Gmap-210, a cis-Golgi network-associated protein, is a minus end microtubule-binding protein
| Autor: | Carlos Infante, Francisco Ramos-Morales, Concepcion Fedriani, Michel Bornens, Rosa M. Rios |
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| Přispěvatelé: | Universidad de Sevilla. Departamento de Genética, Universidad de Sevilla. Departamento de Microbiología |
| Jazyk: | angličtina |
| Rok vydání: | 1999 |
| Předmět: |
DNA
Complementary Paclitaxel Microtubule-associated protein Recombinant Fusion Proteins Green Fluorescent Proteins Molecular Sequence Data Golgi Apparatus Biology Transfection Microtubules microtubules symbols.namesake Microtubule Genes Reporter Tubulin Animals Humans Amino Acid Sequence Nuclear protein Cis-Golgi network Interphase Sequence Deletion Centrosome Binding Sites Binding protein Molecular Motor Proteins microtubule-associated proteins Nuclear Proteins microtubule- associated proteins Cell Biology Golgi apparatus Cell biology Molecular Weight Cytoskeletal Proteins Luminescent Proteins centrosome Microscopy Fluorescence COS Cells symbols biology.protein autoantigens HeLa Cells Regular Articles |
| Zdroj: | The Journal of Cell Biology idUS. Depósito de Investigación de la Universidad de Sevilla instname |
| Popis: | 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. 125:997Ð1013) is a microtubule-binding protein that associates in situ with a subpopulation of stable microtubules. Interaction of this protein, now called GMAP-210, for Golgi microtubule-associated protein 210, with microtubules in vitro is direct, tight and nucleotide-independent. Biochemical analysis further suggests that GMAP-210 specifically binds to microtubule ends. The full-length cDNA encoding GMAP-210 predicts a protein of 1,979 amino acids with a very long central coiled-coil domain. Deletion analyses in vitro show that the COOH terminus of GMAP- 210 binds to microtubules whereas the NH 2 terminus binds to Golgi membranes. Overexpression of GMAP- 210Ðencoding cDNA induced a dramatic enlargement of the Golgi apparatus and perturbations in the microtubule network. These effects did not occur when a mutant lacking the COOH-terminal domain was expressed. When transfected in fusion with the green fluorescent protein, the NH 2 -terminal domain associated with the cis-Golgi network whereas the COOHterminal microtubule-binding domain localized at the centrosome. Altogether these data support the view that GMAP-210 serves to link the cis-Golgi network to the minus ends of centrosome-nucleated microtubules. In addition, this interaction appears essential for ensuring the proper morphology and size of the Golgi apparatus |
| Databáze: | OpenAIRE |
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