Paxillin
Mostrando 1-12 de 106 artigos, teses e dissertações.
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1. Trypanosoma cruzi down-regulates mechanosensitive proteins in cardiomyocytes
BACKGROUND Cardiac physiology depends on coupling and electrical and mechanical coordination through the intercalated disc. Focal adhesions offer mechanical support and signal transduction events during heart contraction-relaxation processes. Talin links integrins to the actin cytoskeleton and serves as a scaffold for the recruitment of other proteins, suc
Mem. Inst. Oswaldo Cruz. Publicado em: 15/08/2019
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2. Avaliação imunohistoquímica das alterações do citoesqueleto na parede alveolar em modelo experimental de lesão pulmonar induzida pela ventilação mecânica em ratos / Immunohistochemical evaluation of the cytoskeletal alterations in the alveolar wall in an experimental model of ventilator-induced lung injury in rats
INTRODUÇÃO: A ventilação mecânica é uma terapia importante, mas com possíveis complicações. Uma das mais relevantes é a lesão pulmonar induzida pelo ventilador (VILI do inglês Ventilator-induced lung injury). Devido à hiperdistensão alveolar, o pulmão inicia um processo inflamatório, com infiltrado neutrofílico, formação de membrana hialin
Publicado em: 2009
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3. Regulation of Rho and Rac Signaling to the Actin Cytoskeleton by Paxillin during Drosophila Development
Paxillin is a prominent focal adhesion docking protein that regulates cell adhesion and migration. Although numerous paxillin-binding proteins have been identified and paxillin is required for normal embryogenesis, the precise mechanism by which paxillin functions in vivo has not yet been determined. We identified an ortholog of mammalian paxillin in Drosoph
American Society for Microbiology.
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4. The Adaptor Protein Paxillin Is Essential for Normal Development in the Mouse and Is a Critical Transducer of Fibronectin Signaling
The integrin family of cell adhesion receptors are important for a diverse set of biological responses during development. Although many integrins have been shown to engage a similar set of cytoplasmic effector proteins in vitro, the importance of these proteins in the biological events mediated by different integrin receptors and ligands is uncertain. We ha
American Society for Microbiology.
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5. Serine and Threonine Phosphorylation of the Paxillin LIM Domains Regulates Paxillin Focal Adhesion Localization and Cell Adhesion to Fibronectin
We have previously shown that the LIM domains of paxillin operate as the focal adhesion (FA)-targeting motif of this protein. In the current study, we have identified the capacity of paxillin LIM2 and LIM3 to serve as binding sites for, and substrates of serine/threonine kinases. The activities of the LIM2- and LIM3-associated kinases were stimulated af
The American Society for Cell Biology.
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6. pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk.
Paxillin, a focal-adhesion-associated protein, becomes phosphorylated in response to a number of stimuli which also induce the tyrosine phosphorylation of the focal-adhesion-associated protein tyrosine kinase pp125FAK. On the basis of their colocalization and coordinate phosphorylation, paxillin is a candidate for a substrate of pp125FAK. We describe here co
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7. A New Paxillin-binding Protein, PAG3/Papα/KIAA0400, Bearing an ADP-Ribosylation Factor GTPase-activating Protein Activity, Is Involved in Paxillin Recruitment to Focal Adhesions and Cell Migration
Paxillin acts as an adaptor molecule in integrin signaling. Paxillin is localized to focal contacts but seems to also exist in a relatively large cytoplasmic pool. Here, we report the identification of a new paxillin-binding protein, PAG3 (paxillin-associated protein with ADP-ribosylation factor [ARF] GTPase-activating protein [GAP] activity, number 3), whic
The American Society for Cell Biology.
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8. An ADP-Ribosylation Factor GTPase-activating Protein Git2-short/KIAA0148 Is Involved in Subcellular Localization of Paxillin and Actin Cytoskeletal Organization
Paxillin acts as an adaptor protein in integrin signaling. We have shown that paxillin exists in a relatively large cytoplasmic pool, including perinuclear areas, in addition to focal complexes formed at the cell periphery and focal adhesions formed underneath the cell. Several ADP-ribosylation factor (ARF) GTPase-activating proteins (GAPs; ARFGAPs) hav
The American Society for Cell Biology.
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9. Hic-5-Reduced Cell Spreading on Fibronectin: Competitive Effects between Paxillin and Hic-5 through Interaction with Focal Adhesion Kinase
Hic-5 is a paxillin homologue that is localized to focal adhesion complexes. Hic-5 and paxillin share structural homology and interacting factors such as focal adhesion kinase (FAK), Pyk2/CAKβ/RAFTK, and PTP-PEST. Here, we showed that Hic-5 inhibits integrin-mediated cell spreading on fibronectin in a competitive manner with paxillin in NIH 3T3 cells. The o
American Society for Microbiology.
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10. RNF5, a RING Finger Protein That Regulates Cell Motility by Targeting Paxillin Ubiquitination and Altered Localization
RNF5 is a RING finger protein found to be important in the growth and development of Caenorhabditis elegans. The search for RNF5-associated proteins via a yeast two-hybrid screen identified a LIM-containing protein in C. elegans which shows homology with human paxillin. Here we demonstrate that the human homologue of RNF5 associates with the amino-terminal d
American Society for Microbiology.
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11. The bovine papillomavirus E6 oncoprotein interacts with paxillin and disrupts the actin cytoskeleton
The E6 oncoprotein of bovine papillomavirus type 1 (BPV-1) has been shown to transform cells through a p53-independent pathway, but its transforming mechanism is unknown. Here we demonstrate in vitro and in vivo interactions between BPV-1 E6 and the focal adhesion protein paxillin. The ability of BPV-1 E6 to complex with paxillin correlated with its ability
The National Academy of Sciences of the USA.
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12. Crk Associates with a Multimolecular Paxillin/GIT2/β-PIX Complex and Promotes Rac-dependent Relocalization of Paxillin to Focal Contacts
We have previously demonstrated that the CrkII and CrkL adapter proteins are required for the spreading of epithelial colonies and the breakdown of adherens junctions in response to hepatocyte growth factor. When overexpressed, CrkII and CrkL promote lamellipodia formation, cell spreading, and the loss of epithelial adherens junctions in the absence of h
The American Society for Cell Biology.