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Volume 271, Number 47, Issue of November 22, 1996 pp. 29882-29890
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Involvement of a Membrane-bound Form of Glutamate Dehydrogenase in the Association of Lysosomes to Microtubules

(Received for publication, July 7, 1996, and in revised form, August 15, 1996)

From the Institut National de la Santé et de la Recherche Médicale, Unité 369, Faculté de Médecine Lyon-RTH Laënnec, 69372 Lyon Cédex 08, France

A 50-kDa membrane protein corresponding to a membrane-bound isoform of glutamate dehydrogenase was proposed as a molecular species that could mediate lysosome-microtubule interactions. This protein, isolated from purified lysosome membranes, is a peripheral membrane protein with an ATP-dependent microtubule binding activity. We have produced antibodies against the purified 50-kDa protein to investigate its role in the association of lysosomes to microtubules using a cell-free reconstitution assay and cell microinjection. Pretreatment of purified lysosomes with the antibodies inhibited the association of these vesicles to microtubules. The blocking effect of antibodies was demonstrated by a differential sedimentation method and negative staining electron microscopy, allowing us to quantify the amount of microtubules interacting with lysosomes and the proportion of lysosomes bound to microtubules, respectively. Affinity-purified antibodies microinjected into intact cells altered the distribution of lysosomes that appeared less clustered in the vicinity of nuclei. The antibody-induced lysosome dispersion was assessed by quantitative videomicroscope analyses. These data show that the 50-kDa membrane protein could act, through its microtubule binding activity, as a molecule of attachment of lysosomes to microtubules. This membrane-bound isoform of glutamate dehydrogenase could be involved in the microtubule-dependent perinuclear localization of lysosomes.

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