Involvement of a membrane-bound form of glutamate dehydrogenase in the association of lysosomes to microtubules.

The Journal of Biological Chemistry
F RajasB Rousset

Abstract

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 m...Continue Reading

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Citations

May 10, 2002·Progress in Neuro-psychopharmacology & Biological Psychiatry·Gulnur Sh BurbaevaIrina S Boksha
May 19, 2009·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·Vasileios MastorodemosAndreas Plaitakis
Jan 18, 2014·Neurochemical Research·Cleanthe SpanakiAndreas Plaitakis
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Jun 20, 2012·Neurochemistry International·Ioannis ZaganasAndreas Plaitakis
May 12, 2009·Neurochemistry International·Ioannis ZaganasAndreas Plaitakis
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