Journal
STRUCTURE
Volume 21, Issue 11, Pages 2069-2077Publisher
CELL PRESS
DOI: 10.1016/j.str.2013.08.019
Keywords
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Funding
- Wellcome Trust [094872/Z/10/Z, 092970MA, 088497/Z/09/Z]
- Biotechnology and Biological Sciences Research Council [BB/J008265/1, BB/1019855/1]
- Marie Curie Intra-European Fellowship [235532]
- BBSRC [BB/J008265/1] Funding Source: UKRI
- Wellcome Trust [088497/Z/09/Z, 094872/Z/10/Z] Funding Source: Wellcome Trust
- Biotechnology and Biological Sciences Research Council [BB/J008265/1] Funding Source: researchfish
- Engineering and Physical Sciences Research Council [1104702] Funding Source: researchfish
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Centrioles are evolutionarily conserved eukaryotic organelles composed of a protein scaffold surrounded by sets of microtubules organized with a 9-fold radial symmetry. CPAP, a centriolar protein essential for microtubule recruitment, features a C-terminal domain of unknown structure, the G-box. A missense mutation in the G-box reduces affinity for the centriolar shuttling protein STIL and causes primary microcephaly. Here, we characterize the molecular architecture of CPAP and determine the G-box structure alone and in complex with a STIL fragment. The G-box comprises a single elongated (3 sheet capable of forming supramolecular assemblies. Structural and biophysical studies highlight the conserved nature of the CPAP-STIL complex. We propose that CPAP acts as a horizontal strut that joins the centriolar scaffold with microtubules, whereas G-box domains form perpendicular connections.
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