Article abstract


Nature Cell Biology 10, 395 - 406 (2008)
Published online: 16 March 2008 | doi:10.1038/ncb1701

Inn1 couples contraction of the actomyosin ring to membrane ingression during cytokinesis in budding yeast

Alberto Sanchez-Diaz1, Vanessa Marchesi1, Stephen Murray1, Richard Jones2,3, Gislene Pereira1,4, Ricky Edmondson2,5, Terry Allen1 & Karim Labib1


By rapidly depleting each of the essential budding yeast proteins of unknown function, we identified a novel factor that we call Inn1, which associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis. We show that Inn1 has a C2 domain at the amino terminus of the protein that is required for ingression of the plasma membrane, whereas the remainder of the protein recruits Inn1 to the actomyosin ring. The lethal effects of deleting the INN1 gene can be suppressed by artificial fusion of the C2 domain to other components of the actomyosin ring, restoring membrane ingression on contraction of the actomyosin ring. Our data indicate that recruitment of the C2 domain of Inn1 to the contractile actomyosin ring is crucial for ingression of the plasma membrane during cytokinesis in budding yeast.

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  1. Cancer Research U.K., Paterson Institute for Cancer Research, University of Manchester, Wilmslow Road, Manchester, M20 4BX, UK.
  2. FDA-NCTR, 3900 NCTR Road, Jefferson, AR 72079, USA.
  3. Current address: NextGen Sciences, Inc., 4401 Varsity Drive, Suite E, Ann Arbor, MI 48108, USA.
  4. Current address: German Cancer Research Centre, Im Neuenheimer Feld 581, 69120 Heidelberg, Germany.
  5. Current address: Myeloma Institute for Research and Therapy, University of Arkansas for Medical Sciences, 4301 W.Markham #776, Little Rock, AR 72205, USA.

Correspondence to: Karim Labib1 e-mail: klabib@picr.man.ac.uk



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