中国科学院大连化学物理研究所机构知识库
Advanced  
DICP OpenIR  > 中国科学院大连化学物理研究所  > 期刊论文
题名: Fructose-1,6-bisphosphate and aldolase mediate glucose sensing by AMPK
作者: Zhang, Chen-Song1;  Hawley, Simon A.2;  Zong, Yue1;  Li, Mengqi1;  Wang, Zhichao3, 4, 5;  Gray, Alexander2;  Ma, Teng1;  Cui, Jiwen1;  Feng, Jin-Wei1;  Zhu, Mingjiang6;  Wu, Yu-Qing1;  Li, Terytty Yang1;  Ye, Zhiyun1;  Lin, Shu-Yong1;  Yin, Huiyong6;  Piao, Hai-Long3;  Hardie, D. G. Rahame2;  Lin, Sheng-Cai1
刊名: NATURE
发表日期: 2017-08-03
DOI: 10.1038/nature23275
卷: 548, 期:7665, 页:112-+
收录类别: SCI
文章类型: Article
WOS标题词: Science & Technology
类目[WOS]: Multidisciplinary Sciences
研究领域[WOS]: Science & Technology - Other Topics
英文摘要: The major energy source for most cells is glucose, from which ATP is generated via glycolysis and/or oxidative metabolism. Glucose deprivation activates AMP-activated protein kinase (AMPK)(1), but it is unclear whether this activation occurs solely via changes in AMP or ADP, the classical activators of AMPK(2-5). Here, we describe an AMP/ADP-independent mechanism that triggers AMPK activation by sensing the absence of fructose-1,6-bisphosphate (FBP), with AMPK being progressively activated as extracellular glucose and intracellular FBP decrease. When unoccupied by FBP, aldolases promote the formation of a lysosomal complex containing at least v-ATPase, ragulator, axin, liver kinase B1 (LKB1) and AMPK, which has previously been shown to be required for AMPK activation(6,7). Knockdown of aldolases activates AMPK even in cells with abundant glucose, whereas the catalysis-defective D34S aldolase mutant, which still binds FBP, blocks AMPK activation. Cell-free reconstitution assays show that addition of FBP disrupts the association of axin and LKB1 with v-ATPase and ragulator. Importantly, in some cell types AMP/ATP and ADP/ATP ratios remain unchanged during acute glucose starvation, and intact AMP-binding sites on AMPK are not required for AMPK activation. These results establish that aldolase, as well as being a glycolytic enzyme, is a sensor of glucose availability that regulates AMPK.
关键词[WOS]: VACUOLAR H+-ATPASE ;  ACTIVATED PROTEIN-KINASE ;  PHOSPHORYLATION ;  DISEASE ;  CELLS ;  METABOLISM ;  MECHANISM ;  AUTOPHAGY ;  REVEALS ;  COMPLEX
语种: 英语
WOS记录号: WOS:000406831700047
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/149824
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

Files in This Item:

There are no files associated with this item.


作者单位: 1.Xiamen Univ, Sch Life Sci, Innovat Ctr Cell Signaling Network, State Key Lab Cellular Stress Biol, Xiamen 361102, Fujian, Peoples R China
2.Univ Dundee, Div Cell Signalling & Immunol, Coll Life Sci, Dundee DD1 5EH, Scotland
3.Chinese Acad Sci, Dalian Inst Chem Phys, Sci Res Ctr Translat Med, Dalian 116023, Liaoning, Peoples R China
4.Chinese Acad Sci, Dalian Inst Chem Phys, Key Lab Separat Sci Analyt Chem, Dalian 116023, Liaoning, Peoples R China
5.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
6.Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Nutr Sci, Key Lab Food Safety Res, Shanghai 200031, Peoples R China

Recommended Citation:
Zhang, Chen-Song,Hawley, Simon A.,Zong, Yue,et al. Fructose-1,6-bisphosphate and aldolase mediate glucose sensing by AMPK[J]. NATURE,2017,548(7665):112-+.
Service
 Recommend this item
 Sava as my favorate item
 Show this item's statistics
 Export Endnote File
Google Scholar
 Similar articles in Google Scholar
 [Zhang, Chen-Song]'s Articles
 [Hawley, Simon A.]'s Articles
 [Zong, Yue]'s Articles
CSDL cross search
 Similar articles in CSDL Cross Search
 [Zhang, Chen-Song]‘s Articles
 [Hawley, Simon A.]‘s Articles
 [Zong, Yue]‘s Articles
Related Copyright Policies
Null
Social Bookmarking
  Add to CiteULike  Add to Connotea  Add to Del.icio.us  Add to Digg  Add to Reddit 
所有评论 (0)
暂无评论
 
评注功能仅针对注册用户开放,请您登录
您对该条目有什么异议,请填写以下表单,管理员会尽快联系您。
内 容:
Email:  *
单位:
验证码:   刷新
您在IR的使用过程中有什么好的想法或者建议可以反馈给我们。
标 题:
 *
内 容:
Email:  *
验证码:   刷新

Items in IR are protected by copyright, with all rights reserved, unless otherwise indicated.

 

 

Valid XHTML 1.0!
Powered by CSpace