Purification and Characterization of a Ubiquitin-like System for Autophagosome Formation
- Purification and Characterization of a Ubiquitin-like System for Autophagosome Formation
- 박현호; 배주영
- PROTEIN CONJUGATION SYSTEM; MOLECULAR-MECHANISM; EXPANSION; PATHWAY; YEAST; ATG8; CELL
- Issue Date
- KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.20, no.12, pp.1647 - 1652
- 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.
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