The Experts below are selected from a list of 69 Experts worldwide ranked by ideXlab platform

J. Hegemann - One of the best experts on this subject based on the ideXlab platform.

  • The Vesicular Transport Protein Cgp1p/Vps54p/Tcs3p/Luv1p is required for the integrity of the actin cytoskeleton
    Molecular Genetics and Genomics, 2002
    Co-Authors: T. Fiedler, T. Karpova, U. Fleig, M. Young, J. Cooper, J. Hegemann
    Abstract:

    The CGP1 gene was identified in a screen for mutations that were synthetic lethal in combination with a deletion of the gene ( CPF1 ) for centromere and promoter factor 1. Cells deleted for CGP1 showed reduced viability, were temperature sensitive for growth and exhibited altered sensitivity to microtubule-destabilizing drugs. Furthermore, Δ cgp1 cells showed increased rates of loss of a circular minichromosome and defects in the positioning of the short mitotic spindle. Further phenotypic analysis of Δ cgp1 cells revealed that loss of Cgp1p function led to severe depolarization of the actin cytoskeleton. In addition, cells deleted for CGP1 were hypersensitive to the actin-disrupting compound Latrunculin-A, exhibited strongly reduced polarized localization of the unconventional myosin Myo2p, and showed defects in other actin-related processes, such as shmoo formation and cell wall integrity. Cgp1p was recently identified by several groups as Vps54p, which is a member of the VFT complex that is involved in Vesicular Protein Transport at the level of the late Golgi, acting as a tethering factor. Our data show for the first time that Cgp1p/Vps54p links aspects of Vesicular Protein Transport with the organization of the actin cytoskeleton.

  • the Vesicular Transport Protein cgp1p vps54p tcs3p luv1p is required for the integrity of the actin cytoskeleton
    Molecular Genetics and Genomics, 2002
    Co-Authors: T A Fiedler, T. Karpova, U. Fleig, Michael E Young, John A Cooper, J. Hegemann
    Abstract:

    The CGP1 gene was identified in a screen for mutations that were synthetic lethal in combination with a deletion of the gene (CPF1) for centromere and promoter factor 1. Cells deleted for CGP1 showed reduced viability, were temperature sensitive for growth and exhibited altered sensitivity to microtubule-destabilizing drugs. Furthermore, Δ cgp1 cells showed increased rates of loss of a circular minichromosome and defects in the positioning of the short mitotic spindle. Further phenotypic analysis of Δ cgp1 cells revealed that loss of Cgp1p function led to severe depolarization of the actin cytoskeleton. In addition, cells deleted for CGP1 were hypersensitive to the actin-disrupting compound Latrunculin-A, exhibited strongly reduced polarized localization of the unconventional myosin Myo2p, and showed defects in other actin-related processes, such as shmoo formation and cell wall integrity. Cgp1p was recently identified by several groups as Vps54p, which is a member of the VFT complex that is involved in Vesicular Protein Transport at the level of the late Golgi, acting as a tethering factor. Our data show for the first time that Cgp1p/Vps54p links aspects of Vesicular Protein Transport with the organization of the actin cytoskeleton.

U. Fleig - One of the best experts on this subject based on the ideXlab platform.

  • The Vesicular Transport Protein Cgp1p/Vps54p/Tcs3p/Luv1p is required for the integrity of the actin cytoskeleton
    Molecular Genetics and Genomics, 2002
    Co-Authors: T. Fiedler, T. Karpova, U. Fleig, M. Young, J. Cooper, J. Hegemann
    Abstract:

    The CGP1 gene was identified in a screen for mutations that were synthetic lethal in combination with a deletion of the gene ( CPF1 ) for centromere and promoter factor 1. Cells deleted for CGP1 showed reduced viability, were temperature sensitive for growth and exhibited altered sensitivity to microtubule-destabilizing drugs. Furthermore, Δ cgp1 cells showed increased rates of loss of a circular minichromosome and defects in the positioning of the short mitotic spindle. Further phenotypic analysis of Δ cgp1 cells revealed that loss of Cgp1p function led to severe depolarization of the actin cytoskeleton. In addition, cells deleted for CGP1 were hypersensitive to the actin-disrupting compound Latrunculin-A, exhibited strongly reduced polarized localization of the unconventional myosin Myo2p, and showed defects in other actin-related processes, such as shmoo formation and cell wall integrity. Cgp1p was recently identified by several groups as Vps54p, which is a member of the VFT complex that is involved in Vesicular Protein Transport at the level of the late Golgi, acting as a tethering factor. Our data show for the first time that Cgp1p/Vps54p links aspects of Vesicular Protein Transport with the organization of the actin cytoskeleton.

