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Transmembrane Protein

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Shian Wu - One of the best experts on this subject based on the ideXlab platform.

  • the apical Transmembrane Protein crumbs functions as a tumor suppressor that regulates hippo signaling by binding to expanded
    Proceedings of the National Academy of Sciences of the United States of America, 2010
    Co-Authors: Chen Ling, Yonggang Zheng, Jianzhong Yu, Shian Wu, Juan Huang, Yang Hong
    Abstract:

    The Hippo signaling pathway regulates organ size and tissue homeostasis from Drosophila to mammals. At the core of the Hippo pathway is a kinase cascade extending from the Hippo (Hpo) tumor suppressor to the Yorkie (Yki) oncoProtein. The Hippo kinase cascade, in turn, is regulated by apical membrane-associated Proteins such as the FERM domain Proteins Merlin and Expanded (Ex), and the WW- and C2-domain Protein Kibra. How these apical Proteins are themselves regulated remains poorly understood. Here, we identify the Transmembrane Protein Crumbs (Crb), a determinant of epithelial apical-basal polarity in Drosophila embryos, as an upstream component of the Hippo pathway in imaginal disk growth control. Loss of Crb leads to tissue overgrowth and target gene expression characteristic of defective Hippo signaling. Crb directly binds to Ex through its juxtamembrane FERM-binding motif (FBM). Loss of Crb or mutation of its FBM leads to mislocalization of Ex to basolateral domain of imaginal disk epithelial cells. These results shed light on the mechanism of Ex regulation and provide a molecular link between apical-basal polarity and tissue growth. Furthermore, our studies implicate Crb as a putative cell surface receptor for Hippo signaling by uncovering a Transmembrane Protein that directly binds to an apical component of the Hippo pathway.

  • the apical Transmembrane Protein crumbs functions as a tumor suppressor that regulates hippo signaling by binding to expanded
    Proceedings of the National Academy of Sciences of the United States of America, 2010
    Co-Authors: Chen Ling, Yonggang Zheng, Jianzhong Yu, Shian Wu, Juan Huang, Yang Hong
    Abstract:

    The Hippo signaling pathway regulates organ size and tissue homeostasis from Drosophila to mammals. At the core of the Hippo pathway is a kinase cascade extending from the Hippo (Hpo) tumor suppressor to the Yorkie (Yki) oncoProtein. The Hippo kinase cascade, in turn, is regulated by apical membrane-associated Proteins such as the FERM domain Proteins Merlin and Expanded (Ex), and the WW- and C2-domain Protein Kibra. How these apical Proteins are themselves regulated remains poorly understood. Here, we identify the Transmembrane Protein Crumbs (Crb), a determinant of epithelial apical-basal polarity in Drosophila embryos, as an upstream component of the Hippo pathway in imaginal disk growth control. Loss of Crb leads to tissue overgrowth and target gene expression characteristic of defective Hippo signaling. Crb directly binds to Ex through its juxtamembrane FERM-binding motif (FBM). Loss of Crb or mutation of its FBM leads to mislocalization of Ex to basolateral domain of imaginal disk epithelial cells. These results shed light on the mechanism of Ex regulation and provide a molecular link between apical-basal polarity and tissue growth. Furthermore, our studies implicate Crb as a putative cell surface receptor for Hippo signaling by uncovering a Transmembrane Protein that directly binds to an apical component of the Hippo pathway.

Chengqi Zhang - One of the best experts on this subject based on the ideXlab platform.

  • the Transmembrane Protein fgsho1 regulates fungal development and pathogenicity via the mapk module ste50 ste11 ste7 in fusarium graminearum
    New Phytologist, 2015
    Co-Authors: Yun Chen, Ye Liu, Chengqi Zhang
    Abstract:

