C E Turner

Summary

Affiliation: SUNY Upstate Medical University
Country: USA

Publications

  1. ncbi request reprint Paxillin interactions
    C E Turner
    Dept of Cell and Developmental Biology, SUNY Upstate Medical University, Syracuse, NY13210, USA
    J Cell Sci 113:4139-40. 2000
  2. ncbi request reprint Paxillin and focal adhesion signalling
    C E Turner
    Department of Cell and Developmental Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, New York 13210, USA
    Nat Cell Biol 2:E231-6. 2000
  3. pmc The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL)
    K A West
    Department of Cell and Developmental Biology, State University of New York, Upstate Medical University, 750 East Adams St, Syracuse, NY 13210, USA
    J Cell Biol 154:161-76. 2001
  4. pmc Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion
    S N Nikolopoulos
    Department of Cell and Developmental Biology, State University of New York Upstate Medical University, Syracuse, New York 13210, USA
    J Cell Biol 151:1435-48. 2000
  5. pmc Serine and threonine phosphorylation of the paxillin LIM domains regulates paxillin focal adhesion localization and cell adhesion to fibronectin
    M C Brown
    Department of Anatomy and Cell Biology, Program in Cell and Molecular Biology, State University of New York Health Science Center at Syracuse, Syracuse, New York 13210, USA
    Mol Biol Cell 9:1803-16. 1998
  6. pmc Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling
    C E Turner
    Department of Anatomy and Cell Biology, State University of New York, Health Science Center, Syracuse, New York 13210, USA
    J Cell Biol 145:851-63. 1999
  7. ncbi request reprint Paxillin-ARF GAP signaling and the cytoskeleton
    C E Turner
    Department of Cell and Developmental Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, New York 13210, USA
    Curr Opin Cell Biol 13:593-9. 2001
  8. ncbi request reprint Characterization of paxillin LIM domain-associated serine threonine kinases: activation by angiotensin II in vascular smooth muscle cells
    M C Brown
    Department of Anatomy and Cell Biology, Program in Cell and Molecular Biology, State University of New York Health Science Center at Syracuse, Syracuse, New York 13210, USA
    J Cell Biochem 76:99-108. 1999
  9. ncbi request reprint Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions
    S N Nikolopoulos
    Department of Cell and Developmental Biology, State University of New York Upstate Medical University, Syracuse, New York 13210, USA
    J Biol Chem 276:23499-505. 2001
  10. ncbi request reprint Cell motility: ARNOand ARF6 at the cutting edge
    C E Turner
    Department of Cell and Developmental Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, New York 13210, USA
    Curr Biol 11:R875-7. 2001

Collaborators

Detail Information

Publications11

  1. ncbi request reprint Paxillin interactions
    C E Turner
    Dept of Cell and Developmental Biology, SUNY Upstate Medical University, Syracuse, NY13210, USA
    J Cell Sci 113:4139-40. 2000
    ....
  2. ncbi request reprint Paxillin and focal adhesion signalling
    C E Turner
    Department of Cell and Developmental Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, New York 13210, USA
    Nat Cell Biol 2:E231-6. 2000
    ..Paxillin is a multi-domain adaptor found at the interface between the plasma membrane and the actin cytoskeleton. Here it provides a platform for the integration and processing of adhesion- and growth factor-related signals...
  3. pmc The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL)
    K A West
    Department of Cell and Developmental Biology, State University of New York, Upstate Medical University, 750 East Adams St, Syracuse, NY 13210, USA
    J Cell Biol 154:161-76. 2001
    ..These data suggest that the paxillin association with PKL is essential for normal integrin-mediated cell spreading, and locomotion and that this interaction is necessary for the regulation of Rac activity during these events...
  4. pmc Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion
    S N Nikolopoulos
    Department of Cell and Developmental Biology, State University of New York Upstate Medical University, Syracuse, New York 13210, USA
    J Cell Biol 151:1435-48. 2000
    ..Together, these results suggest an important role for actopaxin in integrin-dependent remodeling of the actin cytoskeleton during cell motility and cell adhesion...
  5. pmc Serine and threonine phosphorylation of the paxillin LIM domains regulates paxillin focal adhesion localization and cell adhesion to fibronectin
    M C Brown
    Department of Anatomy and Cell Biology, Program in Cell and Molecular Biology, State University of New York Health Science Center at Syracuse, Syracuse, New York 13210, USA
    Mol Biol Cell 9:1803-16. 1998
    ..Additionally, these results provide the first evidence that paxillin contributes to "inside-out" integrin-mediated signal transduction...
  6. pmc Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling
    C E Turner
    Department of Anatomy and Cell Biology, State University of New York, Health Science Center, Syracuse, New York 13210, USA
    J Cell Biol 145:851-63. 1999
    ..These data implicate paxillin as a mediator of p21 GTPase-regulated actin cytoskeletal reorganization through the recruitment to nascent focal adhesion structures of an active PAK/PIX complex potentially via interactions with p95PKL...
  7. ncbi request reprint Paxillin-ARF GAP signaling and the cytoskeleton
    C E Turner
    Department of Cell and Developmental Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, New York 13210, USA
    Curr Opin Cell Biol 13:593-9. 2001
    ..Evidence suggests an important role for ARF GAPs in mediating changes in the cell's actin cytoskeleton in response to adhesion and growth factor stimulation...
  8. ncbi request reprint Characterization of paxillin LIM domain-associated serine threonine kinases: activation by angiotensin II in vascular smooth muscle cells
    M C Brown
    Department of Anatomy and Cell Biology, Program in Cell and Molecular Biology, State University of New York Health Science Center at Syracuse, Syracuse, New York 13210, USA
    J Cell Biochem 76:99-108. 1999
    ....
  9. ncbi request reprint Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions
    S N Nikolopoulos
    Department of Cell and Developmental Biology, State University of New York Upstate Medical University, Syracuse, New York 13210, USA
    J Biol Chem 276:23499-505. 2001
    ..Thus, paxillin binding is necessary for efficient focal adhesion targeting of ILK and may therefore impact the role of ILK in integrin-mediated signal transduction events...
  10. ncbi request reprint Cell motility: ARNOand ARF6 at the cutting edge
    C E Turner
    Department of Cell and Developmental Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, New York 13210, USA
    Curr Biol 11:R875-7. 2001
    ..Recent studies have shown that ARNO and ARF6 play significant roles in coordinating this transition, providing new insight into the interplay between the Rho and ARF families of GTPases...
  11. pmc Adhesion of fibroblasts to fibronectin stimulates both serine and tyrosine phosphorylation of paxillin
    S L Bellis
    Department of Anatomy and Cell Biology, State University of New York Health Science Center, 750 E Adams Street, Syracuse, NY 13210, USA
    Biochem J 325:375-81. 1997
    ..These findings support a role for both tyrosine and serine kinases in the signal transduction pathway linking integrin activation to paxillin phosphorylation...