Structures of SAS-6 suggest its organization in centrioles.

Symplectic ID
115738
Source
PubMed
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1
Last Synced with Symplectic
Sunday, 13 September, 2026 - 08:05
DOI
10.1126/science.1199325
Publication Date
Friday, 4 March, 2011
First Page
1196
Last Page
1199
Keywords
Amino Acid Motifs
Animals
Cell Cycle Proteins
Cell Line, Tumor
Centrioles
Centrosome
Chlamydomonas reinhardtii
Chromosomal Proteins, Non-Histone
Crystallography, X-Ray
Flagella
Humans
Hydrophobic and Hydrophilic Interactions
Models, Molecular
Mutant Proteins
Point Mutation
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Tertiary
Recombinant Proteins
Zebrafish
Zebrafish Proteins
Authors
van Breugel, M
Hirono, M
Andreeva, A
Yanagisawa, H-A
Yamaguchi, S
Nakazawa, Y
Morgner, N
Petrovich, M
Ebong, I-O
Robinson, CV
Johnson, CM
Veprintsev, D
Authors list has been truncated
1
Editors list has been truncated
Abstract
Centrioles are cylindrical, ninefold symmetrical structures with peripheral triplet microtubules strictly required to template cilia and flagella. The highly conserved protein SAS-6 constitutes the center of the cartwheel assembly that scaffolds centrioles early in their biogenesis. We determined the x-ray structure of the amino-terminal domain of SAS-6 from zebrafish, and we show that recombinant SAS-6 self-associates in vitro into assemblies that resemble cartwheel centers. Point mutations are consistent with the notion that centriole formation in vivo depends on the interactions that define the self-assemblies observed here. Thus, these interactions are probably essential to the structural organization of cartwheel centers.
Journal Title
Science
eISSN
1095-9203
Volume
331
Issue
6021
ID at Source
21273447
Publication Status
Published
Open access
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chem0596