UNC-98 and UNC-96 Interact with Paramyosin to Promote Its Incorporation into Thick Filaments of<i>Caenorhabditis elegans</i>

Miller, Rachel K.; Qadota, Hiroshi; Mercer, Kristina B.; Gernert, Kim M.; Benian, Guy M.

doi:10.1091/mbc.e07-07-0723

Cited by 10 publications

(24 citation statements)

References 31 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…First, recently synthesized paramyosin::GFP colocalizes with both wild-type and a mutant form of UNC-82. In wild type, paramyosin::GFP driven by a brief heat shock is detected at the M-line (Figure 3; Miller et al 2008), the site of UNC-82::GFP localization. This initial localization of paramyosin at the M-line may represent a staging area for thick filament components prior to incorporation into growing thick filaments.…”

Section: Discussionmentioning

confidence: 99%

“…Transgenic young adult animals were heat-shocked at 30°for 5 hr, and fluorescent images taken within 15 min of treatment. In wild type, the paramyosin::GFP fusion protein appeared in stripes at or near the M-line ( Figure 3E; Miller et al 2008). In the unc-82(0) background, paramyosin::GFP was seen in a patchy distribution throughout the muscle cell ( Figure 3F).…”

Section: Mutant Unc-82 E424k Colocalizes With Abnormal Paramyosin Accmentioning

confidence: 99%

“…Transgenic lines expressing hsp::UNC-15:: GFP were obtained by injecting a 200 ng/ml DNA cocktail containing a 1:100 ratio of the plasmid containing full-length UNC-15::GFP under the control of a heat-shock promoter (described in Miller et al 2008) to pRF4.…”

Section: Generation Of Transgenic Linesmentioning

confidence: 99%

“…Paramyosin aggregates that do not stain for either myosin A or B are found in unc-96 mutants (where aggregates also lack UNC-96), in unc-98 mutants (where aggregates also lack UNC-98/ZnF), and in unc-89(su75) (where aggregates also lack UNC-89/obscurin). Interestingly, like the accumulations in unc-82 missense mutants, the paramyosin accumulations in unc-96, unc-98/ZnF, and unc-89(su75)/obscurin mutants reside at the ends of the muscle cells Miller et al 2008;Qadota et al 2016). The extrachromosomal transgene phEx22 expressing UNC-82::GFP was crossed into these mutant lines.…”

Section: Overexpression Of Unc-82 In Paramyosin Mutantsmentioning

confidence: 99%

“…UNC-98/ZnF has been shown to bind to paramyosin, and has been proposed to promote the proper assembly of paramyosin into thick filaments (Miller et al 2008). It was therefore of interest to examine the localization of UNC-98/ZnF in unc-82 mutants.…”

Section: Localization Of Other M-line Proteins In Unc-82 Mutantsmentioning

confidence: 99%

See 4 more Smart Citations

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

Schiller¹,

Duchesneau²,

Lane³

et al. 2017

Genetics

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Mutant Unc-82 E424k Colocalizes With Abnormal Paramyosin Accmentioning

confidence: 99%

Section: Generation Of Transgenic Linesmentioning

confidence: 99%

Section: Overexpression Of Unc-82 In Paramyosin Mutantsmentioning

confidence: 99%

Section: Localization Of Other M-line Proteins In Unc-82 Mutantsmentioning

confidence: 99%

See 3 more Smart Citations

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

Schiller¹,

Duchesneau²,

Lane³

et al. 2017

Genetics

View full text Add to dashboard Cite

show abstract

Sequences in the myosin A rod interact with UNC‐89/obscurin and the zinc‐finger protein UNC‐98 during thick filament assembly and M‐line formation in C. elegans striated muscle

Almuhanna,

Oishi,

Lee

et al. 2024

Cytoskeleton

View full text Add to dashboard Cite

The M‐line of striated muscle is a complex structure that anchors myosin‐containing thick filaments and also participates in signaling and proteostasis. While the physical associations among many M‐line components have been defined, the mechanism of thick filament attachment is not completely understood. In Caenorhabditis elegans, myosin A is essential for viability and forms the site of M‐line attachment at the center of the filament, whereas myosin B forms the filament arms. Using a mutant myosin A that forms ectopic filaments, we examined interactions between myosin A and M‐line proteins in intact muscle cells. Ectopic myosin A recruits the giant kinase UNC‐89/obscurin, a presumed scaffolding protein, in an interaction that requires the zinc‐finger protein UNC‐98, but not UNC‐82/NUAK, UNC‐97/PINCH, or UNC‐96. In myosin A mutants, UNC‐89/obscurin patterning is highly defective in embryos and adults. A chimeric myosin containing 169 residues of the myosin A C‐terminal rod, coincident with the UNC‐98/ZnF binding site, is sufficient for colocalization of UNC‐89/obscurin and UNC‐98/ZnF in M‐line structures whereas a myosin chimera lacking these residues colocalizes with UNC‐89/obscurin in M‐lines that lack UNC‐98. Thus, at least two myosin A rod regions contribute independently to M‐line organization. We hypothesize that these M‐line‐organizing functions correspond to the essential “filament initiation function” performed by this isoform.

show abstract

RSU-1 regulates the integrity of dense bodies in muscle cells of aging Caenorhabditis elegans

Jiang,

Wang,

Zhang

et al. 2024

iScience

View full text Add to dashboard Cite

UNC-98 and UNC-96 Interact with Paramyosin to Promote Its Incorporation into Thick Filaments ofCaenorhabditis elegans

Cited by 10 publications

References 31 publications

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

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

Sequences in the myosin A rod interact with UNC‐89/obscurin and the zinc‐finger protein UNC‐98 during thick filament assembly and M‐line formation in C. elegans striated muscle

RSU-1 regulates the integrity of dense bodies in muscle cells of aging Caenorhabditis elegans

Contact Info

Product

Resources

About