Grb7 binds to Hax-1 and undergoes an intramolecular domain association that offers a model for Grb7 regulation.

Authors :: Siamakpour-Reihani, Sharareh
Peterson, Tabitha A.
Bradford, Andrew M.
Argiros, Haroula J.
Haas, Laura Lowell
Lor, Siamee N.
Haulsee, Zachary M.
Spuches, Anne M.
Johnson, Dennis L.
Rohrschneider, Larry R.
Shuster, Charles Brad
Lyons, Barbara A.
Source :: Journal of Molecular Recognition. Mar/Apr2011, Vol. 24 Issue 2, p314-321. 8p. 3 Diagrams, 1 Chart, 1 Graph.
Publication Year :: 2011
Abstract: The article discusses a study which identified the interaction partners of Grb7 adaptor protein potentially involved in focal adhesion kinase (FAK)/Grb7-mediated cell migration. It clarifies the role of the Grb7-Ras Associating (RA) and -Pleckstrin Homology (PH) domains in this protein and explores the phosphorylation state of Grb7 necessary for, or during, binding interactions. It also proposes a Grb7autoinhibitory mechanism based upon the results.

Subjects :: *CELL migration
*FOCAL adhesion kinase
*HOMOLOGY (Biology)
*MOLECULAR recognition
*MOLECULAR biology

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