PMID- 24070471
OWN - NLM
STAT- MEDLINE
DCOM- 20140424
LR  - 20130927
IS  - 1744-1358 (Electronic)
IS  - 0071-1365 (Linking)
VI  - 55
DP  - 2013
TI  - The Atg8 family: multifunctional ubiquitin-like key regulators of autophagy.
PG  - 51-64
LID - 10.1042/bse0550051 [doi]
AB  - Autophagy is an evolutionarily-conserved catabolic process initiated by the 
      engulfment of cytosolic components in a crescent-shaped structure, called the 
      phagophore, that expands and fuses to form a closed double-membrane vesicle, the 
      autophagosome. Autophagosomes are subsequently targeted to the lysosome/vacuole 
      with which they fuse to degrade their content. The formation of the autophagosome 
      is carried out by a set of autophagy-related proteins (Atg), highly conserved 
      from yeast to mammals. The Atg8s are Ubl (ubiquitin-like) proteins that play an 
      essential role in autophagosome biogenesis. This family of proteins comprises a 
      single member in yeast and several mammalian homologues grouped into three 
      subfamilies: LC3 (light-chain 3), GABARAP (gamma-aminobutyric acid 
      receptor-associated protein) and GATE-16 (Golgi-associated ATPase enhancer of 16 
      kDa). The Atg8s are synthesized as cytosolic precursors, but can undergo a series 
      of post-translational modifications leading to their tight association with 
      autophagosomal structures following autophagy induction. Owing to this feature, 
      the Atg8 proteins have been widely served as key molecules to monitor 
      autophagosomes and autophagic activity. Studies in both yeast and mammalian 
      systems have demonstrated that Atg8s play a dual role in the autophagosome 
      formation process, coupling between selective incorporation of autophagy cargo 
      and promoting autophagosome membrane expansion and closure. The 
      membrane-remodelling activity of the Atg8 proteins is associated with their 
      capacity to promote tethering and hemifusion of liposomes in vitro.
FAU - Slobodkin, Moran Rawet
AU  - Slobodkin MR
AD  - Department of Biological Chemistry, The Weizmann Institute of Science, 234 Herzl 
      St, Rehovot 7632700, Israel.
FAU - Elazar, Zvulun
AU  - Elazar Z
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
PL  - England
TA  - Essays Biochem
JT  - Essays in biochemistry
JID - 0043306
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Microtubule-Associated Proteins)
RN  - 0 (Ubiquitins)
SB  - IM
MH  - Adaptor Proteins, Signal Transducing/genetics/*metabolism
MH  - Animals
MH  - *Autophagy
MH  - Cytoplasmic Vesicles/metabolism
MH  - Humans
MH  - Microtubule-Associated Proteins/genetics/*metabolism
MH  - Ubiquitins/genetics/*metabolism
EDAT- 2013/09/28 06:00
MHDA- 2014/04/25 06:00
CRDT- 2013/09/28 06:00
PHST- 2013/09/28 06:00 [entrez]
PHST- 2013/09/28 06:00 [pubmed]
PHST- 2014/04/25 06:00 [medline]
AID - bse0550051 [pii]
AID - 10.1042/bse0550051 [doi]
PST - ppublish
SO  - Essays Biochem. 2013;55:51-64. doi: 10.1042/bse0550051.