Purification and Characterization of a Ubiquitin-like System for Autophagosome Formation

Title
Purification and Characterization of a Ubiquitin-like System for Autophagosome Formation
Author(s)
박현호배주영
Keywords
PROTEIN CONJUGATION SYSTEM; MOLECULAR-MECHANISM; EXPANSION; PATHWAY; YEAST; ATG8; CELL
Issue Date
201012
Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
Citation
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.20, no.12, pp.1647 - 1652
Abstract
Autophagy refers to the bulk degradation of cellular proteins and organelles through an autophagosome and plays a pivotal role in the development, cellular differentiation, aging, and elimination of aberrant structures. A failure of autophagy has been implicated in a growing list of mammalian disease states, including cancer and cardiomyopathy. Two ubiquitin-like systems are highly involved in autophagy, especially in the formation of autophagosomes. Here, we purified and characterized Atg7 (an E1-like enzyme), and Atg3 and Atg10 (E2-like enzymes) in order to gain an insight into the role played by ubiquitin-like systems in the formation of autophagosomes. Interestingly, we observed that Atg7 forms a homodimer to construct an active conformation, unlike other El-like enzymes. Although Atg3 was detected as a monomer under physiological conditions, Atg10 existed in an oligomeric form, indicating that the mechanism by which Atg10 functions may differ from that of Atg3.
URI
http://hdl.handle.net/YU.REPOSITORY/23255http://dx.doi.org/10.4014/jmb.1007.07061
ISSN
1017-7825
Appears in Collections:
이과대학 > 화학생화학부 > Articles
생명공학부 > 생명공학부 > Articles
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