An Alpha-Catulin Homologue Controls Neuromuscular Function through Localization of the Dystrophin Complex and BK Channels in Caenorhabditis elegans

Abraham, Linu; Oh, Hyun Ju; Sancar, Feyza; Richmond, Janet E.; Kim, Hongkyun

doi:10.1371/journal.pgen.1001077

Cited by 31 publications

(50 citation statements)

References 48 publications

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“…In these transgenic animals, we investigated the localization pattern of CTN-1 in muscle. We previously reported that CTN-1 and SLO-1 appear as puncta near dense bodies (16). Consistent with this report, the full-length CTN-1 exhibits a punctate pattern at the muscle membrane (Fig.…”

Section: Resultssupporting

confidence: 90%

“…This transgene rescues the headbending phenotype, indicating that CTN-1 localization in these transgenic animals reflects its normal in vivo localization. In wild-type animals CTN-1::GFP shows a punctate pattern as we reported previously (16). However, in both dys-1 and dyb-1 mutants, the punctate pattern of CTN-1::GFP disappeared (Fig.…”

Section: Resultssupporting

confidence: 82%

“…In a C. elegans forward genetic study that identifies mutants exhibiting abnormal localization of SLO-1 in muscle, we previously reported that mutations in ␣-catulin/ctn-1, encoding a putative cytoskeletal protein, cause a disruption of DAPC localization near dense bodies (16). Consistent with the idea that SLO-1 localization is controlled by the DAPC, we observed that mutations in ␣-catulin/ctn-1 disrupt SLO-1 localization as well.…”

supporting

confidence: 82%

“…Localization of Both CTN-1 and DYB-1 in C. elegans Muscle Is Interdependent-Previously, we showed that a ctn-1 mutation disrupts the localization of the DAPC; however, we were not able to identify the molecular link between CTN-1 and the DAPC (16). We now find that CTN-1 physically interacts with DYB-1, a component of the DAPC in muscle.…”

Section: Resultsmentioning

confidence: 59%

“…CTN-1 has three regions that have homology to ␣-catenin/vinculin, previously designated as the VH1 domain, the coiled-coil domain, and the VH2 domain (16,23). This domain organization as well as the overall sequence homology is similar to that of mammalian ␣-catulin.…”

Section: Resultsmentioning

confidence: 99%

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

Abraham

Hengel

et al. 2012

Journal of Biological Chemistry

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Background:The dystrophin complex stabilizes the cell membrane by linking the cytoskeletal network to the extracellular matrix. Results: ␣-Catulin interacts directly with dystrobrevin, a component of the dystrophin complex, in muscle. Conclusion:The interaction of ␣-catulin with dystrobrevin contributes to the integrity of the dystrophin complex in muscle. Significance: A molecular interaction potentially important for muscle pathogenesis is identified.

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Section: Resultssupporting

confidence: 90%

Section: Resultssupporting

confidence: 82%

supporting

confidence: 82%

Section: Resultsmentioning

confidence: 59%

Section: Resultsmentioning

confidence: 99%

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

Abraham

Hengel

et al. 2012

Journal of Biological Chemistry

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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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Slo1 deficiency impaired skeletal muscle regeneration and slow‐twitch fibre formation

Xia

Wang

Jiang

et al. 2023

J cachexia sarcopenia muscle

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Background It has been observed that Slo1 knockout mice have reduced motor function, and people with certain Slo1 mutations have movement problems, but there is no answer whether the movement disorder is caused by the loss of Slo1 in the nervous system, or skeletal muscle, or both. Here, to ascertain in which tissues Slo1 functions to regulate motor function and offer deeper insight in treating related movement disorder, we generated skeletal muscle‐specific Slo1 knockout mice, studied the functional changes in Slo1‐deficient skeletal muscle and explored the underlying mechanism. Methods We used skeletal muscle‐specific Slo1 knockout mice (Myf5‐Cre; Slo1flox/flox mice, called CKO) as in vivo models to examine the role of Slo1 in muscle growth and muscle regeneration. The forelimb grip strength test was used to assess skeletal muscle function and treadmill exhaustion test was used to test whole‐body endurance. Mouse primary myoblasts derived from CKO (myoblast/CKO) mice were used to extend the findings to in vitro effects on myoblast differentiation and fusion. Quantitative real‐time PCR, western blot and immunofluorescence approaches were used to analyse Slo1 expression during myoblast differentiation and muscle regeneration. To investigate the involvement of genes in the regulation of muscle dysfunction induced by Slo1 deletion, RNA‐seq analysis was performed in primary myoblasts. Immunoprecipitation and mass spectrometry were used to identify the protein interacting with Slo1. A dual‐luciferase reporter assay was used to identify whether Slo1 deletion affects NFAT activity. Results We found that the body weight and size of CKO mice were not significantly different from those of Slo1flox/flox mice (called WT). Deficiency of Slo1 in muscles leads to reduced endurance (~30% reduction, P < 0.05) and strength (~30% reduction, P < 0.001). Although there was no difference in the general morphology of the muscles, electron microscopy revealed a considerable reduction in the content of mitochondria in the soleus muscle (~40% reduction, P < 0.01). We found that Slo1 was expressed mainly on the cell membrane and showed higher expression in slow‐twitch fibres. Slo1 protein expression is progressively reduced during muscle postnatal development and regeneration after injury, and the expression is strongly reduced during myoblast differentiation. Slo1 deletion impaired myoblast differentiation and slow‐twitch fibre formation. Mechanistically, RNA‐seq analysis showed that Slo1 influences the expression of genes related to myogenic differentiation and slow‐twitch fibre formation. Slo1 interacts with FAK to influence myogenic differentiation, and Slo1 deletion diminishes NFAT activity. Conclusions Our data reveal that Slo1 deficiency impaired skeletal muscle regeneration and slow‐twitch fibre formation.

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An Alpha-Catulin Homologue Controls Neuromuscular Function through Localization of the Dystrophin Complex and BK Channels in Caenorhabditis elegans

Cited by 31 publications

References 48 publications

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

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

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

Slo1 deficiency impaired skeletal muscle regeneration and slow‐twitch fibre formation

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