    Summary The mitogen-activated Protein kinase (MAPK) signaling pathways have been characterized in Fusarium graminearum. Currently, the upstream sensors of these pathways are unknown. Biological functions of a Transmembrane Protein FgSho1 were investigated using a target gene deletion strategy. The relationship between FgSho1 and the MAPK cassette FgSte50-Ste11-Ste7 was analyzed in depth. The Transmembrane Protein FgSho1 is required for conidiation, full virulence, and deoxynivalenol (DON) biosynthesis in F. graminearum. Furthermore, FgSho1 and FgSln1 have an additive effect on virulence of F. graminearum. The yeast two-hybrid, coimmunoprecipitation, colocalization and affinity capture-mass spectrometry analyses strongly indicated that FgSho1 physically interacts with the MAPK module FgSte50-Ste11-Ste7. Similar to the FgSho1 mutant, the mutants of FgSte50, FgSte11, and FgSte7 were defective in conidiation, pathogenicity, and DON biosynthesis. In addition, FgSho1 plays a minor role in the response to osmotic stress but it is involved in the cell wall integrity pathway, which is independent of the module FgSte50-Ste11-Ste7 in F. graminearum. Collectively, results of this study strongly indicate that FgSho1 regulates fungal development and pathogenicity via the MAPK module FgSte50-Ste11-Ste7 in F. graminearum, which is different from what is known in the budding yeast Saccharomyces cerevisiae.

  • The Transmembrane Protein FgSho1 regulates fungal development and pathogenicity via the MAPK module Ste50‐Ste11‐Ste7 in Fusarium graminearum
    The New phytologist, 2014
    Co-Authors: Yun Chen, Ye Liu, Chengqi Zhang
    Abstract:

    Summary The mitogen-activated Protein kinase (MAPK) signaling pathways have been characterized in Fusarium graminearum. Currently, the upstream sensors of these pathways are unknown. Biological functions of a Transmembrane Protein FgSho1 were investigated using a target gene deletion strategy. The relationship between FgSho1 and the MAPK cassette FgSte50-Ste11-Ste7 was analyzed in depth. The Transmembrane Protein FgSho1 is required for conidiation, full virulence, and deoxynivalenol (DON) biosynthesis in F. graminearum. Furthermore, FgSho1 and FgSln1 have an additive effect on virulence of F. graminearum. The yeast two-hybrid, coimmunoprecipitation, colocalization and affinity capture-mass spectrometry analyses strongly indicated that FgSho1 physically interacts with the MAPK module FgSte50-Ste11-Ste7. Similar to the FgSho1 mutant, the mutants of FgSte50, FgSte11, and FgSte7 were defective in conidiation, pathogenicity, and DON biosynthesis. In addition, FgSho1 plays a minor role in the response to osmotic stress but it is involved in the cell wall integrity pathway, which is independent of the module FgSte50-Ste11-Ste7 in F. graminearum. Collectively, results of this study strongly indicate that FgSho1 regulates fungal development and pathogenicity via the MAPK module FgSte50-Ste11-Ste7 in F. graminearum, which is different from what is known in the budding yeast Saccharomyces cerevisiae.

Christof Niehrs - One of the best experts on this subject based on the ideXlab platform.

  • the Transmembrane Protein xflrt3 forms a complex with fgf receptors and promotes fgf signalling
    Nature Cell Biology, 2004
    Co-Authors: Ralph T Bottcher, Nicolas Pollet, Hajo Delius, Christof Niehrs
    Abstract:

    The Transmembrane Protein XFLRT3 forms a complex with FGF receptors and promotes FGF signalling

  • The Transmembrane Protein XFLRT3 forms a complex with FGF receptors and promotes FGF signalling
    Nature Cell Biology, 2004
    Co-Authors: Ralph T Bottcher, Nicolas Pollet, Hajo Delius, Christof Niehrs
    Abstract:

    Fibroblast growth factors (FGFs) signal through high-affinity tyrosine kinase receptors to regulate a diverse range of cellular processes, including cell growth, differentiation and migration, as well as cell death^ 1 , 2 , 3 , 4 . Here we identify XFLRT3, a member of a leucine-rich-repeat Transmembrane Protein family, as a novel modulator of FGF signalling. XFLRT3 is co-expressed with FGFs, and its expression is both induced after activation and downregulated after inhibition of FGF signalling. In gain- and loss-of function experiments, FLRT3 and FLRT2 phenocopy FGF signalling in Xenopus laevis . XFLRT3 signalling results in phosphorylation of ERK and is blocked by MAPK phosphatase 1, but not by expression of a dominant-negative phosphatidyl inositol 3-OH kinase (PI(3)K) mutant. XFLRT3 interacts with FGF receptors (FGFRs) in co-immunoprecipitation experiments in vitro and in bioluminescence resonance energy transfer assays in vivo . The results indicate that XFLRT3 is a Transmembrane modulator of FGF–MAP kinase signalling in vertebrates.

