scholarly journals Mitochondrial Creatine Kinase and Mitochondrial Outer Membrane Porin Show a Direct Interaction That Is Modulated by Calcium

2001 ◽  
Vol 276 (51) ◽  
pp. 48027-48030 ◽  
Author(s):  
Uwe Schlattner ◽  
Max Dolder ◽  
Theo Wallimann ◽  
Malgorzata Tokarska-Schlattner
Keyword(s):  
Creatine Kinase ◽  
Outer Membrane ◽  
Direct Interaction ◽  
Mitochondrial Outer Membrane ◽  
Mitochondrial Creatine Kinase ◽  
Outer Membrane Porin

scholarly journals Hexokinase inhibits flux of fluorescently labeled ATP through mitochondrial outer membrane porin

FEBS Letters ◽  
2010 ◽  
Vol 584 (11) ◽  
pp. 2397-2402 ◽  
Author(s):  
Irina V. Perevoshchikova ◽  
Savva D. Zorov ◽  
Elena A. Kotova ◽  
Dmitry B. Zorov ◽  
Yuri N. Antonenko
Keyword(s):  
Outer Membrane ◽  
Mitochondrial Outer Membrane ◽  
Outer Membrane Porin

Characterization of Different Reactive Lysines in Bovine Heart Mitochondrial Porin

2002 ◽  
Vol 383 (12) ◽  
pp. 1967-1970 ◽  
Author(s):  
J.A. Al jamal
Keyword(s):  
Outer Membrane ◽  
Fluorescein Isothiocyanate ◽  
Mitochondrial Outer Membrane ◽  
Lipid Phase ◽  
Lipid Bilayer Membranes ◽  
Electrical Measurements ◽  
Elution Pattern ◽  
Outer Membrane Porin ◽  
Lysine Residues ◽  
Substantial Change

Abstract Incubation of mitochondrial outer membrane porin with citraconic anhydride prior to treatment with fluorescein isothiocyanate (FITC) resulted in the labeling of a set of lysines located at a boundary between the water phase and lipid phase. The elution pattern of porin from the cation exchanger has been considered as indicative for the location of lysines. Electrical measurements after reconstitution of the modified protein in lipid bilayer membranes revealed that certain specific lysine residues are more susceptible to alterations. The innermost positive residues were only slightly influenced, while the outermost lysines exhibited a substantial change in channel properties. These results suggest the presence of critical charged residues in mitochondrial outer membrane porin that may be responsible for both the channels selectivity and its voltage dependence.

scholarly journals Octameric mitochondrial creatine kinase induces and stabilizes contact sites between the inner and outer membrane

2005 ◽  
Vol 385 (2) ◽  
pp. 445-450 ◽  
Author(s):  
Oliver SPEER ◽  
Nils BÄCK ◽  
Tanja BUERKLEN ◽  
Dieter BRDICZKA ◽  
Alan KORETSKY ◽  
...  
Keyword(s):  
Creatine Kinase ◽  
Transgenic Mice ◽  
Outer Membrane ◽  
Liver Mitochondria ◽  
Wild Type ◽  
Mitochondrial Creatine Kinase ◽  
Membrane Contact Sites ◽  
Contact Sites ◽  
Membrane Contact

We have investigated the role of the protein ubiquitous mitochondrial creatine kinase (uMtCK) in the formation and stabilization of inner and outer membrane contact sites. Using liver mitochondria isolated from transgenic mice, which, unlike control animals, express uMtCK in the liver, we found that the enzyme was associated with the mitochondrial membranes and, in addition, was located in membrane-coated matrix inclusions. In mitochondria isolated from uMtCK transgenic mice, the number of contact sites increased 3-fold compared with that observed in control mitochondria. Furthermore, uMtCK-containing mitochondria were more resistant to detergent-induced lysis than wild-type mitochondria. We conclude that octameric uMtCK induces the formation of mitochondrial contact sites, leading to membrane cross-linking and to an increased stability of the mitochondrial membrane architecture.

Sign in / Sign up

Export Citation Format

Share Document