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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 24 (1993), S. 245-255 
    ISSN: 0886-1544
    Keywords: tubulin ; microtubule-associated proteins ; membranous organelles ; interaction ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: To explore the behaviour of microtubule-associated proteins, MAP2 and TAU in the interactions of mitochondria with microtubules, an homologous acellular system has been reconstituted with organelles isolated from rat brain. We have established a quantitative in vitro binding assay based on the cosedimentation of 125I-labeled microtubules with mitochondria. We found that binding of microtubules to mitochondria was concentration dependent and saturable. Binding was insensitive to ATP. A comparison of taxol-stabilized microtubules prepared from MAP-free tubulin or tubulin coated with TAU or MAP2 showed that the microtubule-associated proteins diminished, or reduced to background levels, the formation of complexes with mitochondria. In contrast, the amount of MAP-free taxol microtubules that cosedimented with mitochondria increased two- and six-fold when mitochondria were coated with MAP2 or TAU. These studies suggest that the two major brain MAPs could have a crosslinking or a spacing role, depending on their organelle localization. © 1993 Wiley-Liss, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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