GMAP-210, A Cis-Golgi Network-associated Protein, Is a Minus End Microtubule-binding Protein

doi:10.1083/jcb.145.1.83

A correction to this article has been published: J. Cell Biol. 158 (3) 593

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J. Cell Biol., Volume 145, Number 1, April 5, 1999 83-98

GMAP-210, A Cis-Golgi Network-associated Protein, Is a Minus End Microtubule-binding Protein

Carlos Infante,^* Francisco Ramos-Morales,^* Concepción Fedriani,^* Michel Bornens, and Rosa M. Rios^*

^* Departamento de Microbiología, Facultad de Biología, Universidad de Sevilla Apdo. 1095, 41080-Sevilla, Spain; and Institut Curie, Section Recherche, UMR144 du CNRS, 75248 Paris, Cedex 05, France

We report that a peripheral Golgi protein with a molecular mass of 210 kD localized at the cis-Golgi network (Rios, R.M.,A.M. Tassin, C. Celati, C. Antony, M.C. Boissier, J.C. Homberg,and M. Bornens. 1994. J. Cell Biol. 125:997-1013) is a microtubule-bindingprotein that associates in situ with a subpopulation of stablemicrotubules. Interaction of this protein, now called GMAP-210,for Golgi microtubule-associated protein 210, with microtubulesin vitro is direct, tight and nucleotide-independent. Biochemicalanalysis further suggests that GMAP-210 specifically binds tomicrotubule ends. The full-length cDNA encoding GMAP-210 predictsa protein of 1,979 amino acids with a very long central coiled-coildomain. Deletion analyses in vitro show that the COOH terminusof GMAP-210 binds to microtubules whereas the NH₂ terminus bindsto Golgi membranes. Overexpression of GMAP-210-encoding cDNA induceda dramatic enlargement of the Golgi apparatus and perturbationsin the microtubule network. These effects did not occur when amutant lacking the COOH-terminal domain was expressed. When transfectedin fusion with the green fluorescent protein, the NH₂-terminaldomain associated with the cis-Golgi network whereas the COOH-terminalmicrotubule-binding domain localized at the centrosome. Altogetherthese data support the view that GMAP-210 serves to link the cis-Golginetwork to the minus ends of centrosome-nucleated microtubules.In addition, this interaction appears essential for ensuring theproper morphology and size of the Golgiapparatus.

Key words: autoantigens; Golgi apparatus; microtubule-associated proteins; microtubules; centrosome

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