期刊
TRENDS IN BIOCHEMICAL SCIENCES
卷 42, 期 11, 页码 873-886出版社
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tibs.2017.09.002
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资金
- Dr Miriam and Sheldon G. Adelson Medical Research Foundation (AMRF)
- Israel Science Foundation (ISF)
- I-CORE Program of the Planning and Budgeting Committee
- ISF [1775/12]
- Deutsch-Israelische Projektkooperation (DIP)
- Basic Science Research Program - Ministry of Science, ICT, and Future Planning (MSIP) of Korea [NRF-2016R1A2B3011389]
- Brain Korea 21 PLUS Program
- Seoul National University Nobel Laureates Invitation Program
- Mr Albert Sweet of California, USA
- National Research Foundation of Korea [2016R1A2B3011389] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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).
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