TY  - JOUR
AB  - Existence 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.
AU  - Liashkovich, Ivan
AU  - Pasrednik, Dzmitry
AU  - Prystopiuk, Valeria
AU  - Rosso, Gonzalo
AU  - Oberleithner, Hans
AU  - Shahin, Victor
DA  - 2015-05-06
DO  - 10.1038/srep09994
LA  - eng
N1  - Scientific Reports 5 (2015) 9994, 1-9
N1  - Finanziert durch den Open-Access-Publikationsfonds 2015/2016 der Westfälischen Wilhelms-Universität Münster (WWU Münster).
PY  - 2015-05-06
SN  - 2045-2322
TI  - Clathrin inhibitor Pitstop-2 disrupts the nuclear pore complex permeability barrier
UR  - https://nbn-resolving.org/urn:nbn:de:hbz:6-57279462104
Y2  - 2024-11-22T03:30:14
ER  -