서울대학교 의과대학, Technion-Israel Institute of Technology

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Reviews & Commentaries
The Ubiquitin Code in the Ubiquitin-Proteasome System and Autophagy
펼치기 Authors and Affiliations
Abstract
The conjugation of the 76 amino acid protein ubiquitin to other proteins can alter the metabolic stability or non-proteolytic functions of the substrate. Once attached to a substrate (monoubiquitination), ubiquitin can itself be ubiquitinated on any of its seven lysine (Lys) residues or its N-terminal methionine (Met1). A single ubiquitin polymer may contain mixed linkages and/or two or more branches. In addition, ubiquitin can be conjugated with ubiquitin-like modifiers such as SUMO or small molecules such as phosphate. The diverse ways to assemble ubiquitin chains provide countless means to modulate biological processes. We overview here the complexity of the ubiquitin code, with an emphasis on the emerging role of linkage-specific degradation signals (degrons) in the ubiquitin-proteasome system (UPS) and the autophagy-lysosome system (hereafter autophagy).

Keywords : ubiquitination, proteolysis, autophagy-lysosome, system, ubiquitin, linkages, protein quality control
주소복사
논문정보   
- 형식: Review Paper
- 게재일: 2017년 11월 (BRIC 등록일 2020-03-19)
- 연구진: 국내(교신)+국외 연구진태극기
- 분야: Biochemistry
- 피인용횟수: 최근 3년간 60회 이상 인용된 논문
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