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 language | English (US) |
|---|---|
| Pages (from-to) | 569-581 |
| Number of pages | 13 |
| Journal | Journal of Cell Biology |
| Volume | 184 |
| Issue number | 4 |
| DOIs | |
| State | Published - Feb 23 2009 |
Fingerprint
ASJC Scopus subject areas
- Cell Biology
- Medicine(all)
Cite this
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 journal › Article
}
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 -