Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/14486
Title: Components of the Hippo pathway cooperate with Nek2 kinase to regulate centrosome disjunction
Authors: Mardin, Balca R.
Lange, Cornelia
Baxter, Joanne E.
Hardy, Tara
Scholz, Sebastian R.
Fry, Andrew M.
Schiebel, Elmar
First Published: 14-Nov-2010
Publisher: Nature Publishing Group
Citation: Nature Cell Biology, 2010, 12 (12), pp. 1166-1176
Abstract: During interphase, centrosomes are held together by a proteinaceous linker that connects the proximal ends of the mother and daughter centriole. This linker is disassembled at the onset of mitosis in a process known as centrosome disjunction, thereby facilitating centrosome separation and bipolar spindle formation. The NIMA (never in mitosis A)-related kinase Nek2A is implicated in disconnecting the centrosomes through disjoining the linker proteins C-Nap1 and rootletin. However, the mechanisms controlling centrosome disjunction remain poorly understood. Here, we report that two Hippo pathway components, the mammalian sterile 20-like kinase 2 (Mst2) and the scaffold protein Salvador (hSav1), directly interact with Nek2A and regulate its ability to localize to centrosomes, and phosphorylate C-Nap1 and rootletin. Furthermore, we demonstrate that the hSav1–Mst2–Nek2A centrosome disjunction pathway becomes essential for bipolar spindle formation on partial inhibition of the kinesin-5 Eg5. We propose that hSav1–Mst2–Nek2A and Eg5 have distinct, but complementary functions, in centrosome disjunction.
DOI Link: 10.1038/ncb2120
ISSN: 1465-7392
eISSN: 1476-4679
Links: http://hdl.handle.net/2381/14486
http://www.nature.com/ncb/journal/v12/n12/full/ncb2120.html
Version: Post-print
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © 2010 Macmillan Publishers Limited. All rights reserved. Deposited with reference to the publisher’s open access archiving policy.
Appears in Collections:Published Articles, Dept. of Biochemistry

Files in This Item:
File Description SizeFormat 
FRYhippo.pdfPost-review (final submitted)1.2 MBAdobe PDFView/Open


Items in LRA are protected by copyright, with all rights reserved, unless otherwise indicated.