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- W2067635861 endingPage "411" @default.
- W2067635861 startingPage "395" @default.
- W2067635861 abstract "Cell motility is induced by many growth factors acting through cognate receptors with intrinsic tyrosine kinase activity (RPTK). However, most of the links between receptor activation and the biophysical processes of cell motility remain undeciphered. We have focused on the mechanisms by which the EGF receptor (EGFR) actuates fibroblast cell motility in an attempt to define this integrated process in one system. Our working model is that divergent, but interconnected pathways lead to the biophysical processes necessary for cell motility: cytoskeleton reorganization, membrane extension, formation of new adhesions to substratum, cell contraction, and release of adhesions at the rear. We postulate that for any given growth factor some of the pathways/processes will be actively signaled and rate-limiting, while others will be permissive due to background low-level activation. Certain couplings have been defined, such as PLCgamma and actin modifying proteins being involved in cytoskeletal reorganization and lamellipod extension and MEK being implicated in detachment from substratum. Others are suggested by complementary investigations in integrin-mediated motility, including rac in membrane protrusion, rho in new adhesions, myosin II motors in contraction, and calpain in detachment, but have yet to be placed in growth factor-induced motility. Our model postulates that many biochemical pathways will be shared between chemokinetic and haptokinetic motility but that select pathways will be activated only during RPTK-enhanced motility." @default.
- W2067635861 created "2016-06-24" @default.
- W2067635861 creator A5022592413 @default.
- W2067635861 creator A5038986832 @default.
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- W2067635861 creator A5059014214 @default.
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- W2067635861 creator A5087720227 @default.
- W2067635861 date "1998-12-01" @default.
- W2067635861 modified "2023-10-06" @default.
- W2067635861 title "Epidermal growth factor receptor-mediated motility in fibroblasts" @default.
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