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Sci. Signal., 29 November 2011
Vol. 4, Issue 201, p. rs13
[DOI: 10.1126/scisignal.2002189]


Editor's Summary

A GAP in the Network
The activity of Rho family small guanosine triphosphatases (GTPases), which play prominent roles in regulating such processes as cytoskeletal organization, is regulated by their associated GAPs (GTPase activating proteins) and GEFs (guanine nucleotide exchange factors). Many Rho GAPs contain SH3 domains, enabling them to undergo transient interactions with various binding partners, which in turn can influence their subcellular location and the specific signaling pathways with which they interact. Okada et al. used a domain-based proteomics approach to identify possible binding partners for nine Rho GAPs and combined their data with information culled from the literature to construct networks of associated proteins, providing insight into potential functions of the different GAPs. Further characterization of the predicted function of one GAP, WRP, enabled the authors to identify a role for this GAP in determining the structure of inhibitory GABAergic synapses.

Citation: H. Okada, A. Uezu, F. M. Mason, E. J. Soderblom, M. A. Moseley, III, S. H. Soderling, SH3 Domain–Based Phototrapping in Living Cells Reveals Rho Family GAP Signaling Complexes. Sci. Signal. 4, rs13 (2011).

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Modified SH2 domain to phototrap and identify phosphotyrosine proteins from subcellular sites within cells.
A. Uezu, H. Okada, H. Murakoshi, C. D. del Vescovo, R. Yasuda, D. Diviani, and S. H. Soderling (2012)
PNAS 109, E2929-E2938
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