PMID- 21738264
OWN - NLM
STAT- MEDLINE
DCOM- 20111025
LR  - 20211020
IS  - 1738-0006 (Electronic)
IS  - 0023-4001 (Print)
IS  - 0023-4001 (Linking)
VI  - 49
IP  - 2
DP  - 2011 Jun
TI  - Atg3-mediated lipidation of Atg8 is involved in encystation of Acanthamoeba.
PG  - 103-8
LID - 10.3347/kjp.2011.49.2.103 [doi]
AB  - Autophagy is a catabolic process involved in the degradation of a cell's own 
      components for cell growth, development, homeostasis, and the recycling of 
      cellular products. Autophagosome is an essential component in the protozoan 
      parasite during differentiation and encystation. The present study identified and 
      characterized autophagy-related protein (Atg) 3, a member of Atg8 conjugation 
      system, in Acanthamoeba castellanii (AcAtg3). AcAtg3 encoding a 304 amino acid 
      protein showed high similarity with the catalytic cysteine site of other E2 like 
      enzymes of ubiquitin system. Predicted 3D structure of AcAtg3 revealed a 
      hammer-like shape, which is the characteristic structure of E2-like enzymes. The 
      expression level of AcAtg3 did not increase during encystation. However, the 
      formation of mature cysts was significantly reduced in Atg3-siRNA transfected 
      cells in which the production of Atg8-phosphatidylethanolamine conjugate was 
      inhibited. Fluorescent microscopic analysis revealed that dispersed AcAtg3-EGFP 
      fusion protein gathered around autophagosomal membranes during encystation. These 
      results provide important information for understanding autophagic machinery 
      through the lipidation reaction mediated by Atg3 in Acanthamoeba.
FAU - Moon, Eun-Kyung
AU  - Moon EK
AD  - Department of Parasitology, Kyungpook National University School of Medicine, 
      Daegu 700-721, Korea.
FAU - Chung, Dong-Il
AU  - Chung DI
FAU - Hong, Yeonchul
AU  - Hong Y
FAU - Kong, Hyun-Hee
AU  - Kong HH
LA  - eng
SI  - GENBANK/GU270859
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20110614
PL  - Korea (South)
TA  - Korean J Parasitol
JT  - The Korean journal of parasitology
JID - 9435800
RN  - 0 (Protozoan Proteins)
RN  - 0 (RNA, Small Interfering)
RN  - EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes)
SB  - IM
MH  - Acanthamoeba castellanii/*growth & development/*metabolism
MH  - Animals
MH  - Gene Knockdown Techniques
MH  - Lipid Metabolism
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - Protein Structure, Tertiary
MH  - Protozoan Proteins/genetics
MH  - RNA, Small Interfering/metabolism
MH  - Rats
MH  - Sequence Analysis, DNA
MH  - Spores, Protozoan/*growth & development/*metabolism
MH  - Ubiquitin-Conjugating Enzymes/genetics/*metabolism
PMC - PMC3121065
OTO - NOTNLM
OT  - Acanthamoeba
OT  - Atg3
OT  - autophagosome
OT  - encystation
EDAT- 2011/07/09 06:00
MHDA- 2011/10/26 06:00
PMCR- 2011/06/01
CRDT- 2011/07/09 06:00
PHST- 2010/11/19 00:00 [received]
PHST- 2011/02/07 00:00 [revised]
PHST- 2011/02/18 00:00 [accepted]
PHST- 2011/07/09 06:00 [entrez]
PHST- 2011/07/09 06:00 [pubmed]
PHST- 2011/10/26 06:00 [medline]
PHST- 2011/06/01 00:00 [pmc-release]
AID - 10.3347/kjp.2011.49.2.103 [doi]
PST - ppublish
SO  - Korean J Parasitol. 2011 Jun;49(2):103-8. doi: 10.3347/kjp.2011.49.2.103. Epub 
      2011 Jun 14.