Faculty Opinions recommendation of Modulation of mitochondrial protein phosphorylation by soluble adenylyl cyclase ameliorates cytochrome oxidase defects.

2010 ◽  
Author(s):  
Eduardo Rial
Keyword(s):  
Protein Phosphorylation ◽  
Adenylyl Cyclase ◽  
Cytochrome Oxidase ◽  
Mitochondrial Protein ◽  
Soluble Adenylyl Cyclase

scholarly journals Modulation of mitochondrial protein phosphorylation by soluble adenylyl cyclase ameliorates cytochrome oxidase defects

2009 ◽  
Vol 1 (8‐9) ◽  
pp. 392-406 ◽  
Author(s):  
Rebeca Acin‐Perez ◽  
Eric Salazar ◽  
Sonja Brosel ◽  
Hua Yang ◽  
Eric A. Schon ◽  
...  
Keyword(s):  
Protein Phosphorylation ◽  
Adenylyl Cyclase ◽  
Cytochrome Oxidase ◽  
Mitochondrial Protein ◽  
Soluble Adenylyl Cyclase

scholarly journals cAMP and Mitochondria

Physiology ◽  
2013 ◽  
Vol 28 (3) ◽  
pp. 199-209 ◽  
Author(s):  
Federica Valsecchi ◽  
Lavoisier S. Ramos-Espiritu ◽  
Jochen Buck ◽  
Lonny R. Levin ◽  
Giovanni Manfredi
Keyword(s):  
Protein Phosphorylation ◽  
Adenylyl Cyclase ◽  
Regulatory Mechanism ◽  
Mitochondrial Proteins ◽  
Camp Signaling ◽  
Metabolic Adaptation ◽  
Mitochondrial Bioenergetics ◽  
Soluble Adenylyl Cyclase

Phosphorylation of mitochondrial proteins has emerged as a major regulatory mechanism for metabolic adaptation. cAMP signaling and PKA phosphorylation of mitochondrial proteins have just started to be investigated, and the presence of cAMP-generating enzymes and PKA inside mitochondria is still controversial. Here, we discuss the role of cAMP in regulating mitochondrial bioenergetics through protein phosphorylation and the evidence for soluble adenylyl cyclase as the source of cAMP inside mitochondria.

Two domains are critical for the nuclear localization of soluble adenylyl cyclase

Biochimie ◽  
2006 ◽  
Vol 88 (3-4) ◽  
pp. 319-328 ◽  
Author(s):  
Q FENG ◽  
Y ZHANG ◽  
Y LI ◽  
Z LIU ◽  
J ZUO ◽  
...  
Keyword(s):  
Adenylyl Cyclase ◽  
Nuclear Localization ◽  
Soluble Adenylyl Cyclase

scholarly journals Non-canonical regulation of glycogenolysis and the Warburg phenotype by soluble adenylyl cyclase

2020 ◽  
Author(s):  
Jung-Chin Chang ◽  
Simei Go ◽  
Eduardo H. Gilglioni ◽  
Hang Lam Li ◽  
Hsu-Li Huang ◽  
...  
Keyword(s):  
Oxidative Phosphorylation ◽  
Adenylyl Cyclase ◽  
Energy Homeostasis ◽  
Aerobic Glycolysis ◽  
Glycogen Metabolism ◽  
Adenylyl Cyclases ◽  
Soluble Adenylyl Cyclase ◽  
Atp Level ◽  
Downstream Effectors ◽  
Different Types

AbstractCyclic AMP is produced in cells by two very different types of adenylyl cyclases: the canonical transmembrane adenylyl cyclases (tmACs, ADCY1∼9) and the evolutionarily more conserved soluble adenylyl cyclase (sAC, ADCY10). While the role and regulation of tmACs is well documented, much less is known of sAC in cellular metabolism. We demonstrate here that sAC is an acute regulator of glycolysis, oxidative phosphorylation and glycogen metabolism, tuning their relative bioenergetic contributions. Suppression of sAC activity leads to aerobic glycolysis, enhanced glycogenolysis, decreased oxidative phosphorylation, and an elevated cytosolic NADH/NAD+ ratio, resembling the Warburg phenotype. Importantly, we found that glycogen metabolism is regulated in opposite directions by cAMP depending on its location of synthesis and downstream effectors. While the canonical tmAC-cAMP-PKA axis promotes glycogenolysis, we identify a novel sAC-cAMP-Epac1 axis that suppresses glycogenolysis. These data suggest that sAC is an autonomous bioenergetic sensor that suppresses aerobic glycolysis and glycogenolysis when ATP levels suffice. When the ATP level falls, diminished sAC activity induces glycogenolysis and aerobic glycolysis to maintain energy homeostasis.

