Spatial colocalization and functional link of purinosomes with mitochondria

Author:

French Jarrod B.1,Jones Sara A.2,Deng Huayun3,Pedley Anthony M.4,Kim Doory25,Chan Chung Yu6,Hu Haibei3,Pugh Raymond J.4,Zhao Hong4,Zhang Youxin2,Huang Tony Jun6,Fang Ye3,Zhuang Xiaowei257,Benkovic Stephen J.4

Affiliation:

1. Department of Biochemistry and Cell Biology, Department of Chemistry, Stony Brook University, Stony Brook, NY 11794, USA.

2. Department of Chemistry and Chemical Biology, Harvard University, Cambridge, MA 02138, USA.

3. Biochemical Technologies, Science and Technology Division, Corning Incorporated, Corning, NY 14831, USA.

4. Department of Chemistry, The Pennsylvania State University, University Park, PA 16802, USA.

5. Howard Hughes Medical Institute, Harvard University, Cambridge, MA 02138, USA.

6. Department of Engineering Science and Mechanics, The Pennsylvania State University, University Park, PA 16802, USA.

7. Department of Physics, Harvard University, Cambridge, MA 02138, USA.

Abstract

Spatial control of cellular enzymes Purine is a building block of DNA and also a component of ATP that is used as an energy source in the cell. Enzymes involved in purine biosynthesis organize into dynamic bodies called purinosomes. French et al. found that purinosomes colocalize with mitochondria, organelles that generate ATP (see the Perspective by Ma and Jones). Dysregulation of mitochondria caused an increase in the number of purinosomes. This suggests a synergy, with the purinosomes supplying the purine required for ATP production and in turn using ATP in the biosynthetic pathway. A master regulator of cellular metabolism, mTOR, appears to mediate the association of purinosomes and mitochondria. This could make purine and ATP synthesis responsive to changes in the metabolic needs of the cell. Science , this issue p. 733 ; see also p. 670

Funder

National Institutes of Health

Howard Hughes Medical Institute

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3