Binding dynamics of structural nucleoporins govern nuclear pore complex permeability and may mediate channel gating.
The nuclear pore complex (NPC) is a permeable sieve that can dilate to facilitate the bidirectional translocation of a wide size range of receptor-cargo complexes. The binding of receptors to FG nucleoporin docking sites triggers channel gating by an unknown mechanism. Previously, we used deoxyglucose and chilling treatments to implicate Nup170p and Nup188p in the control of NPC sieving in Saccharomyces cerevisiae. Here, we report that aliphatic alcohols increase the permeability of wild-type and nup170Delta NPCs. In conjunction with increases in permeability, aliphatic alcohols, deoxyglucose, and chilling trigger the reversible dissociation of several nucleoporins from nup170Delta NPCs. These results are consistent with the hypothesis that NPC gating occurs when molecular latches composed of FG repeats and structural nucleoporins dissociate.
Shulga
Nataliya
N
Department of Biology, University of Rochester, Rochester, New York 14627, USA.
Goldfarb
David S
DS
D000438:Alcohols / Q000494:pharmacology; D002467:Cell Nucleus / Q000378:metabolism*; D004305:Dose-Response Relationship, Drug; D000431:Ethanol / Q000494:pharmacology; D006018:Glycols / Q000494:pharmacology; D049452:Green Fluorescent Proteins; D007700:Kinetics; D008164:Luminescent Proteins / Q000378:metabolism; D018613:Microscopy, Confocal; D022022:Nuclear Pore / Q000737:chemistry* / Q000378:metabolism; D028861:Nuclear Pore Complex Proteins / Q000737:chemistry* / Q000378:metabolism*; D011485:Protein Binding; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism / Q000502:physiology*; D013997:Time Factors
D000438:Alcohols; D006018:Glycols; D008164:Luminescent Proteins; D028861:Nuclear Pore Complex Proteins; D011993:Recombinant Fusion Proteins; D049452:Green Fluorescent Proteins; D000431:Ethanol; C027765:hexamethylene glycol