Eugene E. Marcantonio
Columbia University
23 Papers
244 Citations
Eugene E. Marcantonio is an academic researcher from Columbia University. The author has contributed to research in topics: Integrin & Focal adhesion. The author has an hindex of 14, co-authored 23 publications.
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Papers
The Adaptor Protein Shc Couples a Class of Integrins to the Control of Cell Cycle Progression
Kishore K. Wary,Fabrizio Mainiero,Steven J. Isakoff,Eugene E. Marcantonio,Filippo G. Giancotti +4 more
TL;DR: It is shown that the association of specific integrins with Shc regulates cell survival and cell cycle progression and that Shc is necessary and sufficient for activation of the MAP kinase pathway in response to integrin ligation.
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Src SH2 Arginine 175 Is Required for Cell Motility: Specific Focal Adhesion Kinase Targeting and Focal Adhesion Assembly Function
Myeong Gu Yeo,Michael A. Partridge,Ellen J. Ezratty,Qiong Shen,Gregg G. Gundersen,Eugene E. Marcantonio +5 more
TL;DR: Rec recapitulate wild-type motile behavior and FA formation by directing the kinase to FAs, clearly implicating the SH2 domain in recruitment to FAK and indicating that this targeting capacity, and not simply Src-FAK scaffolding, was critical for normal Src function.
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Assembly and function of integrin receptors is dependent on opposing alpha and beta cytoplasmic domains.
TL;DR: It is shown that proper integrin assembly requires opposed alpha and beta cytoplasmic domains, and this opposition prevents ligand-independent focal contact localization.
Integrin beta 1 cytoplasmic domain dominant negative effects revealed by lysophosphatidic acid treatment.
TL;DR: Results imply that a beta 1 cytoplasmic domain, which is uncoupled from adhesion, can compete with the cytopalasmicdomain of native integrin beta 1 for cytoskeletal proteins.
Role of the I‐domain in collagen binding specificity and activation of the integrins α1β1 and α2β1
TL;DR: It is found that introducing the α2 I domain into α1 results in surface expression of a functional collagen receptor, and collagen adhesion of NIH‐3T3 mediated by α2β1 or α1‐2‐1β1, but not by α1, requires the presence of Mn2+ ions.
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