Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 13, Issue 9, Pages 798-805Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1133
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Funding
- NATIONAL CANCER INSTITUTE [ZIABC010304, Z01BC010304, Z01BC003229] Funding Source: NIH RePORTER
- OFFICE OF THE DIRECTOR, NATIONAL INSTITUTES OF HEALTH [Z01OD010485] Funding Source: NIH RePORTER
- Intramural NIH HHS Funding Source: Medline
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Receptor oligomerization is vital for activating intracellular signaling, in part by initiating events that recruit effector and adaptor proteins to sites of active signaling. Whether these distal molecules themselves oligomerize is not well appreciated. In this study, we examined the molecular interactions of the adaptor protein GRB2. In T cells, the SH2 domain of GRB2 binds phosphorylated tyrosines on the adaptor protein LAT and the GRB2 SH3 domains associate with the proline-rich regions of SOS1 and CBL. Using biochemical and biophysical techniques in conjunction with confocal microscopy, we observed that the simultaneous association of GRB2, via its SH2 and SH3 domains, with multivalent ligands led to the oligomerization of these ligands, which affected signaling. These data suggest that multipoint binding of distal adaptor proteins mediates the formation of oligomeric signaling clusters vital for intracellular signaling.
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