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Jeffrey S. Simske - One of the best experts on this subject based on the ideXlab platform.

  • the minus end actin capping protein unc 94 tropomodulin regulates development of the caenorhabditis elegans intestine
    Developmental Dynamics, 2014
    Co-Authors: Elisabeth Coxpaulson, Vincent L. Cannataro, Thomas Gallagher, Corey M. Hoffman, Gary Mantione, Matthew Mcintosh, Malan Silva, Nicole Vissichelli, Rachel Walker, Jeffrey S. Simske
    Abstract:

    Background: Tropomodulins are actin-capping proteins that regulate the stability of the slow-growing, minus-ends of actin filaments. The C. elegans tropomodulin homolog, UNC-94, has sequence and functional similarity to vertebrate tropomodulins. We investigated the role of UNC-94 in C. elegans intestinal morphogenesis. Results: In the embryonic C. elegans intestine, UNC-94 localizes to the Terminal Web, an actin- and intermediate filament-rich structure that underlies the apical membrane. Loss of UNC-94 function results in areas of flattened intestinal lumen. In worms homozygous for the strong loss-of-function allele, unc-94(tm724), the Terminal Web is thinner and the amount of F-actin is reduced, pointing to a role for UNC-94 in regulating the structure of the Terminal Web. The non-muscle myosin, NMY-1, also localizes to the Terminal Web, and we present evidence that increasing actomyosin contractility by depleting the myosin phosphatase regulatory subunit, mel-11, can rescue the flattened lumen phenotype of unc-94 mutants. Conclusions: The data support a model in which minus-end actin capping by UNC-94 promotes proper F-actin structure and contraction in the Terminal Web, yielding proper shape of the intestinal lumen. This establishes a new role for a tropomodulin in regulating lumen shape during tubulogenesis. Developmental Dynamics 243:753–764, 2014. V C 2014 Wiley Periodicals, Inc.

  • The Minus-End Actin Capping Protein, UNC-94/Tropomodulin, Regulates Development of the Caenorhabditis elegans Intestine
    Developmental Dynamics, 2014
    Co-Authors: Elisabeth Cox-paulson, Vincent L. Cannataro, Thomas Gallagher, Corey M. Hoffman, Gary Mantione, Matthew Mcintosh, Malan Silva, Nicole Vissichelli, Rachel L. Walker, Jeffrey S. Simske
    Abstract:

    Background: Tropomodulins are actin-capping proteins that regulate the stability of the slow-growing, minus-ends of actin filaments. The C. elegans tropomodulin homolog, UNC-94, has sequence and functional similarity to vertebrate tropomodulins. We investigated the role of UNC-94 in C. elegans intestinal morphogenesis. Results: In the embryonic C. elegans intestine, UNC-94 localizes to the Terminal Web, an actin- and intermediate filament-rich structure that underlies the apical membrane. Loss of UNC-94 function results in areas of flattened intestinal lumen. In worms homozygous for the strong loss-of-function allele, unc-94(tm724), the Terminal Web is thinner and the amount of F-actin is reduced, pointing to a role for UNC-94 in regulating the structure of the Terminal Web. The non-muscle myosin, NMY-1, also localizes to the Terminal Web, and we present evidence that increasing actomyosin contractility by depleting the myosin phosphatase regulatory subunit, mel-11, can rescue the flattened lumen phenotype of unc-94 mutants. Conclusions: The data support a model in which minus-end actin capping by UNC-94 promotes proper F-actin structure and contraction in the Terminal Web, yielding proper shape of the intestinal lumen. This establishes a new role for a tropomodulin in regulating lumen shape during tubulogenesis. Developmental Dynamics 243:753–764, 2014. V C 2014 Wiley Periodicals, Inc.

Gary Mantione - One of the best experts on this subject based on the ideXlab platform.

  • the minus end actin capping protein unc 94 tropomodulin regulates development of the caenorhabditis elegans intestine
    Developmental Dynamics, 2014
    Co-Authors: Elisabeth Coxpaulson, Vincent L. Cannataro, Thomas Gallagher, Corey M. Hoffman, Gary Mantione, Matthew Mcintosh, Malan Silva, Nicole Vissichelli, Rachel Walker, Jeffrey S. Simske
    Abstract:

