Pom121 links two essential subcomplexes of the nuclear pore complex core to the membrane.
Nuclear pore complexes (NPCs) control the movement of molecules across the nuclear envelope (NE). We investigated the molecular interactions that exist at the interface between the NPC scaffold and the pore membrane. We show that key players mediating these interactions in mammalian cells are the nucleoporins Nup155 and Nup160. Nup155 depletion massively alters NE structure, causing a dramatic decrease in NPC numbers and the improper targeting of membrane proteins to the inner nuclear membrane. The role of Nup155 in assembly is likely closely linked to events at the membrane as we show that Nup155 interacts with pore membrane proteins Pom121 and NDC1. Furthermore, we demonstrate that the N terminus of Pom121 directly binds the β-propeller regions of Nup155 and Nup160. We propose a model in which the interactions of Pom121 with Nup155 and Nup160 are predicted to assist in the formation of the nuclear pore and the anchoring of the NPC to the pore membrane.
Department of Cell Biology, University of Alberta, Edmonton, Alberta, Canada.
Jana M
JM
Mitchell
Jörg
J
Mansfeld
Juliana
J
Capitanio
Ulrike
U
Kutay
Richard W
RW
Wozniak
D006801:Humans; D008562:Membrane Glycoproteins / Q000378:metabolism*; D008954:Models, Biological; D009685:Nuclear Envelope / Q000378:metabolism*; D022022:Nuclear Pore / Q000378:metabolism*; D028861:Nuclear Pore Complex Proteins / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism
D008562:Membrane Glycoproteins; C080427:NUP155 protein, human; C440251:NUP160 protein, human; D028861:Nuclear Pore Complex Proteins; D009687:Nuclear Proteins; C094157:POM121 protein, human