Distinct Roles of Four Gelsolin-like Domains of <i>Caenorhabditis elegans</i> Gelsolin-like Protein-1 in Actin Filament Severing, Barbed End Capping, and Phosphoinositide Binding

Liu, Zhongmei; Klaavuniemi, Tuula; Ono, Shoichiro

doi:10.1021/bi100215b

Cited by 21 publications

(30 citation statements)

References 39 publications

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“…Direct observation of actin filaments by fluorescence microscopy DyLight549-labeled actin was prepared as described previously (Liu et al, 2010). G-actin (2 mM, 20% DyLight549 labeled) was mixed with 0.5 mM MBP, MBP-CAS-1, MBP-CAS-1N, or MBP-CAS-1C in the presence or absence of 1 mM UNC-60B in G-buffer and polymerized for 30 min at room temperature by addition of final 0.1 M KCl, 2 mM MgCl 2 , 1 mM EGTA, and 20 mM HepesNaOH, pH 7.5.…”

Section: Measurements Of Actin Turnover By Phosphate Releasementioning

confidence: 99%

CAS-1, a C. elegans cyclase-associated protein, is required for sarcomeric actin assembly in striated muscle

Nomura

Ono

2012

Journal of Cell Science

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SummaryAssembly of contractile apparatuses in striated muscle requires precisely regulated reorganization of the actin cytoskeletal proteins into sarcomeric organization. Regulation of actin filament dynamics is one of the essential processes of myofibril assembly, but the mechanism of actin regulation in striated muscle is not clearly understood. Actin depolymerizing factor (ADF)/cofilin is a key enhancer of actin filament dynamics in striated muscle in both vertebrates and nematodes. Here, we report that CAS-1, a cyclase-associated protein in Caenorhabditis elegans, promotes ADF/cofilin-dependent actin filament turnover in vitro and is required for sarcomeric actin organization in striated muscle. CAS-1 is predominantly expressed in striated muscle from embryos to adults. In vitro, CAS-1 binds to actin monomers and enhances exchange of actin-bound ATP/ADP even in the presence of UNC-60B, a muscle-specific ADF/cofilin that inhibits the nucleotide exchange. As a result, CAS-1 and UNC-60B cooperatively enhance actin filament turnover. The two proteins also cooperate to shorten actin filaments. A cas-1 mutation is homozygous lethal with defects in sarcomeric actin organization. cas-1-mutant embryos and worms have aggregates of actin in muscle cells, and UNC-60B is mislocalized to the aggregates. These results provide genetic and biochemical evidence that cyclase-associated protein is a critical regulator of sarcomeric actin organization in striated muscle.

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Section: Measurements Of Actin Turnover By Phosphate Releasementioning

confidence: 99%

CAS-1, a C. elegans cyclase-associated protein, is required for sarcomeric actin assembly in striated muscle

Nomura

Ono

2012

Journal of Cell Science

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“…These results suggested that each module of fascin has a different role in binding different molecules, including proteins and other organic compounds. Liu et al also reported that each gelsolin-like domain of Caenorhabditis elegans gelsolin, another actin binding protein, plays distinct roles in actin filament binding, severing, and capping, although amino acid sequences of the four gelsolin-like domains are highly homologous (33). The lack of cosedimentation of rLamC-ΔC and F-actin indicated that the fascin-like module of LamC could not bind to F-actin (Fig.…”

Section: Figmentioning

confidence: 96%

Functional Analysis of a Novel β-(1,3)-Glucanase from Corallococcus sp. Strain EGB Containing a Fascin-Like Module

