title: A role for the yeast CLIP170 ortholog, the plus-end-tracking protein Bik1, and the Rho1 GTPase in Snc1 trafficking.
abstract: The diversity of microtubule functions is dependent on the status of tubulin C-termini. To address the physiological role of the C-terminal aromatic residue of α-tubulin, a tub1-Glu yeast strain expressing an α-tubulin devoid of its C-terminal amino acid was used to perform a genome-wide-lethality screen. The identified synthetic lethal genes suggested links with endocytosis and related processes. In the tub1-Glu strain, the routing of the v-SNARE Snc1 was strongly impaired, with a loss of its polarized distribution in the bud, and Abp1, an actin patch or endocytic marker, developed comet-tail structures. Snc1 trafficking required dynamic microtubules but not dynein and kinesin motors. Interestingly, deletion of the microtubule plus-end-tracking protein Bik1 (a CLIP170 ortholog), which is preferentially recruited to the C-terminal residue of α-tubulin, similarly resulted in Snc1 trafficking defects. Finally, constitutively active Rho1 rescued both Bik1 localization at the microtubule plus-ends in tub1-Glu strain and a correct Snc1 trafficking in a Bik1-dependent manner. Our results provide the first evidence for a role of microtubule plus-ends in membrane cargo trafficking in yeast, through Rho1- and Bik1-dependent mechanisms, and highlight the importance of the C-terminal α-tubulin amino acid in this process.
authors.affiliation: Univ. Grenoble Alpes, Grenoble F-38000, France Inserm, U1216, Grenoble F-38000, France CEA, BIG, Grenoble F-38000, France Cecile.Boscheron@univ-grenoble-alpes.fr Annie.Andrieux@univ-grenoble-alpes.fr.
authors.forename: Cécile
authors.identifier: 0000-0002-0620-4026
authors.initials: C
authors.lastname: Boscheron
authors.affiliation: Univ. Grenoble Alpes, Grenoble F-38000, France Inserm, U1216, Grenoble F-38000, France CEA, BIG, Grenoble F-38000, France Institute of Biochemistry, Department of Biology, ETH Zurich, Zurich 8093, Switzerland.
authors.forename: Fabrice
authors.identifier: 0000-0001-5159-1507
authors.initials: F
authors.lastname: Caudron
authors.affiliation: Institut Curie, Recombinaison et Instabilité Génétique, CNRS UMR3244, Université Pierre et Marie Curie, Paris Cedex 75048, France.
authors.forename: Sophie
authors.initials: S
authors.lastname: Loeillet
authors.affiliation: Univ. Grenoble Alpes, Grenoble F-38000, France Inserm, U1216, Grenoble F-38000, France CEA, BIG, Grenoble F-38000, France.
authors.forename: Charlotte
authors.identifier: 0000-0003-3980-3524
authors.initials: C
authors.lastname: Peloso
authors.affiliation: Univ. Grenoble Alpes, Grenoble F-38000, France Inserm, U1216, Grenoble F-38000, France CEA, BIG, Grenoble F-38000, France.
authors.forename: Marine
authors.identifier: 0000-0001-8625-9766
authors.initials: M
authors.lastname: Mugnier
authors.affiliation: CEA, BIG, Grenoble F-38000, France.
authors.forename: Laetitia
authors.initials: L
authors.lastname: Kurzawa
authors.affiliation: Institut Curie, Recombinaison et Instabilité Génétique, CNRS UMR3244, Université Pierre et Marie Curie, Paris Cedex 75048, France.
authors.forename: Alain
authors.identifier: 0000-0002-0559-312X
authors.initials: A
authors.lastname: Nicolas
authors.affiliation: Univ. Grenoble Alpes, Grenoble F-38000, France Inserm, U1216, Grenoble F-38000, France CEA, BIG, Grenoble F-38000, France.
authors.forename: Eric
authors.initials: E
authors.lastname: Denarier
authors.affiliation: Univ. Grenoble Alpes, Grenoble F-38000, France CEA, BIG, Grenoble F-38000, France Inserm, U1038, Grenoble F-38000, France.
authors.forename: Laurence
authors.initials: L
authors.lastname: Aubry
authors.affiliation: Univ. Grenoble Alpes, Grenoble F-38000, France Inserm, U1216, Grenoble F-38000, France CEA, BIG, Grenoble F-38000, France Cecile.Boscheron@univ-grenoble-alpes.fr Annie.Andrieux@univ-grenoble-alpes.fr.
authors.forename: Annie
authors.identifier: 0000-0002-4022-6405
authors.initials: A
authors.lastname: Andrieux
mesh_terms: D003080:Cold Temperature; D005820:Genetic Testing; D018698:Glutamic Acid / Q000378:metabolism; D049452:Green Fluorescent Proteins / Q000378:metabolism; D008869:Microtubule-Associated Proteins / Q000737:chemistry* / Q000378:metabolism*; D008870:Microtubules / Q000378:metabolism; D009363:Neoplasm Proteins / Q000737:chemistry*; D021381:Protein Transport; D050683:R-SNARE Proteins / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014404:Tubulin / Q000737:chemistry / Q000378:metabolism; D020741:rho GTP-Binding Proteins / Q000378:metabolism*
chemical_list: C488173:Bik1 protein, S cerevisiae; D008869:Microtubule-Associated Proteins; D009363:Neoplasm Proteins; D050683:R-SNARE Proteins; C083241:SNC1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D014404:Tubulin; D049452:Green Fluorescent Proteins; C076744:cytoplasmic linker protein 170; D018698:Glutamic Acid; C051302:RHO1 protein, S cerevisiae; D020741:rho GTP-Binding Proteins
keywords: +Tips; CLIP170; Microtubule; Rho1; Trafficking; Tyrosination