Christine Petit - One of the best experts on this subject based on the ideXlab platform.

  • Vezatin, a novel Transmembrane Protein, bridges myosin VIIA to the cadherin–catenins complex
    The EMBO journal, 2000
    Co-Authors: Polonca Küssel-andermann, Aziz El-amraoui, Saaid Safieddine, Sylvie Nouaille, Uwe Wolfrum, Isabelle Perfettini, Marc Lecuit, Pascale Cossart, Christine Petit
    Abstract:

    Defects in myosin VIIA are responsible for deafness in the human and mouse. The role of this unconventional myosin in the sensory hair cells of the inner ear is not yet understood. Here we show that the C-terminal FERM domain of myosin VIIA binds to a novel Transmembrane Protein, vezatin, which we identified by a yeast two-hybrid screen. Vezatin is a ubiquitous Protein of adherens cell-cell junctions, where it interacts with both myosin VIIA and the cadherin-catenins complex. Its recruitment to adherens junctions implicates the C-terminal region of alpha-catenin. Taken together, these data suggest that myosin VIIA, anchored by vezatin to the cadherin-catenins complex, creates a tension force between adherens junctions and the actin cytoskeleton that is expected to strengthen cell-cell adhesion. In the inner ear sensory hair cells vezatin is, in addition, concentrated at another membrane-membrane interaction site, namely at the fibrillar links interconnecting the bases of adjacent stereocilia. In myosin VIIA-defective mutants, inactivity of the vezatin-myosin VIIA complex at both sites could account for splaying out of the hair cell stereocilia.

  • vezatin a novel Transmembrane Protein bridges myosin viia to the cadherin catenins complex
    The EMBO Journal, 2000
    Co-Authors: Polonca Kusselandermann, Saaid Safieddine, Sylvie Nouaille, Uwe Wolfrum, Isabelle Perfettini, Marc Lecuit, Pascale Cossart, Aziz Elamraoui, Christine Petit
    Abstract:

    Defects in myosin VIIA are responsible for deafness in the human and mouse. The role of this unconventional myosin in the sensory hair cells of the inner ear is not yet understood. Here we show that the C-terminal FERM domain of myosin VIIA binds to a novel Transmembrane Protein, vezatin, which we identified by a yeast two-hybrid screen. Vezatin is a ubiquitous Protein of adherens cell–cell junctions, where it interacts with both myosin VIIA and the cadherin–catenins complex. Its recruitment to adherens junctions implicates the C-terminal region of α-catenin. Taken together, these data suggest that myosin VIIA, anchored by vezatin to the cadherin–catenins complex, creates a tension force between adherens junctions and the actin cytoskeleton that is expected to strengthen cell–cell adhesion. In the inner ear sensory hair cells vezatin is, in addition, concentrated at another membrane–membrane interaction site, namely at the fibrillar links interconnecting the bases of adjacent stereocilia. In myosin VIIA-defective mutants, inactivity of the vezatin–myosin VIIA complex at both sites could account for splaying out of the hair cell stereocilia.

Yun Chen - One of the best experts on this subject based on the ideXlab platform.

  • the Transmembrane Protein fgsho1 regulates fungal development and pathogenicity via the mapk module ste50 ste11 ste7 in fusarium graminearum
    New Phytologist, 2015
    Co-Authors: Yun Chen, Ye Liu, Chengqi Zhang
    Abstract:

