TY  - JOUR
A1  - Angerer, Heike
T1  - Eukaryotic LYR proteins interact with mitochondrial protein complexes
T2  - Biology
N2  - In eukaryotic cells, mitochondria host ancient essential bioenergetic and biosynthetic pathways. LYR (leucine/tyrosine/arginine) motif proteins (LYRMs) of the Complex1_LYR-like superfamily interact with protein complexes of bacterial origin. Many LYR proteins function as extra subunits (LYRM3 and LYRM6) or novel assembly factors (LYRM7, LYRM8, ACN9 and FMC1) of the oxidative phosphorylation (OXPHOS) core complexes. Structural insights into complex I accessory subunits LYRM6 and LYRM3 have been provided by analyses of EM and X-ray structures of complex I from bovine and the yeast Yarrowia lipolytica, respectively. Combined structural and biochemical studies revealed that LYRM6 resides at the matrix arm close to the ubiquinone reduction site. For LYRM3, a position at the distal proton-pumping membrane arm facing the matrix space is suggested. Both LYRMs are supposed to anchor an acyl-carrier protein (ACPM) independently to complex I. The function of this duplicated protein interaction of ACPM with respiratory complex I is still unknown. Analysis of protein-protein interaction screens, genetic analyses and predicted multi-domain LYRMs offer further clues on an interaction network and adaptor-like function of LYR proteins in mitochondria.
KW  - LYR proteins
KW  - LYRM
KW  - LYR motif
KW  - mitochondria
KW  - OXPHOS complexes
KW  - respiratory complex I
KW  - mitochondrial acyl-carrier protein
KW  - ACPM
KW  - mitochondrial fatty acid synthesis type II
KW  - lipoic acid (6,8-dithio-octanoic acid)
KW  - reactive oxygen species
KW  - insulin resistance
Y1  - 2015
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/36625
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-366252
SN  - 2079-7737
N1  - This is an open access article distributed under the Creative Commons Attribution License  http://creativecommons.org/licenses/by/4.0/ which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
VL  - 4
IS  - 1
SP  - 133
EP  - 150
PB  - MDPI
CY  - Basel
ER  -