Differential localization of two myosins within nematode thick filaments

Miller, David M.; Ortiz, Irving; Berliner, Gary C.; Epstein, Henry F.

doi:10.1016/0092-8674(83)90381-1

Cited by 293 publications

(310 citation statements)

References 46 publications

Supporting

Mentioning

294

Contrasting

Order By: Relevance

“…Previous studies by others have shown that the myoepithelial sheath cells express MYO-3 (myoA; Fig. 4A-C) and UNC-54 (myoB) myosin heavy chains (Ardizzi and Epstein, 1987) that are also expressed in the striated body wall muscle and that UNC-54 localizes to the outer regions, whereas MYO-3 is limited to the central part of the thick filaments (Rose et al, 1997) as observed in the thick filaments in the striated body wall muscle (Miller et al, 1983). UNC-15 paramyosin was also expressed in the myoepithelial sheath (Ardizzi and Epstein, 1987;Fig.…”

Section: Thick Filamentsmentioning

confidence: 74%

“…Anti-actin rabbit polyclonal antibody (AAN01) was purchased from Cytoskeleton, Inc. Anti-myoA (5-6; Miller et al, 1983) and antiparamyosin (5-23; Ardizzi and Epstein, 1987) mouse monoclonal antibodies were provided by Dr. Henry Epstein (University of Texas Medical Branch, Galveston, TX). Anti-PAT-3 ␤-integrin (MH25; Francis and Waterston, 1985), anti-DEB-1 vinculin (MH24; Francis and Waterston, 1985), anti-UNC-52 perlecan (MH2; Francis and Waterston, 1991) monoclonal antibodies were obtained from the Developmental Studies Hybridoma Bank (University of Iowa, Iowa City, IA).…”

Section: Antibodies and Fluorescent Probesmentioning

confidence: 99%

“…The myoepithelial sheath cells express MYO-3 and UNC-54 myosin heavy chains (Ardizzi and Epstein, 1987), which are also expressed in striated body wall muscle (Miller et al, 1983). Ovulation is perturbed by disturbing functions of several structural proteins, including MUP-2 troponin T (Myers et al, 1996), PAT-10 troponin C (Ono and Ono, 2004), LEV-11 tropomyosin (Ono and Ono, 2004), PAT-3 ␤-integrin , talin (Cram et al, 2003), PAT-4 integrin-linked kinase (Xu et al, 2006), and UNC-112 Mig-2 (Xu et al, 2006).…”

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Structural components of the nonstriated contractile apparatuses in the Caenorhabditis elegans gonadal myoepithelial sheath and their essential roles for ovulation

Ono

2007

Developmental Dynamics

View full text Add to dashboard Cite

Ovulation in the nematode Caenorhabditis elegans is regulated by complex signal transduction pathways and cell-cell interactions. Myoepithelial sheath cells of the proximal ovary are smooth muscle-like cells that provide contractile forces to push a mature oocyte into the spermatheca for fertilization. Although several genes that regulate sheath contraction have been characterized, basic components of the contractile apparatuses of the myoepithelial sheath have not been extensively studied. We identified major structural proteins of the contractile apparatuses of the myoepithelial sheath and characterized their nonstriated arrangement. Of interest, integrin and perlecan were found only at the dense bodies, whereas they localized to both dense bodies and M-lines in the striated body wall muscle. RNA interference of most of the myofibrillar components impaired ovulation in a soma-specific manner. Our results provide basic information that helps understanding the mechanism of sheath contraction during ovulation and establishing a new model to study morphogenesis of nonstriated muscle. Developmental Dynamics 236: 1093-1105, 2007.

show abstract

Section: Thick Filamentsmentioning

confidence: 74%

Section: Antibodies and Fluorescent Probesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Structural components of the nonstriated contractile apparatuses in the Caenorhabditis elegans gonadal myoepithelial sheath and their essential roles for ovulation

