Binding of microtubule-associated proteins (MAPs) to rat brain mitochondria: A comparative study of the binding of MAP2, Its microtubule-binding and projection domains, and tau proteins

1989 ◽  
Vol 14 (3) ◽  
pp. 372-381 ◽  
Author(s):  
Veronika Jancsik ◽  
Dominique Filliol ◽  
Simone Felter ◽  
Alvaro Rendon
Keyword(s):  
Comparative Study ◽  
Rat Brain ◽  
Brain Mitochondria ◽  
Tau Proteins ◽  
Microtubule Binding ◽  
Microtubule Associated Proteins ◽  
Rat Brain Mitochondria ◽  
Associated Proteins

scholarly journals The specific binding of the microtubule-associated protein 2 (MAP2) to the outer membrane of rat brain mitochondria

1989 ◽  
Vol 261 (1) ◽  
pp. 167-173 ◽  
Author(s):  
M Lindén ◽  
B D Nelson ◽  
J F Leterrier
Keyword(s):  
Rat Brain ◽  
Outer Membrane ◽  
Binding Sites ◽  
Specific Binding ◽  
Brain Mitochondria ◽  
Microtubule Associated Proteins ◽  
Cross Linkage ◽  
Associated Proteins ◽  
A Site

Purified mitochondria from rat brain contain microtubule-associated proteins (MAPs) bound to the outer membrane. Studies of binding in vitro performed with microtubules and with purified microtubule proteins showed that mitochondria preferentially interact with the high-molecular-mass MAPs (and not with Tau protein). Incubation of intact mitochondria with Taxol-stabilized microtubules resulted in the selective trapping of both MAPs 1 and 2 on mitochondria, indicating that an interaction between the two organelles occurred through a site on the arm-like projection of MAPs. Two MAP-binding sites were located on intact mitochondria. The lower-affinity MAP2-binding site (Kd = 2 x 10(-7) M) was preserved and enriched in the outer-membrane fraction, whereas the higher-affinity site (Kd = 1 x 10(-9) M) was destroyed after removing the outer membrane with digitonin. Detergent fractionation of mitochondrial outer membranes saturated with MAP2 bound in vitro showed that MAPs are associated with membrane fragments which contain the pore-forming protein (porin). MAP2 also partially prevents the solubilization of porin from outer membrane, indicating a MAP-induced change in the membrane environment of porin. These observations demonstrate the presence of specific MAP-binding sites on the outer membrane, suggesting an association between porin and the membrane domain involved in the cross-linkage between microtubules and mitochondria.

Acyl-CoA: sn-Glycerol-3-Phosphate O-Acyltransferase in Rat Brain Mitochondria and Microsomes

1982 ◽  
Vol 39 (1) ◽  
pp. 286-289 ◽  
Author(s):  
Susan M. Fitzpatrick ◽  
Giovanna Sorresso ◽  
Dipak Haldar
Keyword(s):  
Rat Brain ◽  
Brain Mitochondria ◽  
Rat Brain Mitochondria
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