Published 18 February 2002. doi:10.1083/jcb.200111003
© The Rockefeller University Press,
0021-9525/2002/2/631 $5.00
The Journal of Cell Biology, Volume 156, Number 4, February 18, 2002 631-642
CLIPR-59, a new trans-Golgi/TGN cytoplasmic linker protein belonging to the CLIP-170 family
Franck Perez1,
Karin Pernet-Gallay1,
Clément Nizak1,
Holly V. Goodson2,
Thomas E. Kreis3 and
Bruno Goud1
1 Institut Curie, CNRS UMR144, 75248 Paris, France
2 University of Notre Dame, Department of Chemistry and Biochemistry, Notre Dame, IN 46556
3 University of Geneva, Department of Cell Biology, 1211 Geneva 4, Switzerland
Address correspondence to Franck Perez, Institut Curie, CNRS UMR144, 26 rue d'Ulm, 75248 Paris Cedex 05, France. Tel.: 33-14-234-6440. Fax: 33-14-234-6382. E-mail: franck.perez{at}curie.fr
The microtubule cytoskeleton plays a fundamental role in cell organization and membrane traffic in higher eukaryotes. It is well established that molecular motors are involved in membranemicrotubule interactions, but it has also been proposed that nonmotor microtubule-binding (MTB) proteins known as CLIPs (cytoplasmic linker proteins) have basic roles in these processes. We report here the characterization of CLIPR-59, a CLIP-170related protein localized to the trans-most part of the Golgi apparatus. CLIPR-59 contains an acidic region followed by three ankyrin-like repeats and two CLIP-170related MTB motifs. We show that the 60amino acidlong carboxy-terminal domain of CLIPR-59 is necessary and sufficient to achieve Golgi targeting, which represents the first identification of a membrane targeting domain in a CLIP-170related protein. The MTB domain of CLIPR-59 is functional because it localizes to microtubules when expressed as a fragment in HeLa cells. However, our results suggest that this domain is normally inhibited by the presence of adjacent domains, because neither full-length CLIPR-59 nor a CLIPR-59 mutant missing its membrane-targeting region localize to microtubules. Consistent with this observation, overexpression of CLIPR-59 does not affect the microtubule network. However, CLIPR-59 overexpression strongly perturbs early/recycling endosomeTGN dynamics, implicating CLIPR-59 in the regulation of this pathway.
Key Words: microtubules; Golgi apparatus; trans-Golgi network; endocytosis; intracellular traffic

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