Centaurin-α2 is constituted by an Arf-Gap zinc binding domain and two PH domains. In EGF stimulated cells, centaurin-α2 localizes at plasma membrane through PIP2/PIP3 binding and it promotes the inactivation of Arf6, involved in intracellular vesicular trafficking and in cytoskeletal rearrangement. With the final aim of elucidating the centaurin-α2 molecular pathways and its biological role/s, we searched for centaurin- α2 interacting proteins by an yeast two-hybrid assay: our studies evidenced the interaction between centaurin-α2 and tubulin β, confirmed by coimmunoprecipitation experiments. Confocal microscopy analysis allowed us to co-localize centaurin-α2 with microtubules. By western blotting analyses we found that centaurin-α2 is preferentially associated with polymerized fraction of tubulin and remained associated with microtubules resistant to cold or/and nocodazol treatment. Moreover in cell transfected with centaurin-α2, we observed an increase of acetylated microtubules (MT), a well known marker of stable MT, suggesting that centaurin-α2 increases the stability of MT. We are going to define the centaurin-α2 domain/s interacting with tubulin β by β-galactosidase assay and immunofluorescence experiments. We will check by live imaging the co-localization of centaurin-α2 with tubulin β during its translocation from cytosol to membrane, by means of GFP-centaurin-α2 transfection following EGF stimulation. Our finding allow us to speculate that centaurin-α2 can move to plasma membrane through microtubule anchoring and that this protein could act as agent stabilizing microtubules

Centaurin-α2 and tubulin interaction increases microtubule stability / M. Stroppi, D. Cartelli, G. Cappelletti, M. Venturin, S. Rigoletto, E. Battaglioli, P. Riva. - In: EUROPEAN JOURNAL OF HUMAN GENETICS. - ISSN 1018-4813. - 18:Suppl.1(2010), pp. 272-273. (Intervento presentato al convegno European Human Genetics Conference tenutosi a Gothenburg nel 2010) [10.1038/ejhg.2009.203].

Centaurin-α2 and tubulin interaction increases microtubule stability

M. Stroppi;D. Cartelli;G. Cappelletti;M. Venturin;E. Battaglioli;P. Riva
2010

Abstract

Centaurin-α2 is constituted by an Arf-Gap zinc binding domain and two PH domains. In EGF stimulated cells, centaurin-α2 localizes at plasma membrane through PIP2/PIP3 binding and it promotes the inactivation of Arf6, involved in intracellular vesicular trafficking and in cytoskeletal rearrangement. With the final aim of elucidating the centaurin-α2 molecular pathways and its biological role/s, we searched for centaurin- α2 interacting proteins by an yeast two-hybrid assay: our studies evidenced the interaction between centaurin-α2 and tubulin β, confirmed by coimmunoprecipitation experiments. Confocal microscopy analysis allowed us to co-localize centaurin-α2 with microtubules. By western blotting analyses we found that centaurin-α2 is preferentially associated with polymerized fraction of tubulin and remained associated with microtubules resistant to cold or/and nocodazol treatment. Moreover in cell transfected with centaurin-α2, we observed an increase of acetylated microtubules (MT), a well known marker of stable MT, suggesting that centaurin-α2 increases the stability of MT. We are going to define the centaurin-α2 domain/s interacting with tubulin β by β-galactosidase assay and immunofluorescence experiments. We will check by live imaging the co-localization of centaurin-α2 with tubulin β during its translocation from cytosol to membrane, by means of GFP-centaurin-α2 transfection following EGF stimulation. Our finding allow us to speculate that centaurin-α2 can move to plasma membrane through microtubule anchoring and that this protein could act as agent stabilizing microtubules
Settore BIO/13 - Biologia Applicata
Settore BIO/06 - Anatomia Comparata e Citologia
2010
European Society of Human Genetics
https://www.eshg.org/fileadmin/www.eshg.org/abstracts/ESHG2010Abstracts.pdf
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/199762
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