HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 280, Issue 19, 18598-18603, May 13, 2005

This Article Full Text Full Text (PDF) All Versions of this Article: 280/19/18598    most recent M500807200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Neutzner, A. Articles by Youle, R. J. Search for Related Content PubMed PubMed Citation Articles by Neutzner, A. Articles by Youle, R. J. Social Bookmarking                      What's this?

Instability of the Mitofusin Fzo1 Regulates Mitochondrial Morphology during the Mating Response of the Yeast Saccharomyces cerevisiae^*

Albert Neutzner and Richard J. Youle

From the Biochemistry Section, Surgical Neurological Branch, NINDS, National Institutes of Health, Bethesda, Maryland 20892

Mitochondria form a highly dynamic network that is shaped by continuous fission and fusion of these organelles. In the yeast Saccharomyces cerevisiae two machineries are involved in this process, one of which includes the mitochondrial fusion promoting GTPase Fzo1. Although a role for the F-box protein Mdm30 in regulating the stability of Fzo1 has been proposed, the molecular basis for the regulation of the fission to fusion ratio of mitochondria remains unknown. To discern the mechanism of the regulation of mitochondrial morphology, we arrested cells at different stages of the cell cycle and examined mitochondrial morphology as well as the stability of mitochondrial fission and fusion proteins. In response to a G₁ arrest evoked by the mating pheromone factor the mitochondrial network fragmented into small pieces, which was accompanied by dramatic down-regulation of Fzo1. Mating pheromone also triggered the degradation of Fzo1 produced under the control of a constitutive promoter, and Fzo1 was stabilized upon proteasome inhibition, indicating a role for the proteasome system in the degradation of Fzo1. However, deletion of MDM30 did not stabilize Fzo1 after mating pheromone treatment, showing a different mechanism from the previously reported process of steady state Fzo1 regulation. We show an example for a regulated change of the mitochondrial fission to fusion ratio during the life cycle of budding yeast. Proteasomal degradation of Fzo1 in response to the mating pheromone is proposed to mediate the remodeling of the mitochondrial network during the process of mating.

Received for publication, January 21, 2005 , and in revised form, March 9, 2005.

^* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Biochemistry Section, Surgical Neurological Branch, NINDS, National Institutes of Health, 35 Convent Dr., Bethesda, MD 20892. Tel.: 301-496-6628; Fax: 301-496-3444; E-mail: youler{at}ninds.nih.gov.

CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				M. Liesa, M. Palacin, and A. Zorzano Mitochondrial Dynamics in Mammalian Health and Disease Physiol Rev, July 1, 2009; 89(3): 799 - 845. [Abstract] [Full Text] [PDF]

				D.-F. Suen, K. L. Norris, and R. J. Youle Mitochondrial dynamics and apoptosis Genes & Dev., June 15, 2008; 22(12): 1577 - 1590. [Abstract] [Full Text] [PDF]

				M. M.J. Cohen, G. P. Leboucher, N. Livnat-Levanon, M. H. Glickman, and A. M. Weissman Ubiquitin-Proteasome-dependent Degradation of a Mitofusin, a Critical Regulator of Mitochondrial Fusion Mol. Biol. Cell, June 1, 2008; 19(6): 2457 - 2464. [Abstract] [Full Text] [PDF]

				B. Westermann Molecular Machinery of Mitochondrial Fusion and Fission J. Biol. Chem., May 16, 2008; 283(20): 13501 - 13505. [Full Text] [PDF]

				N. Nakamura and S. Hirose Regulation of Mitochondrial Morphology by USP30, a Deubiquitinating Enzyme Present in the Mitochondrial Outer Membrane Mol. Biol. Cell, May 1, 2008; 19(5): 1903 - 1911. [Abstract] [Full Text] [PDF]

				T. Rinaldi, L. Hofmann, A. Gambadoro, R. Cossard, N. Livnat-Levanon, M. H. Glickman, L. Frontali, and A. Delahodde Dissection of the Carboxyl-Terminal Domain of the Proteasomal Subunit Rpn11 in Maintenance of Mitochondrial Structure and Function Mol. Biol. Cell, March 1, 2008; 19(3): 1022 - 1031. [Abstract] [Full Text] [PDF]

				M. Karbowski, A. Neutzner, and R. J. Youle The mitochondrial E3 ubiquitin ligase MARCH5 is required for Drp1 dependent mitochondrial division J. Cell Biol., October 3, 2007; 178(1): 71 - 84. [Abstract] [Full Text] [PDF]

				S. Lee, S.-Y. Jeong, W.-C. Lim, S. Kim, Y.-Y. Park, X. Sun, R. J. Youle, and H. Cho Mitochondrial Fission and Fusion Mediators, hFis1 and OPA1, Modulate Cellular Senescence J. Biol. Chem., August 3, 2007; 282(31): 22977 - 22983. [Abstract] [Full Text] [PDF]

				M. Durr, M. Escobar-Henriques, S. Merz, S. Geimer, T. Langer, and B. Westermann Nonredundant Roles of Mitochondria-associated F-Box Proteins Mfb1 and Mdm30 in Maintenance of Mitochondrial Morphology in Yeast Mol. Biol. Cell, September 1, 2006; 17(9): 3745 - 3755. [Abstract] [Full Text] [PDF]

				K. S. Dimmer and L. Scorrano (De)constructing Mitochondria: What For? Physiology, August 1, 2006; 21: 233 - 241. [Abstract] [Full Text] [PDF]

				M. Escobar-Henriques, B. Westermann, and T. Langer Regulation of mitochondrial fusion by the F-box protein Mdm30 involves proteasome-independent turnover of Fzo1 J. Cell Biol., June 5, 2006; 173(5): 645 - 650. [Abstract] [Full Text] [PDF]