Abstract：
:Phenylalanine-glycine-rich nucleoporins (FG-Nups) are intrinsically disordered proteins, constituting the selective barrier of the nuclear pore complex (NPC). Previous studies showed that nuclear transport receptors (NTRs) were found to interact with FG-Nups by forming an "archetypal-fuzzy" complex through the rapid formation and breakage of interactions with many individual FG motifs. Here, we use single-molecule studies combined with atomistic simulations to show that, in sharp contrast, FG-Nup214 undergoes a coupled reconfiguration-binding mechanism when interacting with the export receptor CRM1. Association and dissociation rate constants are more than an order of magnitude lower than in the archetypal-fuzzy complex between FG-Nup153 and NTRs. Unexpectedly, this behavior appears not to be encoded selectively into CRM1 but rather into the FG-Nup214 sequence. The same distinct binding mechanisms are unperturbed in O-linked β-N-acetylglucosamine-modified FG-Nups. Our results have implications for differential roles of distinctly spatially distributed FG-Nup⋅NTR interactions in the cell.
journal_name
Cell Repjournal_title
Cell reportsauthors
Tan PS,Aramburu IV,Mercadante D,Tyagi S,Chowdhury A,Spitz D,Shammas SL,Gräter F,Lemke EAdoi
10.1016/j.celrep.2018.03.022subject
Has Abstractpub_date
2018-03-27 00:00:00pages
3660-3671issue
13issn
2211-1247pii
S2211-1247(18)30351-6journal_volume
22pub_type
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