Zhou

et al. 2017

Appl Environ Microbiol

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A novel ␤-(1,3)-glucanase gene designated lamC, cloned from Corallococcus sp. strain EGB, contains a fascin-like module and a glycoside hydrolase family 16 (GH16) catalytic module. LamC displays broad hydrolytic activity toward various polysaccharides. Analysis of the hydrolytic products revealed that LamC is an exoacting enzyme on ␤-(1,3)(1,3)-and ␤-(1,6)-linked glucan substrates and an endoacting enzyme on ␤-(1,4)-linked glucan and xylan substrates. Site-directed mutagenesis of conserved catalytic Glu residues (E304A and E309A) demonstrated that these activities were derived from the same active site. Excision of the fascin-like module resulted in decreased activity toward ␤-(1,3)(1,3)-linked glucans. The carbohydratebinding assay showed that the fascin-like module was a novel ␤-(1,3)-linked glucanbinding module. The functional characterization of the fascin-like module and catalytic module will help us better understand these enzymes and modules. -(1,3)-glucan, which is the main cell wall component in yeast and filamentous fungi and a structural polysaccharide (e.g., callose) in plants and is also found in exopolysaccharides produced by some bacteria (1). Based on their amino acid sequence similarity and secondary structure, ␤-(1,3)-glucanases are classified mainly into glycoside hydrolase family 16 (GH16) and GH17. However, these two families have the same hydrolytic mechanism with anomeric retention (2).Numerous genes encoding ␤-(1,3)-glucanase have been cloned and characterized from different sources, including varieties of plants (3-5), bacteria, and archaea, such as Bacillus circulans (6), Paenibacillus (7, 8), Thermotoga neapolitana (1), Rhodothermus marinus (9), and Pyrococcus furiosus (10). Few glucanases exhibit broad substrate linkage specificity, although Lafond et al. cloned a gene from Podospora anserina that encodes a broad-specificity ␤-glucanase acting on ␤-(1,3)-, ␤-(1,4)-, and ␤-(1,6)-glucans (11).Many polysaccharide-degrading enzymes display a modular structure, in which a catalytic module is attached to one or more noncatalytic modules (8, 12, 13). The impact of the noncatalytic modules on the enzymatic properties of ␤-(1,3)-glucanase

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“…However, unlike gelsolin, GSNL-1 remains bound to the side of actin filaments and does not nucleate actin polymerization (14). Analysis of the domainfunction relationship of GSNL-1 shows that G1 and the linker between G1 and G2 are sufficient for actin filament severing in a similar manner to the equivalent part of vertebrate gelsolin (15). However, an F-actin-binding site of GSNL-1 is present in G3-G4 (15), whereas G2 of vertebrate gelsolin binds to F-actin (16).…”

Section: Or Segments (G1-g6) a Ca 2ϩmentioning

confidence: 99%

“…Analysis of the domainfunction relationship of GSNL-1 shows that G1 and the linker between G1 and G2 are sufficient for actin filament severing in a similar manner to the equivalent part of vertebrate gelsolin (15). However, an F-actin-binding site of GSNL-1 is present in G3-G4 (15), whereas G2 of vertebrate gelsolin binds to F-actin (16). Moreover, the G1G2G3 fragment of GSNL-1 severs actin filaments in a Ca 2ϩ -dependent manner (15), whereas the equivalent fragments of vertebrate gelsolin exhibit Ca 2ϩ -independent actin-severing activity (17,18).…”

Section: Or Segments (G1-g6) a Ca 2ϩmentioning

confidence: 99%

“…However, an F-actin-binding site of GSNL-1 is present in G3-G4 (15), whereas G2 of vertebrate gelsolin binds to F-actin (16). Moreover, the G1G2G3 fragment of GSNL-1 severs actin filaments in a Ca 2ϩ -dependent manner (15), whereas the equivalent fragments of vertebrate gelsolin exhibit Ca 2ϩ -independent actin-severing activity (17,18). Because G4 of GSNL-1 is much shorter than G4 -G6 of gelsolin, the C terminus of GSNL-1 may not extend to G2 to function as a latch.…”

Section: Or Segments (G1-g6) a Ca 2ϩmentioning

confidence: 99%

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Calcium-sensitive Activity and Conformation of Caenorhabditis elegans Gelsolin-like Protein 1 Are Altered by Mutations in the First Gelsolin-like Domain

Liu

Kanzawa

Ono

2011

Journal of Biological Chemistry

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Background:The gelsolin family of actin-severing/capping proteins is calcium-regulated. Results: Two acidic residues of Caenorhabditis elegans gelsolin-like protein 1 (GSNL-1) were important for calcium regulation. Mutation at these residues sensitized GSNL-1 for calcium. Conclusion:The two acidic residues are important to maintain normal calcium sensitivity of GSNL-1. Significance: These residues are conserved, suggesting their importance in calcium regulation of the gelsolin family.

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Distinct Roles of Four Gelsolin-like Domains of Caenorhabditis elegans Gelsolin-like Protein-1 in Actin Filament Severing, Barbed End Capping, and Phosphoinositide Binding

Cited by 21 publications

References 39 publications

CAS-1, a C. elegans cyclase-associated protein, is required for sarcomeric actin assembly in striated muscle

CAS-1, a C. elegans cyclase-associated protein, is required for sarcomeric actin assembly in striated muscle

Functional Analysis of a Novel β-(1,3)-Glucanase from Corallococcus sp. Strain EGB Containing a Fascin-Like Module

Calcium-sensitive Activity and Conformation of Caenorhabditis elegans Gelsolin-like Protein 1 Are Altered by Mutations in the First Gelsolin-like Domain

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