TY - JOUR
T1 - Structural and functional analysis of Nup120 suggests ring formation of the Nup84 complex
AU - Seo, Hyuk Soo
AU - Ma, Yingli
AU - Debler, Erik W.
AU - Wacker, Daniel
AU - Kutik, Stephan
AU - Blobel, Günter
AU - Hoelz, André
PY - 2009/8/25
Y1 - 2009/8/25
N2 - The Nup84 complex constitutes a key building block in the nuclear pore complex (NPC). Here we present the crystal structure of one of its 7 components, Nup120, which reveals a β propeller and an α-helical domain representing a novel fold. We discovered a previously unidentified interaction of Nup120 with Nup133 and confirmed the physiological relevance in vivo. As mapping of the individual components in the Nup84 complex places Nup120 and Nup133 at opposite ends of the heptamer, our findings indicate a head-to-tail arrangement of elongated Nup84 complexes into a ring structure, consistent with a fence-like coat for the nuclear pore membrane. The attachment site for Nup133 lies at the very end of an extended unstructured region, which allows for flexibility in the diameter of the Nup84 complex ring. These results illuminate important roles of terminal unstructured segments in nucleoporins for the architecture, function, and assembly of the NPC.
AB - The Nup84 complex constitutes a key building block in the nuclear pore complex (NPC). Here we present the crystal structure of one of its 7 components, Nup120, which reveals a β propeller and an α-helical domain representing a novel fold. We discovered a previously unidentified interaction of Nup120 with Nup133 and confirmed the physiological relevance in vivo. As mapping of the individual components in the Nup84 complex places Nup120 and Nup133 at opposite ends of the heptamer, our findings indicate a head-to-tail arrangement of elongated Nup84 complexes into a ring structure, consistent with a fence-like coat for the nuclear pore membrane. The attachment site for Nup133 lies at the very end of an extended unstructured region, which allows for flexibility in the diameter of the Nup84 complex ring. These results illuminate important roles of terminal unstructured segments in nucleoporins for the architecture, function, and assembly of the NPC.
KW - Crystal structure
KW - Fluorescence localization
KW - Nuclear pore complex
KW - Site-directed mutagenesis
KW - mRNA export
UR - http://www.scopus.com/inward/record.url?scp=70149101590&partnerID=8YFLogxK
U2 - 10.1073/pnas.0907453106
DO - 10.1073/pnas.0907453106
M3 - Article
C2 - 19706512
AN - SCOPUS:70149101590
SN - 0027-8424
VL - 106
SP - 14281
EP - 14286
JO - Proceedings of the National Academy of Sciences of the United States of America
JF - Proceedings of the National Academy of Sciences of the United States of America
IS - 34
ER -