Einzeltreffer — DigiBib

Mitochondrial structure and distribution are regulated by division and fusion events. Mitochondrial division is regulated by Dnm1/Drp1, a dynamin-related protein that forms helices around mitochondria to mediate fission. Little is known about what determines sites of mitochondrial fission within the mitochondrial network. The endoplasmic reticulum (ER) and mitochondria exhibit tightly coupled dynamics and have extensive contacts. We tested whether ER plays a role in mitochondrial division. We found that mitochondrial division occurred at positions where ER tubules contacted mitochondria and mediated constriction before Drp1 recruitment. Thus, ER tubules may play an active role in defining the position of mitochondrial division sites.

Titel:	ER tubules mark sites of mitochondrial division.
Autor/in / Beteiligte Person:	Friedman, JR ; Lackner, LL ; West, M ; DiBenedetto, JR ; Nunnari, J ; Voeltz, GK
Link:	Volltext (PDF)
Zeitschrift:	Science (New York, N.Y.), Jg. 334 (2011-10-21), Heft 6054, S. 358-62
Veröffentlichung:	<Oct. 4, 1991- > : Washington, DC : American Association for the Advancement of Science ; <i>Original Publication</i>: New York, N.Y. : [s.n.] 1880-, 2011
Medientyp:	academicJournal
ISSN:	1095-9203 (electronic)
DOI:	10.1126/science.1207385
Schlagwort:	Animals COS Cells Chlorocebus aethiops Dynamins GTP Phosphohydrolases genetics GTP Phosphohydrolases metabolism Humans Membrane Proteins genetics Membrane Proteins metabolism Microscopy, Electron Microscopy, Fluorescence Microtubule-Associated Proteins genetics Microtubule-Associated Proteins metabolism Mitochondria ultrastructure Mitochondrial Proteins genetics Mitochondrial Proteins metabolism Saccharomyces cerevisiae Proteins genetics Saccharomyces cerevisiae Proteins metabolism Transfection Endoplasmic Reticulum physiology Endoplasmic Reticulum ultrastructure Mitochondria physiology Saccharomyces cerevisiae ultrastructure
Sonstiges:	Nachgewiesen in: MEDLINE Sprachen: English Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't Language: English [Science] 2011 Oct 21; Vol. 334 (6054), pp. 358-62. <i>Date of Electronic Publication: </i>2011 Sep 01. MeSH Terms: Endoplasmic Reticulum / physiology ; Endoplasmic Reticulum / ultrastructure ; Mitochondria / physiology ; Saccharomyces cerevisiae / ultrastructure ; Animals ; COS Cells ; Chlorocebus aethiops ; Dynamins ; GTP Phosphohydrolases / genetics ; GTP Phosphohydrolases / metabolism ; Humans ; Membrane Proteins / genetics ; Membrane Proteins / metabolism ; Microscopy, Electron ; Microscopy, Fluorescence ; Microtubule-Associated Proteins / genetics ; Microtubule-Associated Proteins / metabolism ; Mitochondria / ultrastructure ; Mitochondrial Proteins / genetics ; Mitochondrial Proteins / metabolism ; Saccharomyces cerevisiae Proteins / genetics ; Saccharomyces cerevisiae Proteins / metabolism ; Transfection Comments: Comment in: Nat Rev Mol Cell Biol. 2011 Oct;12(10):627. (PMID: 21941274) References: J Biol Chem. 2006 Jan 27;281(4):2177-83. (PMID: 16272155) ; J Cell Biol. 1999 Nov 15;147(4):699-706. (PMID: 10562274) ; Mol Biol Cell. 2001 Aug;12(8):2245-56. (PMID: 11514614) ; J Cell Biol. 2010 Dec 13;191(6):1141-58. (PMID: 21149567) ; J Cell Biol. 2000 Aug 7;150(3):461-74. (PMID: 10931860) ; Nat Struct Mol Biol. 2011 Jan;18(1):20-6. (PMID: 21170049) ; Science. 2009 Jul 24;325(5939):477-81. (PMID: 19556461) ; Mol Biol Cell. 2008 Jun;19(6):2402-12. (PMID: 18353969) ; Mol Biol Cell. 2001 Sep;12(9):2894-905. (PMID: 11553726) ; Mol Biol Cell. 2009 Aug;20(15):3525-32. (PMID: 19477917) ; EMBO J. 2010 Aug 18;29(16):2715-23. (PMID: 20717141) ; Cell. 2006 Feb 10;124(3):573-86. (PMID: 16469703) ; J Cell Biol. 2001 Apr 2;153(1):47-62. (PMID: 11285273) ; Nature. 2008 Dec 4;456(7222):605-10. (PMID: 19052620) ; J Cell Biol. 2005 Sep 26;170(7):1021-7. (PMID: 16186251) ; Traffic. 2011 Jan;12(1):28-41. (PMID: 20955502) ; Sci Signal. 2009 Aug 18;2(84):ra47. (PMID: 19690333) ; Science. 2009 Aug 14;325(5942):874-7. (PMID: 19679814) ; Mol Biol Cell. 2003 May;14(5):1953-63. (PMID: 12802067) ; Antioxid Redox Signal. 2011 Feb 1;14(3):439-57. (PMID: 20518704) ; J Cell Biol. 2010 Aug 9;190(3):363-75. (PMID: 20696706) ; Mol Cell. 1999 Nov;4(5):815-26. (PMID: 10619028) ; J Struct Biol. 1996 Jan-Feb;116(1):71-6. (PMID: 8742726) ; J Cell Biol. 2011 Apr 18;193(2):333-46. (PMID: 21502358) ; Biochim Biophys Acta. 2009 Dec;1792(12):1138-44. (PMID: 19100831) ; Cell Mol Life Sci. 2010 Oct;67(20):3435-47. (PMID: 20577776) ; J Biol Chem. 2008 Jul 4;283(27):18892-904. (PMID: 18442980) ; Yeast. 2000 Nov;16(15):1421-7. (PMID: 11054823) Grant Information: T32 GM008759 United States GM NIGMS NIH HHS; GM08759 United States GM NIGMS NIH HHS; R01 GM083977 United States GM NIGMS NIH HHS; R01 GM062942 United States GM NIGMS NIH HHS; T32 GM142607 United States GM NIGMS NIH HHS Substance Nomenclature: 0 (Membrane Proteins) ; 0 (Mff protein, human) ; 0 (Microtubule-Associated Proteins) ; 0 (Mitochondrial Proteins) ; 0 (Saccharomyces cerevisiae Proteins) ; EC 3.6.1.- (GTP Phosphohydrolases) ; EC 3.6.5.5 (DNM1 protein, S cerevisiae) ; EC 3.6.5.5 (DNM1L protein, human) ; EC 3.6.5.5 (Dynamins) Entry Date(s): Date Created: 20110903 Date Completed: 20111031 Latest Revision: 20220408 Update Code: 20231215 PubMed Central ID: PMC3366560

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ER tubules mark sites of mitochondrial division.