XMAP215 regulates microtubule dynamics through two distinct domains

XMAP215 belongs to a family of proteins involved in the regulation of microtubule dynamics. In this study we analyze the function of different parts of XMAP215 in vivo and in Xenopus egg extracts. XMAP215 has been divided into three fragments, FrN, FrM and FrC (for N‐terminal, middle and C‐terminal,...

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Published in:	The EMBO journal Vol. 20; no. 3; pp. 397 - 410
Main Authors:	Popov, Andrei V., Pozniakovsky, Andrei, Arnal, Isabelle, Antony, Claude, Ashford, Anthony J., Kinoshita, Kazuhisa, Tournebize, Regis, Hyman, Anthony A., Karsenti, Eric
Format:	Journal Article
Language:	English
Published:	Chichester, UK John Wiley & Sons, Ltd 01-02-2001 Blackwell Publishing Ltd Oxford University Press
Subjects:	Animals Binding Sites Cell Line centrosome Centrosome - metabolism Centrosome - ultrastructure Disasters Female In Vitro Techniques Microscopy, Immunoelectron microtubule dynamics Microtubule-Associated Proteins - chemistry Microtubule-Associated Proteins - genetics Microtubule-Associated Proteins - metabolism Microtubules - metabolism Microtubules - ultrastructure mitotic spindle Oocytes - metabolism Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - metabolism Protein Structure, Tertiary Xenopus Xenopus Proteins
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Summary:	XMAP215 belongs to a family of proteins involved in the regulation of microtubule dynamics. In this study we analyze the function of different parts of XMAP215 in vivo and in Xenopus egg extracts. XMAP215 has been divided into three fragments, FrN, FrM and FrC (for N‐terminal, middle and C‐terminal, respectively). FrN co‐localizes with microtubules in egg extracts but not in cells, FrC co‐ localizes with microtubules and centrosomes both in egg extracts and in cells, while FrM does not co‐ localize with either centrosomes or microtubules. In Xenopus egg extracts, FrN stimulates microtubule growth at plus‐ends by inhibiting catastrophes, while FrM has no effect, and FrC suppresses microtubule growth by promoting catastrophes. Our results suggest that XMAP215 is targeted to centrosomes and microtubules mainly through its C‐terminal domain, while the evolutionarily conserved N‐terminal domain contains its microtubule‐stabilizing activity.
Bibliography:	istex:937903178EB02057042EF185C6A4C4648727D8FA ArticleID:EMBJ7593547 Supplementary figure 1. Immunofluorescence localization of XMAP215. (A) With indirect immunofluorescence, XMAP215 is associated with microtubules of a Xenopus XL177 cell during all cell cycle stages. Note the stronger staining of the spindle microtubules compared with astral microtubules. Scale bar, 10 μm.(B) High-magnification immunofluorescence image showing the co-localization of XMAP215 with microtubules in an interphase XL177 cell. XMAP215 appears as punctate staining. Scale bar, 10 μm.Supplementary figure 2. Immunofluorescence localization of ch-TOG. With indirect immunofluorescence using anti-XMAP215 antibodies, ch-TOG appears associated with microtubules and spindle poles of a human HeLa cell. (A) An interphase cell. Scale bar, 10 μm.(B) A metaphase cell. Scale bar, 10 μm.Supplementary data ark:/67375/WNG-H3ZB90FJ-L ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0261-4189 1460-2075 1460-2075
DOI:	10.1093/emboj/20.3.397