Ono

2007

Developmental Dynamics

View full text Add to dashboard Cite

show abstract

“…Myosin surrounds this core plus sheath structure. The myosin A isoform is located in the central (M-line) region of the thick filaments, and the myosin B isoform on the distal regions of the filament (Miller III et al, 1983;Epstein, 1985Epstein, , 1988Barral and Epstein, 1999;Müller et al, 2001). The myosin A and B isoforms always form homodimers (Schachat et al, 1977(Schachat et al, , 1978.…”

Section: 23mentioning

confidence: 99%

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Hooper

Hobbs

Thuma

2008

Progress in Neurobiology

128

View full text Add to dashboard Cite

This is the second in a series of canonical reviews on invertebrate muscle. We cover here thin and thick filament structure, the molecular basis of force generation and its regulation, and two special properties of some invertebrate muscle, catch and asynchronous muscle. Invertebrate thin filaments resemble vertebrate thin filaments, although helix structure and tropomyosin arrangement show small differences. Invertebrate thick filaments, alternatively, are very different from vertebrate striated thick filaments and show great variation within invertebrates. Part of this diversity stems from variation in paramyosin content, which is greatly increased in very large diameter invertebrate thick filaments. Other of it arises from relatively small changes in filament backbone structure, which results in filaments with grossly similar myosin head placements (rotating crowns of heads every 14.5 nm) but large changes in detail (distances between heads in azimuthal registration varying from three to thousands of crowns). The lever arm basis of force generation is common to both vetebrates and invertebrates, and in some invertebrates this process is understood on the near atomic level. Invertebrate actomyosin is both thin (tropomyosin:troponin) and thick (primarily via direct Ca ++ binding to myosin) filament regulated, and most invertebrate muscles are dually regulated. These mechanisms are well understood on the molecular level, but the behavioral utility of dual regulation is less so. The phosphorylation state of the thick filament associated giant protein, twitchin, has been recently shown to be the molecular basis of catch. The molecular basis of the stretch activation underlying asynchronous muscle activity, however, remains unresolved.

show abstract

“…Work on the body wall musculature of C . elegans indicates that the A and B MHC isoforms of the nematode are differentially incorporated into sarcomeres (Miller et al, 1983;Epstein et al, 1986;Epstein and Fischman, 1991). A study of the incorporation of actin monomers into myofibrils in vitro has shown that a-actin is more efficiently incorporated into sarcomeres than is (3-actin (Peng and Fischman, 1991).…”

Section: Significance Of the Differentiation Programmentioning

confidence: 99%

Identification of a program of contractile protein gene expression initiated upon skeletal muscle differentiation

Sutherland

Esser

Elsom

et al. 1993

Developmental Dynamics

View full text Add to dashboard Cite

The functional diversity of skeletal muscle is largely determined by the combinations of contractile protein isoforms that are expressed in different fibers. Just how the developmental expression of this large array of genes is regulated to give functional phenotypes is thus of great interest. In the present study, we perform a comprehensive analysis of contractile protein isoform mRNA profiles in skeletal muscle systems representing each generation of fiber formed: primary, secondary, and regenerating fibers. We find that in each system examined there is a common pattern of isoform gene expression during early differentiation for 5 of the 6 gene families we have investigated: myosin light chain (MLCI1, MLC2, tropomyosin, troponin (Tn)C, and TnI. We suggest that the common isoform patterns observed together represent a genetic program of skeletal muscle differentiation that is independent of the mature fiber phenotype and is found in all newly formed myotubes. Within each of these contractile protein gene families the program is independent of the isoforms of myosin heavy chain (MHC) expressed. The maintenance of such a program may reflect a specific requirement of the initial differentiation process. 0 1993 Wiley-Liss, Inc.

show abstract

Differential localization of two myosins within nematode thick filaments

Cited by 293 publications

References 46 publications

Structural components of the nonstriated contractile apparatuses in the Caenorhabditis elegans gonadal myoepithelial sheath and their essential roles for ovulation

Structural components of the nonstriated contractile apparatuses in the Caenorhabditis elegans gonadal myoepithelial sheath and their essential roles for ovulation

Invertebrate muscles: Thin and thick filament structure; molecular basis of contraction and its regulation, catch and asynchronous muscle

Identification of a program of contractile protein gene expression initiated upon skeletal muscle differentiation

Contact Info

Product

Resources

About