JCB logo
MBL International Tel: 800.200.5459 CLICK HERE
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published online
doi:10.1083/jcb.200705197
The Journal of Cell Biology, Vol. 179, No. 3, 423-436
The Rockefeller University Press, 0021-9525 $30.00
© Maekawa et al.
This Article
Right arrow Full Text
Right arrow Full Text (PDF, 4981K)
Right arrow PPT slides of all figures
Right arrow Supplemental Material Index
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Maekawa, H.
Right arrow Articles by Schiebel, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Maekawa, H.
Right arrow Articles by Schiebel, E.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

Article

The yeast centrosome translates the positional information of the anaphase spindle into a cell cycle signal



Hiromi Maekawa1, Claire Priest3, Johannes Lechner2, Gislene Pereira4, and Elmar Schiebel1

1 Zentrum für Molekulare Biologie and 2 Biochemie-Zentrum, Universität Heidelberg, 69120 Heidelberg, Germany
3 The Paterson Institute for Cancer Research, Manchester M20 4BX, UK
4 German Cancer Research Centre, 69120 Heidelberg, Germany

Correspondence to Gislene Pereira: g.pereira{at}dkfz-heidelberg.de; or Elmar Schiebel: e.schiebel{at}zmbh.uni-heidelberg.de

The spindle orientation checkpoint (SPOC) of budding yeast delays mitotic exit when cytoplasmic microtubules (MTs) are defective, causing the spindle to become misaligned. Delay is achieved by maintaining the activity of the Bfa1–Bub2 guanosine triphosphatase–activating protein complex, an inhibitor of mitotic exit. In this study, we show that the spindle pole body (SPB) component Spc72, a transforming acidic coiled coil–like molecule that interacts with the {gamma}-tubulin complex, recruits Kin4 kinase to both SPBs when cytoplasmic MTs are defective. This allows Kin4 to phosphorylate the SPB-associated Bfa1, rendering it resistant to inactivation by Cdc5 polo kinase. Consistently, forced targeting of Kin4 to both SPBs delays mitotic exit even when the anaphase spindle is correctly aligned. Moreover, we present evidence that Spc72 has an additional function in SPOC regulation that is independent of the recruitment of Kin4. Thus, Spc72 provides a missing link between cytoplasmic MT function and components of the SPOC.

Abbreviations used in this paper: CBB, Coomassie brilliant blue; GAP, GTPase-activating protein; MALDI-TOF, matrix-assisted laser desorption ionization–time of flight; MBP, maltose-binding protein; MEN, mitotic exit network; MT, microtubule; SPB, spindle pole body; SPOC, spindle orientation checkpoint; TACC, transforming acidic coiled coil.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents