Development, structure, and maintenance of C. elegans body wall muscle

Gieseler, Kathrin; Qadota, Hiroshi; Benian, Guy M.

doi:10.1895/wormbook.1.81.2

Cited by 115 publications

(129 citation statements)

References 41 publications

(129 reference statements)

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“…Within the sarcomere at the level of the M-band, mammalian obscurins interact with titin, myomesin, ankyrin-B, Ras homolog gene family, member A (RhoA), and slow skeletal myosin binding protein C variant 1 (sMyBP-Cv1) (Perry et al 2013). In C. elegans at the M-band, UNC-89 interacts with copine domain protein atypical-1 (CPNA-1), UNC-15 (paramyosin), small CTD-phosphatase-like-1 (SCPL-1), four and a half LIM domains protein 9 (LIM9/FHL), maternal effect lethal 26 (MEL-26), and Rho1 (Gieseler et al 2016;Qadota et al 2008a, b;Warner et al 2013;Wilson et al 2012) and Drosophila obscurins interact with Ball and multiple ankyrin repeats single KH domain (MASK) at the M-band (Katzemich et al 2015). In addition, mammalian obscurins interact with the NH 2 -terminus of titin and Ran-binding protein 9 (RanBP9) at Z-discs (Bowman et al 2008), small ankyrin-1 at the SR , and ankyrin-B at costameres (Randazzo et al 2013).…”

Section: Varied Ligands Of Obscurinsmentioning

confidence: 99%

Obscure functions: the location–function relationship of obscurins

2017

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The obscurin family of polypeptides is essential for normal striated muscle function and contributes to the pathogenesis of fatal diseases, including cardiomyopathies and cancers. The single mammalian obscurin gene, OBSCN, gives rise to giant (∼800 kDa) and smaller (∼40-500 kDa) proteins that are composed of tandem adhesion and signaling motifs. Mammalian obscurin proteins are expressed in a variety of cell types, including striated muscles, and localize to distinct subcellular compartments where they contribute to diverse cellular processes. Obscurin homologs in Caenorhabditis elegans and Drosophila possess a similar domain architecture and are also expressed in striated muscles. The long sought after question, "what does obscurin do?" is complex and cannot be addressed without taking into consideration the subcellular distribution of these proteins and local isoform concentration. Herein, we present an overview of the functions of obscurins and begin to define the intricate relationship between their subcellular distributions and functions in striated muscles.

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Section: Varied Ligands Of Obscurinsmentioning

confidence: 99%

Obscure functions: the location–function relationship of obscurins

2017

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“…The thin filaments are attached to the dense bodies (Z-disk analogs, not line but “dot” or “finger” like structures), and the thick filaments are organized around M-lines. Moreover, all the dense bodies and M-lines are anchored to the muscle cell membrane and extracellular matrix (ECM, basement membrane), which is attached to the hypodermis and thus to the cuticle [Waterston, 1988; Moerman and Fire, 1997; Moerman and Williams, 2006; Gieseler et al, 2016;]. This allows the force of muscle contraction to be transmitted directly to the cuticle and allows movement of the whole animal.…”

Section: Introductionmentioning

confidence: 99%

“…Many of the proteins of myofilaments, attachment structures, and regulators of contraction/relaxation have been identified through genetic and molecular biological analyses, and characterized cell biologically by using specific antibodies and GFP fusion proteins [Moerman and Fire, 1997; Qadota and Benian, 2010; Gieseler et al, 2016]. For C. elegans muscle, electron microscopy images are also available [Waterston et al, 1980; Zengel and Epstein, 1980; Waterston, 1988; Gieseler et al, 2016].…”

Section: Introductionmentioning

confidence: 99%

“…For C. elegans muscle, electron microscopy images are also available [Waterston et al, 1980; Zengel and Epstein, 1980; Waterston, 1988; Gieseler et al, 2016]. However, since conventional fluorescence microscopy has limited resolution (~250 nm in the x-y plane) and EM provides too narrow a view, whole muscle three-dimensional structure is difficult to perceive in single images.…”

