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DNA 双海滨裂缝修理: 小径选择的一个故事
  • ISSN号:1672-9145
  • 期刊名称:《生物化学与生物物理学报:英文版》
  • 时间:0
  • 分类:Q10[生物学—普通生物学] TS941.717[轻工技术与工程—服装设计与工程]
  • 作者机构:Beijing Key Laboratory of DNA Damage Response and College of Life Sciences, Capital Normal University, Be!jing 100048, China
  • 相关基金:supported by the National Natural Science Foundation of China (NSFC;Grant Nos.31530016 and 31461143012); the National Basic Research Program of China (973 Program;Grant Nos.2013CB911002 and 2015CB910601); the Scientific Research Base Development Program of the Beijing Municipal Commission of Education,China to XX
中文摘要:

Ubiquitin-fold modifier 1(UFM1) is one of the newly-identified ubiquitin-like proteins.Similar to ubiquitin,UFM1 is conjugated to its target proteins by a three-step enzymatic reaction.The UFM1-activating enzyme,ubiquitin-like modifier-activating enzyme 5(UBA5),serves as the E1 to activate UFM1;UFM1-conjugating enzyme 1(UFC1) acts as the E2 to transfer the activated UFM1 to the active site of the E2;and the UFM1-specific ligase 1(UFL1) acts as the E3 to recognize its substrate,transfer,and ligate the UFM1 from E2 to the substrate.This process is called ufmylation.UFM1 chains can be cleaved from its target proteins by UFM1-specific proteases(Uf SPs),suggesting that the ufmylation modification is reversible.UFM1 cascade is conserved among nearly all of the eukaryotic organisms,but not in yeast,and associated with several cellular activities including the endoplasmic reticulum stress response and hematopoiesis.Furthermore,the UFM1 cascade is closely related to a series of human diseases.In this review,we summarize the molecular details of this reversible modification process,the recent progress of its functional studies,as well as its implication in tumorigenesis and potential therapeutic targets for cancer.

英文摘要:

Ubiquitin-fold modifier 1(UFM1) is one of the newly-identified ubiquitin-like proteins.Similar to ubiquitin,UFM1 is conjugated to its target proteins by a three-step enzymatic reaction.The UFM1-activating enzyme,ubiquitin-like modifier-activating enzyme 5(UBA5),serves as the E1 to activate UFM1;UFM1-conjugating enzyme 1(UFC1) acts as the E2 to transfer the activated UFM1 to the active site of the E2;and the UFM1-specific ligase 1(UFL1) acts as the E3 to recognize its substrate,transfer,and ligate the UFM1 from E2 to the substrate.This process is called ufmylation.UFM1 chains can be cleaved from its target proteins by UFM1-specific proteases(Uf SPs),suggesting that the ufmylation modification is reversible.UFM1 cascade is conserved among nearly all of the eukaryotic organisms,but not in yeast,and associated with several cellular activities including the endoplasmic reticulum stress response and hematopoiesis.Furthermore,the UFM1 cascade is closely related to a series of human diseases.In this review,we summarize the molecular details of this reversible modification process,the recent progress of its functional studies,as well as its implication in tumorigenesis and potential therapeutic targets for cancer.

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期刊信息
  • 《生物化学与生物物理学报:英文版》
  • 北大核心期刊(2004版)
  • 主管单位:
  • 主办单位:中国科学院上海生物化学研究所
  • 主编:
  • 地址:上海岳阳路319号
  • 邮编:200031
  • 邮箱:abbs@sibs.ac.cn
  • 电话:021-54920956 54920955
  • 国际标准刊号:ISSN:1672-9145
  • 国内统一刊号:ISSN:31-1940/Q
  • 邮发代号:4-210
  • 获奖情况:
  • 国内外数据库收录:
  • 美国化学文摘(网络版),英国农业与生物科学研究中心文摘,荷兰文摘与引文数据库,美国生物医学检索系统,美国剑桥科学文摘,美国科学引文索引(扩展库),美国生物科学数据库,英国动物学记录,日本日本科学技术振兴机构数据库,中国中国科技核心期刊,中国北大核心期刊(2004版),英国英国皇家化学学会文摘,中国北大核心期刊(2000版)
  • 被引量:5851