    Summary The mitogen-activated Protein kinase (MAPK) signaling pathways have been characterized in Fusarium graminearum. Currently, the upstream sensors of these pathways are unknown. Biological functions of a Transmembrane Protein FgSho1 were investigated using a target gene deletion strategy. The relationship between FgSho1 and the MAPK cassette FgSte50-Ste11-Ste7 was analyzed in depth. The Transmembrane Protein FgSho1 is required for conidiation, full virulence, and deoxynivalenol (DON) biosynthesis in F. graminearum. Furthermore, FgSho1 and FgSln1 have an additive effect on virulence of F. graminearum. The yeast two-hybrid, coimmunoprecipitation, colocalization and affinity capture-mass spectrometry analyses strongly indicated that FgSho1 physically interacts with the MAPK module FgSte50-Ste11-Ste7. Similar to the FgSho1 mutant, the mutants of FgSte50, FgSte11, and FgSte7 were defective in conidiation, pathogenicity, and DON biosynthesis. In addition, FgSho1 plays a minor role in the response to osmotic stress but it is involved in the cell wall integrity pathway, which is independent of the module FgSte50-Ste11-Ste7 in F. graminearum. Collectively, results of this study strongly indicate that FgSho1 regulates fungal development and pathogenicity via the MAPK module FgSte50-Ste11-Ste7 in F. graminearum, which is different from what is known in the budding yeast Saccharomyces cerevisiae.

  • The Transmembrane Protein FgSho1 regulates fungal development and pathogenicity via the MAPK module Ste50‐Ste11‐Ste7 in Fusarium graminearum
    The New phytologist, 2014
    Co-Authors: Yun Chen, Ye Liu, Chengqi Zhang
    Abstract:

    Summary The mitogen-activated Protein kinase (MAPK) signaling pathways have been characterized in Fusarium graminearum. Currently, the upstream sensors of these pathways are unknown. Biological functions of a Transmembrane Protein FgSho1 were investigated using a target gene deletion strategy. The relationship between FgSho1 and the MAPK cassette FgSte50-Ste11-Ste7 was analyzed in depth. The Transmembrane Protein FgSho1 is required for conidiation, full virulence, and deoxynivalenol (DON) biosynthesis in F. graminearum. Furthermore, FgSho1 and FgSln1 have an additive effect on virulence of F. graminearum. The yeast two-hybrid, coimmunoprecipitation, colocalization and affinity capture-mass spectrometry analyses strongly indicated that FgSho1 physically interacts with the MAPK module FgSte50-Ste11-Ste7. Similar to the FgSho1 mutant, the mutants of FgSte50, FgSte11, and FgSte7 were defective in conidiation, pathogenicity, and DON biosynthesis. In addition, FgSho1 plays a minor role in the response to osmotic stress but it is involved in the cell wall integrity pathway, which is independent of the module FgSte50-Ste11-Ste7 in F. graminearum. Collectively, results of this study strongly indicate that FgSho1 regulates fungal development and pathogenicity via the MAPK module FgSte50-Ste11-Ste7 in F. graminearum, which is different from what is known in the budding yeast Saccharomyces cerevisiae.

  • The Transmembrane Protein CBP plays a role in transiently anchoring small clusters of Thy-1, a GPI-anchored Protein, to the cytoskeleton.
    Journal of Cell Science, 2009
    Co-Authors: Yun Chen, Laurence Veracini, Christine Benistant, Ken Jacobson
    Abstract:

    It remains unclear how GPI-anchored Proteins (GPIAPs), which lack cytoplasmic domains, transduce signals triggered by specific ligation. Such signal transduction has been speculated to require the ligated GPIAP to associate with membrane-spanning Proteins that communicate with obligate cytoplasmic Proteins. Transient anchorage of crosslinked Proteins on the cell surface was previously characterized by single-particle tracking, and temporary association with the actin cytoskeleton was hypothesized to cause regulated anchorage. GPIAPs, such as Thy-1, require clustering, cholesterol and Src-family kinase (SFK) activity to become transiently anchored. By contrast, a Transmembrane Protein, the cystic fibrosis Transmembrane conductance regulator (CFTR), which has a PDZ-binding motif in its cytoplasmic C-terminus that binds the ERM adaptor EBP50, exhibits anchorage that strictly requires EBP50 but has little dependence on cholesterol or SFK. We hypothesized that a Transmembrane Protein would be required to mediate the linkage between Thy-1 and the cytoskeleton. Here, we present evidence, obtained by shRNA knockdown, that the Transmembrane Protein Csk-binding Protein (CBP) plays an obligatory role in the transient anchorage of Thy1. Furthermore, either a dominant-negative form of CBP that did not bind EBP50 or a dominant-negative EBP50 drastically reduced transient anchorage of Thy-1, indicating the involvement of this adaptor. Finally, we speculate on the role of phosphorylation in the regulation of transient anchorage.