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Type: Journal article
Title: A direct interaction with NEDD1 regulates γ-tubulin recruitment to the centrosome
Other Titles: A direct interaction with NEDD1 regulates gamma-tubulin recruitment to the centrosome
Author: Manning, J.
Shalini, S.
Risk, J.
Day, C.
Kumar, S.
Citation: PLoS One, 2010; 5(3):1-12
Publisher: Public Library of Science
Issue Date: 2010
ISSN: 1932-6203
Editor: Hotchin, N.A.
Statement of
Jantina A. Manning, Sonia Shalini, Joanna M. Risk, Catherine L. Day and Sharad Kumar
Abstract: The centrosome is the primary microtubule organizing centre of the cell. γ-tubulin is a core component of the centrosome and is required for microtubule nucleation and centrosome function. The recruitment of γ-tubulin to centrosomes is mediated by its interaction with NEDD1, a WD40-repeat containing protein. Here we demonstrate that NEDD1 is likely to be oligomeric in vivo and binds directly to γ-tubulin through a small region of just 62 residues at the carboxyl-terminus of the protein. This carboxyl-terminal domain that binds γ-tubulin has a helical structure and is a stable tetramer in solution. Mutation of residues in NEDD1 that disrupt binding to γ-tubulin result in a mis-localization of γ-tubulin away from the centrosome. Hence, this study defines the binding site on NEDD1 that is required for its interaction with γ-tubulin, and shows that this interaction is required for the correct localization of γ-tubulin.
Keywords: Cell Line
NIH 3T3 Cells
Microtubule-Associated Proteins
Circular Dichroism
Binding Sites
Protein Structure, Tertiary
Protein Binding
Scattering, Radiation
Rights: © 2010 Manning et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
DOI: 10.1371/journal.pone.0009618
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