scholarly journals Soluble adenylyl cyclase inhibition prevents human sperm functions essential for fertilization

2021 ◽  
Author(s):  
Melanie Balbach ◽  
Lubna Ghanem ◽  
Thomas Rossetti ◽  
Navpreet Kaur ◽  
Carla Ritagliati ◽  
...  
Keyword(s):  
Adenylyl Cyclase ◽  
Acrosome Reaction ◽  
Human Sperm ◽  
Comprehensive Analysis ◽  
Multiple Points ◽  
Soluble Adenylyl Cyclase ◽  
Mouse Sperm ◽  
On Demand ◽  
Sperm Functions

AbstractSoluble adenylyl cyclase (sAC: ADCY10) is essential for activating dormant sperm. Studies of freshly dissected mouse sperm identified sAC as needed for initiating capacitation and activating motility. We now use an improved sAC inhibitor, TDI-10229, for a comprehensive analysis of sAC function in human sperm. Unlike dissected mouse sperm, human sperm are collected post-ejaculation, after sAC activity has already been stimulated. Even in ejaculated human sperm, TDI-10229 interrupts stimulated motility and capacitation, and it prevents acrosome reaction in capacitated sperm. At present, there are no non-hormonal, pharmacological methods for contraception. Because sAC activity is required post-ejaculation at multiple points during the sperm’s journey to fertilize the oocyte, sAC inhibitors define candidates for non-hormonal, on-demand contraceptives suitable for delivery via intravaginal devices in females.

scholarly journals Soluble adenylyl cyclase in health and disease

2014 ◽  
Vol 1842 (12) ◽  
pp. 2584-2592 ◽  
Author(s):  
Andreas Schmid ◽  
Dimirela Meili ◽  
Matthias Salathe
Keyword(s):  
Adenylyl Cyclase ◽  
Soluble Adenylyl Cyclase ◽  
Health And Disease

scholarly journals Changes in the mitochondrial phosphoproteome during mammalian hibernation

2013 ◽  
Vol 45 (10) ◽  
pp. 389-399 ◽  
Author(s):  
Dillon J. Chung ◽  
Beata Szyszka ◽  
Jason C. L. Brown ◽  
Norman P. A. Hüner ◽  
James F. Staples
Keyword(s):  
Protein Phosphorylation ◽  
Mitochondrial Respiration ◽  
Core Body Temperature ◽  
Mitochondrial Protein ◽  
Time Of Flight ◽  
Ground Squirrels ◽  
Mitochondrial Metabolism ◽  
Mitochondrial Enzymes ◽  
Phosphorylation State ◽  
Mammalian Hibernation

Mammalian hibernation involves periods of substantial suppression of metabolic rate (torpor) allowing energy conservation during winter. In thirteen-lined ground squirrels ( Ictidomys tridecemlineatus ), suppression of liver mitochondrial respiration during entrance into torpor occurs rapidly (within 2 h) before core body temperature falls below 30°C, whereas reversal of this suppression occurs slowly during arousal from torpor. We hypothesized that this pattern of rapid suppression in entrance and slow reversal during arousal was related to changes in the phosphorylation state of mitochondrial enzymes during torpor catalyzed by temperature-dependent kinases and phosphatases. We compared mitochondrial protein phosphorylation among hibernation metabolic states using immunoblot analyses and assessed how phosphorylation related to mitochondrial respiration rates. No proteins showed torpor-specific changes in phosphorylation, nor did phosphorylation state correlate with mitochondrial respiration. However, several proteins showed seasonal (summer vs. winter) differences in phosphorylation of threonine or serine residues. Using matrix-assisted laser desorption/ionization-time of flight/time of flight mass spectrometry, we identified three of these proteins: F1-ATPase α-chain, long chain-specific acyl-CoA dehydrogenase, and ornithine transcarbamylase. Therefore, we conclude that protein phosphorylation is likely a mechanism involved in bringing about seasonal changes in mitochondrial metabolism in hibernating ground squirrels, but it seems unlikely to play any role in acute suppression of mitochondrial metabolism during torpor.

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