Journal
EMBO JOURNAL
Volume 22, Issue 5, Pages 1125-1133Publisher
WILEY
DOI: 10.1093/emboj/cdg110
Keywords
crystallography; fluorescence; NMR; polarity; Rho GTPases
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Funding
- NCI NIH HHS [P01 CA040042, CA40042] Funding Source: Medline
- NIGMS NIH HHS [R01 GM056322, R01 GM070902, GM56322] Funding Source: Medline
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Cdc42 is a small GTPase that is required for cell polarity establishment in eukaryotes as diverse as budding yeast and mammals. Par6 is also implicated in metazoan cell polarity establishment and asymmetric cell divisions. Cdc42.GTP interacts with proteins that contain a conserved sequence called a CRIB motif. Uniquely, Par6 possesses a semi-CRIB motif that is not sufficient for binding to Cdc42. An adjacent PDZ domain is also necessary and is required for biological effects of Par6. Here we report the crystal structure of a complex between Cdc42 and the Par6 GTPase-binding domain. The semi-CRIB motif forms a beta-strand that inserts between the four strands of Cdc42 and the three strands of the PDZ domain to form a continuous eight-stranded sheet. Cdc42 induces a conformational change in Par6, detectable by fluorescence resonance energy transfer spectroscopy. Nuclear magnetic resonance studies indicate that the semi-CRIB motif of Par6 is at least partially structured by the PDZ domain. The structure highlights a novel role for a PDZ domain as a structural scaffold.
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