Mitochondrial outer and inner membrane fusion requires a modifi ed carrier protein

Suzanne Hoppins, Jennifer Horner, Cheng Song, J. Michael McCaffery, Jodi Nunnari

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

In yeast, three proteins are essential for mitochondrial fusion. Fzo1 and Mgm1 are conserved guanosine triphosphatases that reside in the outer and inner membranes, respectively. At each membrane, these conserved proteins are required for the distinct steps of membrane tethering and lipid mixing. The third essential component is Ugo1, an outer membrane protein in the mitochondrial transport protein family. We show that Ugo1 is a modifi ed member of this family, containing three transmembrane domains and existing as a dimer, a structure that is critical for the fusion function of Ugo1. Our functional analysis of Ugo1 indicates that it is required distinctly for both outer and inner membrane fusion after membrane tethering, indicating that it operates at the lipid-mixing step of fusion. This role is distinct from the fusion dynamin-related proteins and thus demonstrates that at each membrane, a single fusion protein is not suffi cient to drive the lipid-mixing step, but instead, this step requires a more complex assembly of proteins.

Original languageEnglish (US)
Pages (from-to)569-581
Number of pages13
JournalJournal of Cell Biology
Volume184
Issue number4
DOIs
StatePublished - Feb 23 2009

Fingerprint

Membrane Fusion
Carrier Proteins
Membranes
Proteins
Mitochondrial Dynamics
Dynamins
Lipids
Guanosine
Mitochondrial Proteins
Membrane Lipids
Membrane Proteins
Yeasts

ASJC Scopus subject areas

  • Cell Biology
  • Medicine(all)

Cite this

Hoppins, S., Horner, J., Song, C., McCaffery, J. M., & Nunnari, J. (2009). Mitochondrial outer and inner membrane fusion requires a modifi ed carrier protein. Journal of Cell Biology, 184(4), 569-581. https://doi.org/10.1083/jcb.200809099

Mitochondrial outer and inner membrane fusion requires a modifi ed carrier protein. / Hoppins, Suzanne; Horner, Jennifer; Song, Cheng; McCaffery, J. Michael; Nunnari, Jodi.

In: Journal of Cell Biology, Vol. 184, No. 4, 23.02.2009, p. 569-581.

Research output: Contribution to journalArticle

Hoppins, S, Horner, J, Song, C, McCaffery, JM & Nunnari, J 2009, 'Mitochondrial outer and inner membrane fusion requires a modifi ed carrier protein', Journal of Cell Biology, vol. 184, no. 4, pp. 569-581. https://doi.org/10.1083/jcb.200809099
Hoppins, Suzanne ; Horner, Jennifer ; Song, Cheng ; McCaffery, J. Michael ; Nunnari, Jodi. / Mitochondrial outer and inner membrane fusion requires a modifi ed carrier protein. In: Journal of Cell Biology. 2009 ; Vol. 184, No. 4. pp. 569-581.
@article{77e76a327234461c998052171dc8bff3,
title = "Mitochondrial outer and inner membrane fusion requires a modifi ed carrier protein",
abstract = "In yeast, three proteins are essential for mitochondrial fusion. Fzo1 and Mgm1 are conserved guanosine triphosphatases that reside in the outer and inner membranes, respectively. At each membrane, these conserved proteins are required for the distinct steps of membrane tethering and lipid mixing. The third essential component is Ugo1, an outer membrane protein in the mitochondrial transport protein family. We show that Ugo1 is a modifi ed member of this family, containing three transmembrane domains and existing as a dimer, a structure that is critical for the fusion function of Ugo1. Our functional analysis of Ugo1 indicates that it is required distinctly for both outer and inner membrane fusion after membrane tethering, indicating that it operates at the lipid-mixing step of fusion. This role is distinct from the fusion dynamin-related proteins and thus demonstrates that at each membrane, a single fusion protein is not suffi cient to drive the lipid-mixing step, but instead, this step requires a more complex assembly of proteins.",
author = "Suzanne Hoppins and Jennifer Horner and Cheng Song and McCaffery, {J. Michael} and Jodi Nunnari",
year = "2009",
month = "2",
day = "23",
doi = "10.1083/jcb.200809099",
language = "English (US)",
volume = "184",
pages = "569--581",
journal = "Journal of Cell Biology",
issn = "0021-9525",
publisher = "Rockefeller University Press",
number = "4",

}

TY - JOUR

T1 - Mitochondrial outer and inner membrane fusion requires a modifi ed carrier protein

AU - Hoppins, Suzanne

AU - Horner, Jennifer

AU - Song, Cheng

AU - McCaffery, J. Michael

AU - Nunnari, Jodi

PY - 2009/2/23

Y1 - 2009/2/23

N2 - In yeast, three proteins are essential for mitochondrial fusion. Fzo1 and Mgm1 are conserved guanosine triphosphatases that reside in the outer and inner membranes, respectively. At each membrane, these conserved proteins are required for the distinct steps of membrane tethering and lipid mixing. The third essential component is Ugo1, an outer membrane protein in the mitochondrial transport protein family. We show that Ugo1 is a modifi ed member of this family, containing three transmembrane domains and existing as a dimer, a structure that is critical for the fusion function of Ugo1. Our functional analysis of Ugo1 indicates that it is required distinctly for both outer and inner membrane fusion after membrane tethering, indicating that it operates at the lipid-mixing step of fusion. This role is distinct from the fusion dynamin-related proteins and thus demonstrates that at each membrane, a single fusion protein is not suffi cient to drive the lipid-mixing step, but instead, this step requires a more complex assembly of proteins.

AB - In yeast, three proteins are essential for mitochondrial fusion. Fzo1 and Mgm1 are conserved guanosine triphosphatases that reside in the outer and inner membranes, respectively. At each membrane, these conserved proteins are required for the distinct steps of membrane tethering and lipid mixing. The third essential component is Ugo1, an outer membrane protein in the mitochondrial transport protein family. We show that Ugo1 is a modifi ed member of this family, containing three transmembrane domains and existing as a dimer, a structure that is critical for the fusion function of Ugo1. Our functional analysis of Ugo1 indicates that it is required distinctly for both outer and inner membrane fusion after membrane tethering, indicating that it operates at the lipid-mixing step of fusion. This role is distinct from the fusion dynamin-related proteins and thus demonstrates that at each membrane, a single fusion protein is not suffi cient to drive the lipid-mixing step, but instead, this step requires a more complex assembly of proteins.

UR - http://www.scopus.com/inward/record.url?scp=61449256510&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=61449256510&partnerID=8YFLogxK

U2 - 10.1083/jcb.200809099

DO - 10.1083/jcb.200809099

M3 - Article

C2 - 19237599

AN - SCOPUS:61449256510

VL - 184

SP - 569

EP - 581

JO - Journal of Cell Biology

JF - Journal of Cell Biology

SN - 0021-9525

IS - 4

ER -