Buchumschlag

Two differential binding mechanisms of FG-nucleoporins and nuclear transport receptors

Summary - 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...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Hauptverfasser: Tan, Piau Siong (VerfasserIn) , Mercadante, Davide (VerfasserIn) , Gräter, Frauke (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: March 27, 2018
In: Cell reports
Year: 2018, Jahrgang: 22, Heft: 13, Pages: 3660-3671
ISSN:2211-1247
DOI:10.1016/j.celrep.2018.03.022
Online-Zugang:Verlag, Volltext: https://doi.org/10.1016/j.celrep.2018.03.022
Verlag, Volltext: http://www.sciencedirect.com/science/article/pii/S2211124718303516
Volltext
Verfasserangaben:Piau Siong Tan, Iker Valle Aramburu, Davide Mercadante, Swati Tyagi, Aritra Chowdhury, Daniel Spitz, Sarah L. Shammas, Frauke Gräter, Edward A. Lemke
Beschreibung
Zusammenfassung:Summary - 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.
Beschreibung:Gesehen am 08.05.2019
Beschreibung:Online Resource
ISSN:2211-1247
DOI:10.1016/j.celrep.2018.03.022

Ähnliche Einträge