    Background: Tropomodulins are actin-capping proteins that regulate the stability of the slow-growing, minus-ends of actin filaments. The C. elegans tropomodulin homolog, UNC-94, has sequence and functional similarity to vertebrate tropomodulins. We investigated the role of UNC-94 in C. elegans intestinal morphogenesis. Results: In the embryonic C. elegans intestine, UNC-94 localizes to the Terminal Web, an actin- and intermediate filament-rich structure that underlies the apical membrane. Loss of UNC-94 function results in areas of flattened intestinal lumen. In worms homozygous for the strong loss-of-function allele, unc-94(tm724), the Terminal Web is thinner and the amount of F-actin is reduced, pointing to a role for UNC-94 in regulating the structure of the Terminal Web. The non-muscle myosin, NMY-1, also localizes to the Terminal Web, and we present evidence that increasing actomyosin contractility by depleting the myosin phosphatase regulatory subunit, mel-11, can rescue the flattened lumen phenotype of unc-94 mutants. Conclusions: The data support a model in which minus-end actin capping by UNC-94 promotes proper F-actin structure and contraction in the Terminal Web, yielding proper shape of the intestinal lumen. This establishes a new role for a tropomodulin in regulating lumen shape during tubulogenesis. Developmental Dynamics 243:753–764, 2014. V C 2014 Wiley Periodicals, Inc.

  • The Minus-End Actin Capping Protein, UNC-94/Tropomodulin, Regulates Development of the Caenorhabditis elegans Intestine
    Developmental Dynamics, 2014
    Co-Authors: Elisabeth Cox-paulson, Vincent L. Cannataro, Thomas Gallagher, Corey M. Hoffman, Gary Mantione, Matthew Mcintosh, Malan Silva, Nicole Vissichelli, Rachel L. Walker, Jeffrey S. Simske
    Abstract:

    Background: Tropomodulins are actin-capping proteins that regulate the stability of the slow-growing, minus-ends of actin filaments. The C. elegans tropomodulin homolog, UNC-94, has sequence and functional similarity to vertebrate tropomodulins. We investigated the role of UNC-94 in C. elegans intestinal morphogenesis. Results: In the embryonic C. elegans intestine, UNC-94 localizes to the Terminal Web, an actin- and intermediate filament-rich structure that underlies the apical membrane. Loss of UNC-94 function results in areas of flattened intestinal lumen. In worms homozygous for the strong loss-of-function allele, unc-94(tm724), the Terminal Web is thinner and the amount of F-actin is reduced, pointing to a role for UNC-94 in regulating the structure of the Terminal Web. The non-muscle myosin, NMY-1, also localizes to the Terminal Web, and we present evidence that increasing actomyosin contractility by depleting the myosin phosphatase regulatory subunit, mel-11, can rescue the flattened lumen phenotype of unc-94 mutants. Conclusions: The data support a model in which minus-end actin capping by UNC-94 promotes proper F-actin structure and contraction in the Terminal Web, yielding proper shape of the intestinal lumen. This establishes a new role for a tropomodulin in regulating lumen shape during tubulogenesis. Developmental Dynamics 243:753–764, 2014. V C 2014 Wiley Periodicals, Inc.

Vincent L. Cannataro - One of the best experts on this subject based on the ideXlab platform.

  • the minus end actin capping protein unc 94 tropomodulin regulates development of the caenorhabditis elegans intestine
    Developmental Dynamics, 2014
    Co-Authors: Elisabeth Coxpaulson, Vincent L. Cannataro, Thomas Gallagher, Corey M. Hoffman, Gary Mantione, Matthew Mcintosh, Malan Silva, Nicole Vissichelli, Rachel Walker, Jeffrey S. Simske
    Abstract:

    Background: Tropomodulins are actin-capping proteins that regulate the stability of the slow-growing, minus-ends of actin filaments. The C. elegans tropomodulin homolog, UNC-94, has sequence and functional similarity to vertebrate tropomodulins. We investigated the role of UNC-94 in C. elegans intestinal morphogenesis. Results: In the embryonic C. elegans intestine, UNC-94 localizes to the Terminal Web, an actin- and intermediate filament-rich structure that underlies the apical membrane. Loss of UNC-94 function results in areas of flattened intestinal lumen. In worms homozygous for the strong loss-of-function allele, unc-94(tm724), the Terminal Web is thinner and the amount of F-actin is reduced, pointing to a role for UNC-94 in regulating the structure of the Terminal Web. The non-muscle myosin, NMY-1, also localizes to the Terminal Web, and we present evidence that increasing actomyosin contractility by depleting the myosin phosphatase regulatory subunit, mel-11, can rescue the flattened lumen phenotype of unc-94 mutants. Conclusions: The data support a model in which minus-end actin capping by UNC-94 promotes proper F-actin structure and contraction in the Terminal Web, yielding proper shape of the intestinal lumen. This establishes a new role for a tropomodulin in regulating lumen shape during tubulogenesis. Developmental Dynamics 243:753–764, 2014. V C 2014 Wiley Periodicals, Inc.

