Open AccessSpatial colocalization and functional link of purinosomes with mitochondria
Author(s) -
Jarrod B. French,
Sara A. Jones,
Huayun Deng,
Anthony M. Pedley,
Doory Kim,
Chung Yu Chan,
Haibei Hu,
Raymond Pugh,
Hong Zhao,
Youxin Zhang,
Tony Jun Huang,
Fang Ye,
Xiaowei Zhuang,
Stephen J. Benkovic
Publication year - 2016
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.aac6054
Subject(s) - colocalization , kinome , mitochondrion , microbiology and biotechnology , pi3k/akt/mtor pathway , biology , intracellular , signal transduction , biochemistry , chemistry
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. Frenchet 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
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom