Journal
CHEMISTRY & BIOLOGY
Volume 18, Issue 9, Pages 1143-1152Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2011.06.013
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Funding
- Arnold and Mabel Beckman Foundation
- National Institutes of Health [R01 GM072872]
- National Science Foundation
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PDZ domains are independently folded modules that typically mediate protein-protein interactions by binding to the C termini of their target proteins. However, in a few instances, PDZ domains have been reported to dimerize with other PDZ domains. To investigate this noncanonical-binding mode further, we used protein microarrays comprising virtually every mouse PDZ domain to systematically query all possible PDZ-PDZ pairs. We then used fluorescence polarization to retest and quantify interactions and coaffinity purification to test biophysically validated interactions in the context of their full-length proteins. Overall, we discovered 37 PDZ-PDZ interactions involving 46 PDZ domains (similar to 30% of all PDZ domains tested), revealing that dimerization is a more frequently used binding mode than was previously appreciated. This suggests that many PDZ domains evolved to form multiprotein complexes by simultaneously interacting with more than one ligand.
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