PMID- 29464567
OWN - NLM
STAT- MEDLINE
DCOM- 20180817
LR  - 20220409
IS  - 0306-0225 (Print)
IS  - 0306-0225 (Linking)
VI  - 87
DP  - 2018
TI  - Mitochondrial Proteolipid Complexes of Creatine Kinase.
PG  - 365-408
LID - 10.1007/978-981-10-7757-9_13 [doi]
AB  - Isoforms of creatine kinase (CK) generate and use phosphocreatine, a concentrated 
      and highly diffusible cellular "high energy" intermediate, for the main purpose 
      of energy buffering and transfer in order to maintain cellular energy 
      homeostasis. The mitochondrial CK isoform (mtCK) localizes to the mitochondrial 
      intermembrane and cristae space, where it assembles into peripherally 
      membrane-bound, large cuboidal homooctamers. These are part of proteolipid 
      complexes wherein mtCK directly interacts with cardiolipin and other anionic 
      phospholipids, as well as with the VDAC channel in the outer membrane. This leads 
      to a stabilization and cross-linking of inner and outer mitochondrial membrane, 
      forming so-called contact sites. Also the adenine nucleotide translocator of the 
      inner membrane can be recruited into these proteolipid complexes, probably 
      mediated by cardiolipin. The complexes have functions mainly in energy transfer 
      to the cytosol and stimulation of oxidative phosphorylation, but also in 
      restraining formation of reactive oxygen species and apoptosis. In vitro evidence 
      indicates a putative role of mtCK in mitochondrial phospholipid distribution, and 
      most recently a role in thermogenesis has been proposed. This review summarizes 
      the essential structural and functional data of these mtCK complexes and 
      describes in more detail the more recent advances in phospholipid interaction, 
      thermogenesis, cancer and evolution of mtCK.
FAU - Schlattner, Uwe
AU  - Schlattner U
AD  - Laboratory of Fundamental and Applied Bioenergetics (LBFA), and SFR Environmental 
      and Systems Biology (BEeSy), University Grenoble Alpes, Grenoble, France. 
      uwe.schlattner@univ-grenoble-alpes.fr.
AD  - Inserm, U1055, Grenoble, France. uwe.schlattner@univ-grenoble-alpes.fr.
FAU - Kay, Laurence
AU  - Kay L
AD  - Laboratory of Fundamental and Applied Bioenergetics (LBFA), and SFR Environmental 
      and Systems Biology (BEeSy), University Grenoble Alpes, Grenoble, France.
AD  - Inserm, U1055, Grenoble, France.
FAU - Tokarska-Schlattner, Malgorzata
AU  - Tokarska-Schlattner M
AD  - Laboratory of Fundamental and Applied Bioenergetics (LBFA), and SFR Environmental 
      and Systems Biology (BEeSy), University Grenoble Alpes, Grenoble, France.
AD  - Inserm, U1055, Grenoble, France.
LA  - eng
PT  - Journal Article
PT  - Review
PL  - United States
TA  - Subcell Biochem
JT  - Sub-cellular biochemistry
JID - 0316571
RN  - 0 (Mitochondrial Proteins)
RN  - 0 (Phospholipids)
RN  - 0 (Reactive Oxygen Species)
RN  - EC 2.7.3.2 (Creatine Kinase)
SB  - IM
MH  - Animals
MH  - *Creatine Kinase/chemistry/metabolism
MH  - Cytosol/chemistry/metabolism
MH  - Humans
MH  - *Mitochondria/chemistry/metabolism
MH  - *Mitochondrial Membranes/chemistry/metabolism
MH  - *Mitochondrial Proteins/chemistry/metabolism
MH  - *Phospholipids/chemistry/metabolism
MH  - Reactive Oxygen Species/chemistry/metabolism
MH  - Thermogenesis/physiology
OTO - NOTNLM
OT  - Bioenergetics
OT  - Cancer
OT  - Compartmentalization
OT  - Energy transfer
OT  - Mitochondria
OT  - Oxidative phosphorylation
OT  - Thermogenesis
EDAT- 2018/02/22 06:00
MHDA- 2018/08/18 06:00
CRDT- 2018/02/22 06:00
PHST- 2018/02/22 06:00 [entrez]
PHST- 2018/02/22 06:00 [pubmed]
PHST- 2018/08/18 06:00 [medline]
AID - 10.1007/978-981-10-7757-9_13 [doi]
PST - ppublish
SO  - Subcell Biochem. 2018;87:365-408. doi: 10.1007/978-981-10-7757-9_13.