Abstract
We previously reported that leucine-rich repeat and fibronectin type III domain-containing 4 (LRFN4) functioned in migration and morphological change (i.e. cell elongation) of monocytic cells. Here, we examined a molecular mechanism regulating LRFN4-mediated cell elongation. We found that 14-3-3 and NCK proteins complexed with LRFN4, and they were involved in LRFN4-mediated cell elongation. We also identified the regions of LRFN4 interacting with NCK1 and 14-3-3s. Finally, we demonstrated that a Rac1 small GTPase was involved in LRFN4-mediated cell elongation. These results indicated that LRFN4 complexed with 14-3-3s and NCK1 to mediate elongation in monocytic cells via Rac-1-mediated actin cytoskeleton reorganization.
Copyright © 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
MeSH terms
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14-3-3 Proteins / chemistry*
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14-3-3 Proteins / metabolism
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Actins / metabolism
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Adaptor Proteins, Signal Transducing / chemistry*
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Adaptor Proteins, Signal Transducing / metabolism
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Cell Membrane / metabolism
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Cytoplasm / metabolism
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Cytoskeleton / metabolism
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Dose-Response Relationship, Drug
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HEK293 Cells
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HeLa Cells
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Humans
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Membrane Glycoproteins / chemistry*
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Membrane Glycoproteins / metabolism
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Microscopy, Fluorescence / methods
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Models, Biological
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Monocytes / cytology
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Nerve Tissue Proteins / chemistry*
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Nerve Tissue Proteins / metabolism
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Neurons / metabolism
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Oncogene Proteins / chemistry*
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Oncogene Proteins / metabolism
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Protein Binding
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Protein Isoforms
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rac1 GTP-Binding Protein / metabolism*
Substances
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14-3-3 Proteins
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Actins
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Adaptor Proteins, Signal Transducing
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LRFN4 protein, human
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Membrane Glycoproteins
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Nck protein
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Nerve Tissue Proteins
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Oncogene Proteins
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Protein Isoforms
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RAC1 protein, human
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rac1 GTP-Binding Protein