[原分所演講] IAMS Lecture on Dec 28, 10:00am, Dr. Poe Lecture Hall, Dr. Seung Joong Kim
IAMS Lecture Announcement
中研院原分所演講公告
中研院原分所演講公告
Title: Structural and Functional Anatomy of a Nuclear Pore Complex
Speaker: Dr. Seung Joong Kim (Department of Bioengineering and Therapeutic Sciences, University of California at San Francisco (UCSF), USA)
Time: 10:00 AM, December 28 (Thursday), 2017
Place: Dr. Poe Lecture Hall, IAMS (本所浦大邦講堂 臺大校園內)
Contact: Dr. Jung-Chi Liao 廖仲麒博士
Speaker: Dr. Seung Joong Kim (Department of Bioengineering and Therapeutic Sciences, University of California at San Francisco (UCSF), USA)
Time: 10:00 AM, December 28 (Thursday), 2017
Place: Dr. Poe Lecture Hall, IAMS (本所浦大邦講堂 臺大校園內)
Contact: Dr. Jung-Chi Liao 廖仲麒博士
Abstract:
Despite the central role of Nuclear Pore Complexes (NPCs) as gatekeepers of RNA and protein transport between the cytoplasm and nucleoplasm, their large size and dynamic nature have impeded a full structural and functional elucidation. Here, we have determined a subnanometer precision structure for the entire 552-protein yeast NPC by satisfying diverse data, including primarily stoichiometry, a cryo-electron tomography map, and chemical cross-links. The structure reveals the NPC’s functional elements in unprecedented detail. The NPC is built of sturdy diagonal columns to which are attached connector cables, imbuing both strength and flexibility, and tying together all other elements of the NPC, including membrane-interacting regions and RNA processing platforms. Inwardly-directed anchors create a high density of transport factor-docking Phe-Gly repeats in the NPC’s central channel, organized in distinct functional units. Taken together, this integrative structure allows us to rationalize the architecture, transport mechanism, and evolutionary origins of the NPC.
Despite the central role of Nuclear Pore Complexes (NPCs) as gatekeepers of RNA and protein transport between the cytoplasm and nucleoplasm, their large size and dynamic nature have impeded a full structural and functional elucidation. Here, we have determined a subnanometer precision structure for the entire 552-protein yeast NPC by satisfying diverse data, including primarily stoichiometry, a cryo-electron tomography map, and chemical cross-links. The structure reveals the NPC’s functional elements in unprecedented detail. The NPC is built of sturdy diagonal columns to which are attached connector cables, imbuing both strength and flexibility, and tying together all other elements of the NPC, including membrane-interacting regions and RNA processing platforms. Inwardly-directed anchors create a high density of transport factor-docking Phe-Gly repeats in the NPC’s central channel, organized in distinct functional units. Taken together, this integrative structure allows us to rationalize the architecture, transport mechanism, and evolutionary origins of the NPC.