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Scaffold Proteins: Hubs for Controlling the Flow of Cellular Information

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Journal Science
Specialty Science
Date 2011 May 10
PMID 21551057
Citations 404
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Abstract

The spatial and temporal organization of molecules within a cell is critical for coordinating the many distinct activities carried out by the cell. In an increasing number of biological signaling processes, scaffold proteins have been found to play a central role in physically assembling the relevant molecular components. Although most scaffolds use a simple tethering mechanism to increase the efficiency of interaction between individual partner molecules, these proteins can also exert complex allosteric control over their partners and are themselves the target of regulation. Scaffold proteins offer a simple, flexible strategy for regulating selectivity in pathways, shaping output behaviors, and achieving new responses from preexisting signaling components. As a result, scaffold proteins have been exploited by evolution, pathogens, and cellular engineers to reshape cellular behavior.

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References
1.
DeLisa M, Conrado R . Synthetic metabolic pipelines. Nat Biotechnol. 2009; 27(8):728-9. DOI: 10.1038/nbt0809-728. View

2.
McKay M, Ritt D, Morrison D . Signaling dynamics of the KSR1 scaffold complex. Proc Natl Acad Sci U S A. 2009; 106(27):11022-7. PMC: 2708738. DOI: 10.1073/pnas.0901590106. View

3.
Winters M, Lamson R, Nakanishi H, Neiman A, Pryciak P . A membrane binding domain in the ste5 scaffold synergizes with gbetagamma binding to control localization and signaling in pheromone response. Mol Cell. 2005; 20(1):21-32. DOI: 10.1016/j.molcel.2005.08.020. View

4.
Dickens M, Rogers J, Cavanagh J, Raitano A, Xia Z, Halpern J . A cytoplasmic inhibitor of the JNK signal transduction pathway. Science. 1997; 277(5326):693-6. DOI: 10.1126/science.277.5326.693. View

5.
Bhattacharyya R, Remenyi A, Yeh B, Lim W . Domains, motifs, and scaffolds: the role of modular interactions in the evolution and wiring of cell signaling circuits. Annu Rev Biochem. 2006; 75:655-80. DOI: 10.1146/annurev.biochem.75.103004.142710. View