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Publication Abstract from PubMed

Microtubule nucleation in all eukaryotes involves gamma-tubulin small complexes (gammaTuSCs) that comprise two molecules of gamma-tubulin bound to gamma-tubulin complex proteins (GCPs) GCP2 and GCP3. In many eukaryotes, multiple gammaTuSCs associate with GCP4, GCP5 and GCP6 into large gamma-tubulin ring complexes (gammaTuRCs). Recent cryo-EM studies indicate that a scaffold similar to gammaTuRCs is formed by lateral association of gammaTuSCs, with the C-terminal regions of GCP2 and GCP3 binding gamma-tubulin molecules. However, the exact role of GCPs in microtubule nucleation remains unknown. Here we report the crystal structure of human GCP4 and show that its C-terminal domain binds directly to gamma-tubulin. The human GCP4 structure is the prototype for all GCPs, as it can be precisely positioned within the gammaTuSC envelope, revealing the nature of protein-protein interactions and conformational changes regulating nucleation activity.

Crystal structure of gamma-tubulin complex protein GCP4 provides insight into microtubule nucleation.,Guillet V, Knibiehler M, Gregory-Pauron L, Remy MH, Chemin C, Raynaud-Messina B, Bon C, Kollman JM, Agard DA, Merdes A, Mourey L Nat Struct Mol Biol. 2011 Jul 3;18(8):915-9. doi: 10.1038/nsmb.2083. PMID:21725292^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.