Tara, a novel F-actin binding protein, associates with the Trio guanine nucleotide exchange factor and regulates actin cytoskeletal organization
| العنوان: | Tara, a novel F-actin binding protein, associates with the Trio guanine nucleotide exchange factor and regulates actin cytoskeletal organization |
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| المؤلفون: | Elizabeth Iannotti, Katja Seipel, Stephen J. O'Brien, Quintus G. Medley, Michel Streuli |
| المصدر: | Journal of Cell Science. 114:389-399 |
| بيانات النشر: | The Company of Biologists, 2001. |
| سنة النشر: | 2001 |
| مصطلحات موضوعية: | Recombinant Fusion Proteins, Molecular Sequence Data, macromolecular substances, Protein Serine-Threonine Kinases, Biology, Transfection, Cell morphology, GTP-Binding Proteins, Chlorocebus aethiops, Animals, Drosophila Proteins, Guanine Nucleotide Exchange Factors, Humans, Amino Acid Sequence, Muscle, Skeletal, Cytoskeleton, Actin, Gene Library, Sequence Homology, Amino Acid, Microfilament Proteins, Actin cytoskeleton reorganization, Actin remodeling, Cell Biology, Fibroblasts, Phosphoproteins, Actin cytoskeleton, Actins, Cell biology, COS Cells, Latrunculin, Guanine nucleotide exchange factor, Sequence Alignment, Cytokinesis, HeLa Cells |
| الوصف: | Reorganization of the actin cytoskeleton is essential to numerous cellular processes including cell locomotion and cytokinesis. This actin remodeling is regulated in part by Rho family GTPases. Previous studies implicated Trio, a Dbl-homology guanine nucleotide exchange factor with two exchange factor domains, in regulating actin cytoskeleton reorganization, cell motility and cell growth via activation of Rho GTPases. Trio is essential for mouse embryonic development and Trio-deficiency is associated with abnormal skeletal muscle and neural tissue development. Furthermore, genetic analyses in Caenorhabditis elegans and Drosophila demonstrate a role for trio-like genes in cell migration and axon guidance. Herein we characterize a novel Trio-binding protein, Tara, that is comprised of an N-terminal pleckstrin homology domain and a C-terminal coiled-coil region. Trio and Tara associate as assessed by the yeast interaction-trap assays and mammalian co-immunoprecipitation studies. Ectopically expressed Tara localizes to F-actin in a periodic pattern that is highly similar to the pattern of myosin II. Furthermore, a direct interaction between Tara and F-actin is indicated by in vitro binding studies. Cells that transiently or stably overexpress Tara display an extensively flattened cell morphology with enhanced stress fibers and cortical F-actin. Tara expression does not alter the ability of the cell to attach or to initially spread, but rather increases cell spreading following these initial events. Tara stabilizes F-actin structures as indicated by the relative resistance of Tara-expressing cells to the F-actin destabilizer Latrunculin B. We propose that Tara regulates actin cytoskeletal organization by directly binding and stabilizing F-actin, and that the localized formation of Tara and Trio complexes functions to coordinate actin remodeling. |
| تدمد: | 1477-9137 0021-9533 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::59ca29ec3c4ab17e463eb8b730cb2d53Test https://doi.org/10.1242/jcs.114.2.389Test |
| رقم الانضمام: | edsair.doi.dedup.....59ca29ec3c4ab17e463eb8b730cb2d53 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 14779137 00219533 |
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