  • The Minus-End Actin Capping Protein, UNC-94/Tropomodulin, Regulates Development of the Caenorhabditis elegans Intestine
    Developmental Dynamics, 2014
    Co-Authors: Elisabeth Cox-paulson, Vincent L. Cannataro, Thomas Gallagher, Corey M. Hoffman, Gary Mantione, Matthew Mcintosh, Malan Silva, Nicole Vissichelli, Rachel L. Walker, Jeffrey S. Simske
    Abstract:

    Background: Tropomodulins are actin-capping proteins that regulate the stability of the slow-growing, minus-ends of actin filaments. The C. elegans tropomodulin homolog, UNC-94, has sequence and functional similarity to vertebrate tropomodulins. We investigated the role of UNC-94 in C. elegans intestinal morphogenesis. Results: In the embryonic C. elegans intestine, UNC-94 localizes to the Terminal Web, an actin- and intermediate filament-rich structure that underlies the apical membrane. Loss of UNC-94 function results in areas of flattened intestinal lumen. In worms homozygous for the strong loss-of-function allele, unc-94(tm724), the Terminal Web is thinner and the amount of F-actin is reduced, pointing to a role for UNC-94 in regulating the structure of the Terminal Web. The non-muscle myosin, NMY-1, also localizes to the Terminal Web, and we present evidence that increasing actomyosin contractility by depleting the myosin phosphatase regulatory subunit, mel-11, can rescue the flattened lumen phenotype of unc-94 mutants. Conclusions: The data support a model in which minus-end actin capping by UNC-94 promotes proper F-actin structure and contraction in the Terminal Web, yielding proper shape of the intestinal lumen. This establishes a new role for a tropomodulin in regulating lumen shape during tubulogenesis. Developmental Dynamics 243:753–764, 2014. V C 2014 Wiley Periodicals, Inc.

Nicole Vissichelli - One of the best experts on this subject based on the ideXlab platform.

  • the minus end actin capping protein unc 94 tropomodulin regulates development of the caenorhabditis elegans intestine
    Developmental Dynamics, 2014
    Co-Authors: Elisabeth Coxpaulson, Vincent L. Cannataro, Thomas Gallagher, Corey M. Hoffman, Gary Mantione, Matthew Mcintosh, Malan Silva, Nicole Vissichelli, Rachel Walker, Jeffrey S. Simske
    Abstract:

    Background: Tropomodulins are actin-capping proteins that regulate the stability of the slow-growing, minus-ends of actin filaments. The C. elegans tropomodulin homolog, UNC-94, has sequence and functional similarity to vertebrate tropomodulins. We investigated the role of UNC-94 in C. elegans intestinal morphogenesis. Results: In the embryonic C. elegans intestine, UNC-94 localizes to the Terminal Web, an actin- and intermediate filament-rich structure that underlies the apical membrane. Loss of UNC-94 function results in areas of flattened intestinal lumen. In worms homozygous for the strong loss-of-function allele, unc-94(tm724), the Terminal Web is thinner and the amount of F-actin is reduced, pointing to a role for UNC-94 in regulating the structure of the Terminal Web. The non-muscle myosin, NMY-1, also localizes to the Terminal Web, and we present evidence that increasing actomyosin contractility by depleting the myosin phosphatase regulatory subunit, mel-11, can rescue the flattened lumen phenotype of unc-94 mutants. Conclusions: The data support a model in which minus-end actin capping by UNC-94 promotes proper F-actin structure and contraction in the Terminal Web, yielding proper shape of the intestinal lumen. This establishes a new role for a tropomodulin in regulating lumen shape during tubulogenesis. Developmental Dynamics 243:753–764, 2014. V C 2014 Wiley Periodicals, Inc.

  • The Minus-End Actin Capping Protein, UNC-94/Tropomodulin, Regulates Development of the Caenorhabditis elegans Intestine
    Developmental Dynamics, 2014
    Co-Authors: Elisabeth Cox-paulson, Vincent L. Cannataro, Thomas Gallagher, Corey M. Hoffman, Gary Mantione, Matthew Mcintosh, Malan Silva, Nicole Vissichelli, Rachel L. Walker, Jeffrey S. Simske
    Abstract:

