidence: 99%

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α-Dystrobrevin-1 recruits Grb2 and α-catulin to organize neurotransmitter receptors at the neuromuscular junction

Gingras

Gawor

Bernadzki

et al. 2016

Journal of Cell Science

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Neuromuscular junctions (NMJs), the synapses made by motor neurons on muscle fibers, form during embryonic development but undergo substantial remodeling postnatally. Several lines of evidence suggest that α-dystrobrevin, a component of the dystrophinassociated glycoprotein complex (DGC), is a crucial regulator of the remodeling process and that tyrosine phosphorylation of one isoform, α-dystrobrevin-1, is required for its function at synapses. We identified a functionally important phosphorylation site on α-dystrobrevin-1, generated phosphorylation-specific antibodies to it and used them to demonstrate dramatic increases in phosphorylation during the remodeling period, as well as in nerve-dependent regulation in adults. We then identified proteins that bind to this site in a phosphorylation-dependent manner and others that bind to α-dystrobrevin-1 in a phosphorylation-independent manner. They include multiple members of the DGC, as well as α-catulin, liprin-α1, Usp9x, PI3K, Arhgef5 and Grb2. Finally, we show that two interactors, α-catulin ( phosphorylation independent) and Grb2 ( phosphorylation dependent) are localized to NMJs in vivo, and that they are required for proper organization of neurotransmitter receptors on myotubes.

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“…S3A). This is in agreement with previous observations for α-catulin (Oh et al, 2012). Similar results were obtained after electroporation of GFP-fusion constructs into muscle tissues.…”

Section: Identification Of α-Dystrobrevin-1-interacting Proteinssupporting

confidence: 82%

Section: Identification Of α-Dystrobrevin-1-interacting Proteinsmentioning

confidence: 99%

α-Dystrobrevin-1 recruits Grb2 and α-catulin to organize neurotransmitter receptors at the neuromuscular junction

Gingras

Gawor

Bernadzki

et al. 2016

Journal of Cell Science

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“…Exaggerated head bending has previously been observed by numerous independent research groups in mutants with loss-of-function mutations to dys-1 , the C. elegans ortholog of human Dystrophin, and to components of the Dystrophin associated protein complex (DAPC) (Fig. S1A) (Oh et al . 2012; Kim et al .…”

Section: Resultsmentioning

confidence: 83%

“…Dystrobrevin and syntrophin, which are components of the Dystrophin-associated protein complex, have C. elegans orthologs which interact with with C. elegans DYS-1 (Grisoni et al . 2003; Oh et al . 2012).…”

Section: Discussionmentioning

confidence: 99%

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Class I histone deacetylase HDA-3 is required for full maintenance of locomotor ability in Caenorhabditis elegans

Kawamura

Maruyama

2019

Preprint

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Locomotor ability declines with old age. A person’s capacity to maintain locomotor ability depends on genetic and environmental factors. Currently, the specific genetic factors that work to maintain locomotor ability are not well understood. Here we report the involvement of hda-3, encoding a class I histone deacetylase, as a specific genetic factor that contributes to the maintenance of locomotor ability in C. elegans. From a forward genetic approach, we identified a missense mutation in HDA-3 as the causative mutation for progressive decline in locomotor ability in one of the isolated strains. From transcriptome analysis, we found downregulated expression of two clusters of genes on Chromosome II and IV in this strain. Genes carrying CUB-like domains and genes carrying BATH domains were found on Chromosome II and IV, respectively. Knockdown of CUB-like genes, K08D8.5 and dod-17, and BATH genes, bath-1, bath-21 and bath-24 led to a progressive decline in locomotor ability. Our study identifies specific genetic factors that work to maintain locomotor ability and reveals potential targets for delaying age-related locomotor decline.

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Alpha‐Catulin Co‐Localizes With Vimentin Intermediate Filaments and Functions in Pulmonary Vascular Endothelial Cell Migration via ROCK

Bear

Liu

Abualkhair

et al. 2015

Journal Cellular Physiology

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The ubiquitous α-catulin acts as a scaffold for distinct signalosomes including RhoA/ROCK; however, its function is not well understood. While α-catulin has homology to the cytoskeletal linkers α-catenin and vinculin, it appears to be functionally divergent. Here we further investigated α-catulin function in pulmonary vascular endothelial cells (VEC) on the premise that α-catulin has a unique cytoskeletal role. Examination of endogenous α-catulin intracellular localization by immunofluorescence revealed a highly organized cytosolic filamentous network suggestive of a cytoskeletal system in a variety of cultured VEC. Double-immunofluorescence analyses of VEC showed endogenous α-catulin co-localization with vimentin intermediate filaments. Similar to vimentin, α-catulin was found to distribute into detergent-soluble and -insoluble fractions. Treatment of VEC with withaferinA, an agent that targets vimentin filaments, disrupted the α-catulin network distribution and altered α-catulin solubility. Vimentin participates in cell migration, and withaferinA was found to inhibit VEC migration in vitro; similarly, α-catulin knock-down reduced VEC migration. Based on previous reports showing that ROCK modulates vimentin, we found that ROCK depletion attenuated VEC migration; furthermore, α-catulin depletion was shown to reduce ROCK-induced signaling. These findings indicate that α-catulin has a unique function in co-localization with vimentin filaments that contributes to VEC migration via a pathway that may involve ROCK signaling. J. Cell. Physiol. 231: 934-943, 2016. © 2015 Wiley Periodicals, Inc.

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Interaction of α-Catulin with Dystrobrevin Contributes to Integrity of Dystrophin Complex in Muscle

Cited by 19 publications

References 44 publications

α-Dystrobrevin-1 recruits Grb2 and α-catulin to organize neurotransmitter receptors at the neuromuscular junction

α-Dystrobrevin-1 recruits Grb2 and α-catulin to organize neurotransmitter receptors at the neuromuscular junction

Class I histone deacetylase HDA-3 is required for full maintenance of locomotor ability in Caenorhabditis elegans

Alpha‐Catulin Co‐Localizes With Vimentin Intermediate Filaments and Functions in Pulmonary Vascular Endothelial Cell Migration via ROCK

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