TY  - JOUR
AU  - Schlösser, Lukas
AU  - Sachse, Carsten
AU  - Low, Harry H.
AU  - Schneider, Dirk
TI  - Conserved structures of ESCRT-III superfamily members across domains of life
JO  - Trends in biochemical sciences
VL  - 48
IS  - 11
SN  - 0376-5067
CY  - Amsterdam [u.a.]
PB  - Elsevier Science
M1  - FZJ-2024-02674
SP  - 993 - 1004
PY  - 2023
AB  - Structural and evolutionary studies of cyanobacterial phage shock protein A (PspA) and inner membrane-associated protein of 30 kDa (IM30) have revealed that these proteins belong to the endosomal sorting complex required for transport-III (ESCRT-III) superfamily, which is conserved across all three domains of life. PspA and IM30 share secondary and tertiary structures with eukaryotic ESCRT-III proteins, whilst also oligomerizing via conserved interactions. Here, we examine the structures of bacterial ESCRT-III-like proteins and compare the monomeric and oligomerized forms with their eukaryotic counterparts. We discuss conserved interactions used for self-assembly and highlight key hinge regions that mediate oligomer ultrastructure versatility. Finally, we address the differences in nomenclature assigned to equivalent structural motifs in both the bacterial and eukaryotic fields and suggest a common nomenclature applicable across the ESCRT-III superfamily.
LB  - PUB:(DE-HGF)16
C6  - 37718229
UR  - <Go to ISI:>//WOS:001101421200001
DO  - DOI:10.1016/j.tibs.2023.08.009
UR  - https://juser.fz-juelich.de/record/1025086
ER  -