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© Research
Event

Department of Structural Biology and Chemistry seminar: Pr Michael P. Rout, A Hole New View: Structure-Function Mapping of the Nuclear Pore Complex

Scientific Fields
Diseases
Organisms
Applications
Technique
Date
10
Apr 2019
Time
14:00:00
28 Rue du Dr Roux, Paris, France
Address
Building: François Jacob
Location
2019-04-10 14:00:00 2019-04-10 15:00:00 Europe/Paris Department of Structural Biology and Chemistry seminar: Pr Michael P. Rout, A Hole New View: Structure-Function Mapping of the Nuclear Pore Complex Department of Structural Biology and Chemistry SEMINAR Mercredi 10 avril 2019 à 14h00 Salle AUDITORIUM CENTRE F. JACOB – CFJ RdC 17c Pr Michael P. Rout Rockefeller University, New York A Hole New View: Structure-Function Mapping […] 28 Rue du Dr Roux, Paris, France Riccardo Pellarin riccardo.pellarin@pasteur.fr

About

Department of Structural Biology and Chemistry
SEMINAR

Mercredi 10 avril 2019 à 14h00

Salle AUDITORIUM CENTRE F. JACOB – CFJ RdC 17c

Pr Michael P. Rout

Rockefeller University, New York

A Hole New View: Structure-Function Mapping of the Nuclear Pore Complex

Abstract: Nuclear Pore Complexes (NPCs) serve as the gatekeepers of RNA and protein transport between the cytoplasm and nucleoplasm. Despite this central cellular role, their large size and dynamic nature have impeded a full structural and functional elucidation. We have recently determined a subnanometer precision structure for the entire 52 MDa, 552-protein yeast NPC by satisfying diverse data including stoichiometry, a cryo-electron tomography map, and chemical cross-links, revealing the NPC’s functional elements in unprecedented detail. The NPC is surprisingly modular, consisting of only 30 proteins of the nucleoporin family (Nups). These Nups assemble into sub-complexes that form higher-order structures called spokes. Eight spokes assemble into even larger modules: coaxial outer and inner rings form a symmetric core scaffold at the heart of which are found sturdy diagonal columns. The scaffold is connected to a membrane ring, a nuclear basket and cytoplasmic RNA export platform. Flexible connector cables hold these discrete and relatively rigid modules together, an arrangement that imbues the NPC’s scaffold with both strength and flexibility. The scaffold surrounds a central channel that is formed in part by nucleoporins termed FG Nups, from which multiple intrinsically disordered Phe-Gly (FG) repeat motifs project, contributing to an organized central density termed the central transporter. These FG motifs mediate selective nucleocytoplasmic transport through specific interactions with nuclear transport factors. Taken together, this integrative structure allows us to rationalize the architecture and transport mechanism of the NPC.

Contact : Riccardo Pellarin

Structural Bioinformatics Unit

riccardo.pellarin@pasteur.fr

Location

Building: François Jacob
Address: 28 Rue du Dr Roux, Paris, France