PMID- 33081639
OWN - NLM
STAT- MEDLINE
DCOM- 20210803
LR  - 20210803
IS  - 2046-2441 (Electronic)
IS  - 2046-2441 (Linking)
VI  - 10
IP  - 10
DP  - 2020 Oct
TI  - The aerobic mitochondrial ATP synthesis from a comprehensive point of view.
PG  - 200224
LID - 10.1098/rsob.200224 [doi]
LID - 200224
AB  - Most of the ATP to satisfy the energetic demands of the cell is produced by the 
      F(1)F(o)-ATP synthase (ATP synthase) which can also function outside the 
      mitochondria. Active oxidative phosphorylation (OxPhos) was shown to operate in 
      the photoreceptor outer segment, myelin sheath, exosomes, microvesicles, cell 
      plasma membranes and platelets. The mitochondria would possess the exclusive 
      ability to assemble the OxPhos molecular machinery so to share it with the 
      endoplasmic reticulum (ER) and eventually export the ability to aerobically 
      synthesize ATP in true extra-mitochondrial districts. The ER lipid rafts 
      expressing OxPhos components is indicative of the close contact of the two 
      organelles, bearing different evolutionary origins, to maximize the OxPhos 
      efficiency, exiting in molecular transfer from the mitochondria to the ER. This 
      implies that its malfunctioning could trigger a generalized oxidative stress. 
      This is consistent with the most recent interpretations of the evolutionary 
      symbiotic process whose necessary prerequisite appears to be the presence of the 
      internal membrane system inside the eukaryote precursor, of probable archaeal 
      origin allowing the engulfing of the alpha-proteobacterial precursor of mitochondria. 
      The process of OxPhos in myelin is here studied in depth. A model is provided 
      contemplating the biface arrangement of the nanomotor ATP synthase in the myelin 
      sheath.
FAU - Morelli, Alessandro Maria
AU  - Morelli AM
AD  - Pharmacy Department (DIFAR), Biochemistry Laboratory, University of Genova, Viale 
      Benedetto XV, 3, 16132 Genova, Italy.
FAU - Ravera, Silvia
AU  - Ravera S
AD  - Experimental Medicine Department (DIMES), University of Genova, Via De Toni, 14, 
      16132 Genova, Italy.
FAU - Panfoli, Isabella
AU  - Panfoli I
AD  - Pharmacy Department (DIFAR), Biochemistry Laboratory, University of Genova, Viale 
      Benedetto XV, 3, 16132 Genova, Italy.
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20201021
PL  - England
TA  - Open Biol
JT  - Open biology
JID - 101580419
RN  - 0 (Membrane Proteins)
RN  - 0 (Protons)
RN  - 8L70Q75FXE (Adenosine Triphosphate)
SB  - IM
MH  - Adenosine Triphosphate/*biosynthesis
MH  - Animals
MH  - Endoplasmic Reticulum/metabolism
MH  - Energy Metabolism
MH  - Humans
MH  - Intracellular Membranes/metabolism
MH  - Membrane Proteins/chemistry/metabolism
MH  - Mitochondria/*metabolism
MH  - Myelin Sheath/metabolism
MH  - *Oxidative Phosphorylation
MH  - Oxidative Stress
MH  - Prokaryotic Cells/metabolism
MH  - Protons
MH  - Structure-Activity Relationship
PMC - PMC7653358
OTO - NOTNLM
OT  - ATP synthase
OT  - endoplasmic reticulum
OT  - extra-mitochondrial
OT  - mitochondria
OT  - myelin
OT  - oxidative phosphorylation
COIS- We declare we have no competing interests.
EDAT- 2020/10/22 06:00
MHDA- 2021/08/04 06:00
PMCR- 2020/10/21
CRDT- 2020/10/21 05:37
PHST- 2020/10/21 05:37 [entrez]
PHST- 2020/10/22 06:00 [pubmed]
PHST- 2021/08/04 06:00 [medline]
PHST- 2020/10/21 00:00 [pmc-release]
AID - rsob200224 [pii]
AID - 10.1098/rsob.200224 [doi]
PST - ppublish
SO  - Open Biol. 2020 Oct;10(10):200224. doi: 10.1098/rsob.200224. Epub 2020 Oct 21.