  • the Vesicular Transport Protein cgp1p vps54p tcs3p luv1p is required for the integrity of the actin cytoskeleton
    Molecular Genetics and Genomics, 2002
    Co-Authors: T A Fiedler, T. Karpova, U. Fleig, Michael E Young, John A Cooper, J. Hegemann
    Abstract:

    The CGP1 gene was identified in a screen for mutations that were synthetic lethal in combination with a deletion of the gene (CPF1) for centromere and promoter factor 1. Cells deleted for CGP1 showed reduced viability, were temperature sensitive for growth and exhibited altered sensitivity to microtubule-destabilizing drugs. Furthermore, Δ cgp1 cells showed increased rates of loss of a circular minichromosome and defects in the positioning of the short mitotic spindle. Further phenotypic analysis of Δ cgp1 cells revealed that loss of Cgp1p function led to severe depolarization of the actin cytoskeleton. In addition, cells deleted for CGP1 were hypersensitive to the actin-disrupting compound Latrunculin-A, exhibited strongly reduced polarized localization of the unconventional myosin Myo2p, and showed defects in other actin-related processes, such as shmoo formation and cell wall integrity. Cgp1p was recently identified by several groups as Vps54p, which is a member of the VFT complex that is involved in Vesicular Protein Transport at the level of the late Golgi, acting as a tethering factor. Our data show for the first time that Cgp1p/Vps54p links aspects of Vesicular Protein Transport with the organization of the actin cytoskeleton.

T. Karpova - One of the best experts on this subject based on the ideXlab platform.

  • The Vesicular Transport Protein Cgp1p/Vps54p/Tcs3p/Luv1p is required for the integrity of the actin cytoskeleton
    Molecular Genetics and Genomics, 2002
    Co-Authors: T. Fiedler, T. Karpova, U. Fleig, M. Young, J. Cooper, J. Hegemann
    Abstract:

    The CGP1 gene was identified in a screen for mutations that were synthetic lethal in combination with a deletion of the gene ( CPF1 ) for centromere and promoter factor 1. Cells deleted for CGP1 showed reduced viability, were temperature sensitive for growth and exhibited altered sensitivity to microtubule-destabilizing drugs. Furthermore, Δ cgp1 cells showed increased rates of loss of a circular minichromosome and defects in the positioning of the short mitotic spindle. Further phenotypic analysis of Δ cgp1 cells revealed that loss of Cgp1p function led to severe depolarization of the actin cytoskeleton. In addition, cells deleted for CGP1 were hypersensitive to the actin-disrupting compound Latrunculin-A, exhibited strongly reduced polarized localization of the unconventional myosin Myo2p, and showed defects in other actin-related processes, such as shmoo formation and cell wall integrity. Cgp1p was recently identified by several groups as Vps54p, which is a member of the VFT complex that is involved in Vesicular Protein Transport at the level of the late Golgi, acting as a tethering factor. Our data show for the first time that Cgp1p/Vps54p links aspects of Vesicular Protein Transport with the organization of the actin cytoskeleton.

  • the Vesicular Transport Protein cgp1p vps54p tcs3p luv1p is required for the integrity of the actin cytoskeleton
    Molecular Genetics and Genomics, 2002
    Co-Authors: T A Fiedler, T. Karpova, U. Fleig, Michael E Young, John A Cooper, J. Hegemann
    Abstract:

