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• W50259775 abstract "Research Article1 August 1993free access The N-terminal region of GAP regulates cytoskeletal structure and cell adhesion. J. McGlade J. McGlade Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author B. Brunkhorst B. Brunkhorst Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author D. Anderson D. Anderson Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author G. Mbamalu G. Mbamalu Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author J. Settleman J. Settleman Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author S. Dedhar S. Dedhar Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author M. Rozakis-Adcock M. Rozakis-Adcock Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author L.B. Chen L.B. Chen Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author T. Pawson T. Pawson Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author J. McGlade J. McGlade Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author B. Brunkhorst B. Brunkhorst Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author D. Anderson D. Anderson Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author G. Mbamalu G. Mbamalu Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author J. Settleman J. Settleman Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author S. Dedhar S. Dedhar Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author M. Rozakis-Adcock M. Rozakis-Adcock Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author L.B. Chen L.B. Chen Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author T. Pawson T. Pawson Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. Search for more papers by this author Author Information J. McGlade1, B. Brunkhorst1, D. Anderson1, G. Mbamalu1, J. Settleman1, S. Dedhar1, M. Rozakis-Adcock1, L.B. Chen1 and T. Pawson1 1Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada. The EMBO Journal (1993)12:3073-3081https://doi.org/10.1002/j.1460-2075.1993.tb05976.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info Ras GTPase activating protein (GAP) possesses a C-terminal domain that interacts with GTP-bound Ras, and an N-terminal region containing two SH2 domains and an SH3 domain. In addition to its association with Ras, GAP binds stably to autophosphorylated beta PDGF receptors, and to two cytoplasmic phosphoproteins: p62, an RNA binding protein, and p190, which possesses GAP activity towards small guanine nucleotide binding proteins in the Rho/Rac family. To define the region of GAP that mediates these interactions with cellular phosphoproteins, and to investigate the biological significance of these complexes, a truncated GAP polypeptide (GAP-N) containing residues 1–445 was stably expressed in Rat-2 fibroblasts. GAP-N contains the SH2 and SH3 domains, but lacks the Ras GTPase activating domain. Stimulation of cells expressing GAP-N with PDGF induced association of GAP-N with the beta PDGF receptor, and phosphorylation of GAP-N on tyrosine, consistent with the notion that GAP SH2 domains direct binding to the autophosphorylated beta PDGF receptor in vivo. GAP-N bound constitutively to p190 in both serum-deprived and growth factor-stimulated cells. This GAP-N-p190 complex had Rho GAP activity in vitro. The expression of GAP-N in Rat-2 cells correlated with changes in the cytoskeleton and in cell adhesion, typified by the disruption of action stress fibres, a reduction in focal contacts, and an impaired ability to adhere to fibronectin. These results suggest that the N-terminal domain of GAP can direct interactions with cellular phosphoproteins in vivo, and thereby exert an effector function which modulates the cytoskeleton and cell adhesion.(ABSTRACT TRUNCATED AT 250 WORDS) Previous ArticleNext Article Volume 12Issue 81 August 1993In this issue RelatedDetailsLoading ..." @default.
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• W50259775 title "The N-terminal region of GAP regulates cytoskeletal structure and cell adhesion." @default.
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