    Background: Tropomodulins are actin-capping proteins that regulate the stability of the slow-growing, minus-ends of actin filaments. The C. elegans tropomodulin homolog, UNC-94, has sequence and functional similarity to vertebrate tropomodulins. We investigated the role of UNC-94 in C. elegans intestinal morphogenesis. Results: In the embryonic C. elegans intestine, UNC-94 localizes to the Terminal Web, an actin- and intermediate filament-rich structure that underlies the apical membrane. Loss of UNC-94 function results in areas of flattened intestinal lumen. In worms homozygous for the strong loss-of-function allele, unc-94(tm724), the Terminal Web is thinner and the amount of F-actin is reduced, pointing to a role for UNC-94 in regulating the structure of the Terminal Web. The non-muscle myosin, NMY-1, also localizes to the Terminal Web, and we present evidence that increasing actomyosin contractility by depleting the myosin phosphatase regulatory subunit, mel-11, can rescue the flattened lumen phenotype of unc-94 mutants. Conclusions: The data support a model in which minus-end actin capping by UNC-94 promotes proper F-actin structure and contraction in the Terminal Web, yielding proper shape of the intestinal lumen. This establishes a new role for a tropomodulin in regulating lumen shape during tubulogenesis. Developmental Dynamics 243:753–764, 2014. V C 2014 Wiley Periodicals, Inc.

Malan Silva - One of the best experts on this subject based on the ideXlab platform.

  • the minus end actin capping protein unc 94 tropomodulin regulates development of the caenorhabditis elegans intestine
    Developmental Dynamics, 2014
    Co-Authors: Elisabeth Coxpaulson, Vincent L. Cannataro, Thomas Gallagher, Corey M. Hoffman, Gary Mantione, Matthew Mcintosh, Malan Silva, Nicole Vissichelli, Rachel Walker, Jeffrey S. Simske
    Abstract:

    Background: Tropomodulins are actin-capping proteins that regulate the stability of the slow-growing, minus-ends of actin filaments. The C. elegans tropomodulin homolog, UNC-94, has sequence and functional similarity to vertebrate tropomodulins. We investigated the role of UNC-94 in C. elegans intestinal morphogenesis. Results: In the embryonic C. elegans intestine, UNC-94 localizes to the Terminal Web, an actin- and intermediate filament-rich structure that underlies the apical membrane. Loss of UNC-94 function results in areas of flattened intestinal lumen. In worms homozygous for the strong loss-of-function allele, unc-94(tm724), the Terminal Web is thinner and the amount of F-actin is reduced, pointing to a role for UNC-94 in regulating the structure of the Terminal Web. The non-muscle myosin, NMY-1, also localizes to the Terminal Web, and we present evidence that increasing actomyosin contractility by depleting the myosin phosphatase regulatory subunit, mel-11, can rescue the flattened lumen phenotype of unc-94 mutants. Conclusions: The data support a model in which minus-end actin capping by UNC-94 promotes proper F-actin structure and contraction in the Terminal Web, yielding proper shape of the intestinal lumen. This establishes a new role for a tropomodulin in regulating lumen shape during tubulogenesis. Developmental Dynamics 243:753–764, 2014. V C 2014 Wiley Periodicals, Inc.

  • The Minus-End Actin Capping Protein, UNC-94/Tropomodulin, Regulates Development of the Caenorhabditis elegans Intestine
    Developmental Dynamics, 2014
    Co-Authors: Elisabeth Cox-paulson, Vincent L. Cannataro, Thomas Gallagher, Corey M. Hoffman, Gary Mantione, Matthew Mcintosh, Malan Silva, Nicole Vissichelli, Rachel L. Walker, Jeffrey S. Simske
    Abstract:

    Background: Tropomodulins are actin-capping proteins that regulate the stability of the slow-growing, minus-ends of actin filaments. The C. elegans tropomodulin homolog, UNC-94, has sequence and functional similarity to vertebrate tropomodulins. We investigated the role of UNC-94 in C. elegans intestinal morphogenesis. Results: In the embryonic C. elegans intestine, UNC-94 localizes to the Terminal Web, an actin- and intermediate filament-rich structure that underlies the apical membrane. Loss of UNC-94 function results in areas of flattened intestinal lumen. In worms homozygous for the strong loss-of-function allele, unc-94(tm724), the Terminal Web is thinner and the amount of F-actin is reduced, pointing to a role for UNC-94 in regulating the structure of the Terminal Web. The non-muscle myosin, NMY-1, also localizes to the Terminal Web, and we present evidence that increasing actomyosin contractility by depleting the myosin phosphatase regulatory subunit, mel-11, can rescue the flattened lumen phenotype of unc-94 mutants. Conclusions: The data support a model in which minus-end actin capping by UNC-94 promotes proper F-actin structure and contraction in the Terminal Web, yielding proper shape of the intestinal lumen. This establishes a new role for a tropomodulin in regulating lumen shape during tubulogenesis. Developmental Dynamics 243:753–764, 2014. V C 2014 Wiley Periodicals, Inc.