A Kramer

BB Huelsmann

CJ Edgell

D Devos

E Laurell

I Liashkovich

JB Grinspan

K Ribbeck

KH Bui

L von Kleist

LI Davis

M Raices

MA D′Angelo

MS Moore

PL Paine

RE Vandenbroucke

S Walde

SA Adam

SS Patel

U Griesenbach

U Kutay

Scientific Reports

AbstractExistence of a selective nucleocytoplasmic permeability barrier is attributed to Phenylalanine-Glycine rich proteins (FG-nups) within the central channel of the nuclear pore complex (NPC). Limited understanding of the FG-nup structural arrangement hinders development of strategies directed at disrupting the NPC permeability barrier. In this report we explore an alternative approach to enhancing the NPC permeability for exogenous macromolecules. We demonstrate that the recently discovered inhibitor of clathrin coat assembly Pitstop-2 compromises the NPC permeability barrier in a rapid and effective manner. Treatment with Pitstop-2 causes a collapse of the NPC permeability barrier and a reduction of Importin β binding accompanied by alteration of the NPC ultrastructure. Interestingly, the effects are induced by the same chemical agent that is capable of inhibiting clathrin-mediated endocytosis. To our knowledge, this is the first functional indication of the previously postulated evolutionary relation between clathrin and NPC scaffold proteins.</jats:p

Ivan Liashkovich

Dzmitry Pasrednik

Valeria Prystopiuk

Gonzalo Rosso

Hans Oberleithner

Victor Shahin

Crossref

Clathrin inhibitor Pitstop-2 disrupts the nuclear pore complex permeability barrier

Clathrin inhibitor Pitstop-2 disrupts the nuclear pore complex permeability barrier

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