Journal
CELL REPORTS
Volume 18, Issue 2, Pages 307-313Publisher
CELL PRESS
DOI: 10.1016/j.celrep.2016.12.049
Keywords
-
Categories
Funding
- NIH [U01GM94622, R01DK098672, R01GM115591, P41GM108538, R01GM099752, R35GM118110]
- NSF [CHE-1415910]
- United Mitochondrial Disease Foundation (UMDF)
- NLM [5T15LM007359]
- Emma Francis Dalton Research fund via UMDF
- Direct For Mathematical & Physical Scien
- Division Of Chemistry [1415910] Funding Source: National Science Foundation
Ask authors/readers for more resources
Proper maintenance of mitochondrial activity is essential for metabolic homeostasis. Widespread phosphorylation of mitochondrial proteins may be an important element of this process; yet, little is known about which enzymes control mitochondrial phosphorylation or which phosphosites have functional impact. We investigate these issues by disrupting Ptc7p, a conserved but largely uncharacterized mitochondrial matrix PP2C-type phosphatase. Loss of Ptc7p causes respiratory growth defects concomitant with elevated phosphorylation of select matrix proteins. Among these, Delta ptc7 yeast exhibit an increase in phosphorylation of Cit1p, the canonical citrate synthase of the tricarboxylic acid (TCA) cycle, that diminishes its activity. We find that phosphorylation of S462 can eliminate Cit1p enzymatic activity likely by disrupting its proper dimerization, and that Ptc7p-driven dephosphorylation rescues Cit1p activity. Collectively, our work connects Ptc7p to an essential TCA cycle function and to additional phosphorylation events that may affect mitochondrial activity inadvertently or in a regulatory manner.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available