Section: Introductionmentioning

confidence: 99%

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High‐resolution imaging of muscle attachment structures in Caenorhabditis elegans

et al. 2017

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We used structured illumination microscopy (SIM) to obtain super-resolution images of muscle attachment structures in C. elegans striated muscle. SIM imaging of M-line components revealed two patterns: PAT-3 (β-integrin) and proteins that interact in a complex with the cytoplasmic tail of β-integrin and localize to the basal muscle cell membrane (UNC-112 (kindlin), PAT-4 (ILK), UNC-97 (PINCH), PAT-6 (α-parvin) and UNC-95), are found in discrete, angled segments with gaps. In contrast, proteins localized throughout the depth of the M-line (UNC-89 (obscurin) and UNC-98) are imaged as continuous lines. Systematic immunostaining of muscle cell boundaries revealed that dense body components close to the basal muscle cell membrane also localize at cell boundaries. SIM imaging of muscle cell boundaries reveal “zipper-like” structures. Electron micrographs reveal electron dense material similar in appearance to dense bodies located adjacent to the basolateral cell membranes of adjacent muscle cells separated by ECM. Moreover, by EM, there are a variety of features of the muscle cell boundaries that help explain the zipper-like pattern of muscle protein localization observed by SIM. Short dense bodies in atn-1 mutants that are null for α-actinin and lack the deeper extensions of dense bodies, showed “zipper-like” structures by SIM similar to cell boundary structures, further indicating that the surface-proximal components of dense bodies form the “zipper-like” structures at cell boundaries. Moreover, mutants in thin and thick filament components do not have “dot-like” dense bodies, suggesting that myofilament tension is required for assembly or maintenance of proper dense body shape.

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“…The M-line, the site of thick filament attachment, comprises many structural and probable signaling proteins (reviewed in Qadota and Benian 2010;Gieseler et al 2016). UNC-89/ obscurin is a very large protein with many functional domains that is found at the M-line.…”

mentioning

confidence: 99%

The Role of the UNC-82 Protein Kinase in Organizing Myosin Filaments in Striated Muscle ofCaenorhabditis elegans

Schiller¹,

Duchesneau²,

Lane³

et al. 2017

Genetics

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We study the mechanisms that guide the formation and maintenance of the highly ordered actin-myosin cytoskeleton in striated muscle. The UNC-82 kinase of Caenorhabditis elegans is orthologous to mammalian kinases ARK5/NUAK1 and SNARK/ NUAK2. UNC-82 localizes to the M-line, and is required for proper organization of thick filaments, but its substrate and mechanism of action are unknown. Antibody staining of three mutants with missense mutations in the UNC-82 catalytic domain revealed muscle structure that is less disorganized than in the null unc-82(0), but contained distinctive ectopic accumulations not found in unc-82(0). These accumulations contain paramyosin and myosin B, but lack myosin A and myosin A-associated proteins, as well as proteins of the integrin-associated complex. Fluorescently tagged missense mutant protein UNC-82 E424K localized normally in wild type; however, in unc-82(0), the tagged protein was found in the ectopic accumulations, which we also show to label with recently synthesized paramyosin. Recruitment of wild-type UNC-82::GFP to aggregates of differing protein composition in five muscle-affecting mutants revealed that colocalization of UNC-82 and paramyosin does not require UNC-96, UNC-98/ZnF, UNC-89/obscurin, CSN-5, myosin A, or myosin B individually. Dosage effects in paramyosin mutants suggest that UNC-82 acts as part of a complex, in which its stoichiometric relationship with paramyosin is critical. UNC-82 dosage affects muscle organization in the absence of paramyosin, perhaps through myosin B. We present evidence that the interaction of UNC-98/ZnF with myosin A is independent of UNC-82, and that UNC-82 acts upstream of UNC-98/ZnF in a pathway that organizes paramyosin during thick filament assembly.

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Development, structure, and maintenance of C. elegans body wall muscle

Cited by 115 publications

References 41 publications

Obscure functions: the location–function relationship of obscurins

Obscure functions: the location–function relationship of obscurins

High‐resolution imaging of muscle attachment structures in Caenorhabditis elegans

The Role of the UNC-82 Protein Kinase in Organizing Myosin Filaments in Striated Muscle ofCaenorhabditis elegans

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