Nuclear pore targeting of the yeast Pom33 nucleoporin depends on karyopherin- and lipid-binding Aurélie G. Floch 1,2 , David Tareste 1 , Patrick Fuchs 1 , Anne Chadrin 1,2 , Ikrame Naciri 1 , Thibaut Leger 3 , Gabriel Schlenstedt 4 , Benoit Palancade 1* and Valérie Doye 1* 1 Institut Jacques Monod, UMR 7592 CNRS, Université Paris Diderot, Sorbonne Paris Cité, F-75205 Paris, France 2 Ecole Doctorale Gènes Génomes Cellules, Université Paris Sud, Orsay, France 3 Proteomic facility, Institut Jacques Monod, Paris, France 4 Universität des Saarlandes, Medizinische Biochemie und Molekularbiologie, Homburg, Germany. * The last two authors equally contributed to this study. Correspondence: Valérie DOYE Institut Jacques Monod, UMR7592 CNRS/Université Paris Diderot 15, rue Hélène Brion 75205 PARIS cedex 13 France Phone +33 1 57 27 80 60 Fax +33 1 57 27 80 63 email : doye.valerie@ijm.univ-paris-diderot.fr Keywords: nuclear pore complexes (NPC), integral membrane protein, karyopherin, amphipathic helices, NPC targeting, NPC distribution, TMEM33 family Running title: NPC targeting determinants of Pom33 © 2014. Published by The Company of Biologists Ltd. Journal of Cell Science Accepted manuscript JCS Advance Online Article. Posted on 20 November 2014