    The CGP1 gene was identified in a screen for mutations that were synthetic lethal in combination with a deletion of the gene (CPF1) for centromere and promoter factor 1. Cells deleted for CGP1 showed reduced viability, were temperature sensitive for growth and exhibited altered sensitivity to microtubule-destabilizing drugs. Furthermore, Δ cgp1 cells showed increased rates of loss of a circular minichromosome and defects in the positioning of the short mitotic spindle. Further phenotypic analysis of Δ cgp1 cells revealed that loss of Cgp1p function led to severe depolarization of the actin cytoskeleton. In addition, cells deleted for CGP1 were hypersensitive to the actin-disrupting compound Latrunculin-A, exhibited strongly reduced polarized localization of the unconventional myosin Myo2p, and showed defects in other actin-related processes, such as shmoo formation and cell wall integrity. Cgp1p was recently identified by several groups as Vps54p, which is a member of the VFT complex that is involved in Vesicular Protein Transport at the level of the late Golgi, acting as a tethering factor. Our data show for the first time that Cgp1p/Vps54p links aspects of Vesicular Protein Transport with the organization of the actin cytoskeleton.

Mickie H Cheng - One of the best experts on this subject based on the ideXlab platform.

  • COPA mutations impair ER-Golgi Transport and cause hereditary autoimmune-mediated lung disease and arthritis
    Nature Genetics, 2015
    Co-Authors: Levi B. Watkin, Birthe Jessen, Wojciech Wiszniewski, Timothy J. Vece, Maike Thamsen, Regie Lyn P. Santos-cortez, Tomasz Gambin, Lisa R Forbes, Asbjørg Stray-pedersen, Mickie H Cheng
    Abstract:

    Anthony Shum, Jordan Orange, James Lupski and colleagues show that mutations in the coatamer subunit gene COPA cause an autoimmune syndrome characterized by inflammatory arthritis and interstitial lung disease. They further show that the mutations disrupt ER-Golgi Transport, leading to ER stress and altered T cell function. Unbiased genetic studies have uncovered surprising molecular mechanisms in human cellular immunity and autoimmunity^ 1 . We performed whole-exome sequencing and targeted sequencing in five families with an apparent mendelian syndrome of autoimmunity characterized by high-titer autoantibodies, inflammatory arthritis and interstitial lung disease. We identified four unique deleterious variants in the COPA gene (encoding coatomer subunit α) affecting the same functional domain. Hypothesizing that mutant COPA leads to defective intracellular Transport via coat Protein complex I (COPI)^ 2 , 3 , 4 , we show that COPA variants impair binding to Proteins targeted for retrograde Golgi-to-ER Transport. Additionally, expression of mutant COPA results in ER stress and the upregulation of cytokines priming for a T helper type 17 (T_H17) response. Patient-derived CD4^+ T cells also demonstrate significant skewing toward a T_H17 phenotype that is implicated in autoimmunity^ 5 , 6 . Our findings uncover an unexpected molecular link between a Vesicular Transport Protein and a syndrome of autoimmunity manifested by lung and joint disease.

T A Fiedler - One of the best experts on this subject based on the ideXlab platform.

  • the Vesicular Transport Protein cgp1p vps54p tcs3p luv1p is required for the integrity of the actin cytoskeleton
    Molecular Genetics and Genomics, 2002
    Co-Authors: T A Fiedler, T. Karpova, U. Fleig, Michael E Young, John A Cooper, J. Hegemann
    Abstract:

    The CGP1 gene was identified in a screen for mutations that were synthetic lethal in combination with a deletion of the gene (CPF1) for centromere and promoter factor 1. Cells deleted for CGP1 showed reduced viability, were temperature sensitive for growth and exhibited altered sensitivity to microtubule-destabilizing drugs. Furthermore, Δ cgp1 cells showed increased rates of loss of a circular minichromosome and defects in the positioning of the short mitotic spindle. Further phenotypic analysis of Δ cgp1 cells revealed that loss of Cgp1p function led to severe depolarization of the actin cytoskeleton. In addition, cells deleted for CGP1 were hypersensitive to the actin-disrupting compound Latrunculin-A, exhibited strongly reduced polarized localization of the unconventional myosin Myo2p, and showed defects in other actin-related processes, such as shmoo formation and cell wall integrity. Cgp1p was recently identified by several groups as Vps54p, which is a member of the VFT complex that is involved in Vesicular Protein Transport at the level of the late Golgi, acting as a tethering factor. Our data show for the first time that Cgp1p/Vps54p links aspects of Vesicular Protein Transport with the organization of the actin cytoskeleton.