Boer JM, van Deursen JMA, Huib HC, Fransen JAM, Grosveld GC (1997) The nucleoporin CAN/Nup214 binds to both the cytoplasmic and the nucleoplasmic sides of the nuclear pore complex in overexpressing cells. Exp Cell Res 232: 182–185...
Figure 2. The Nuclear Pore Is a Dense Phase of Disordered Proteins That Forms a Selective Barrier. (A) Schematic of the nuclear pore complex. The nuclear pore is lined with disordered domains of nucleoporin (Nup) proteins containing phenylalanine and glycine (FG) dyad repeats. Image reproduced...
The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88 The oncogenic nucleoporin CAN/Nup214 is essential in vertebrate cells. Its depletion results in defective nuclear protein import, inhibition of messenger R... Fornerod,M. -...
G2 arrest and impaired nucleocytoplasmic transport in mouse embryos lacking the proto-oncogene CAN/Nup214. The vertebrate nucleopore complex (NPC) is a 125 MDa multiprotein assembly that mediates nucleocytoplasmic transport, One of its components, CAN/Nup214, is... van Deursen, J.,J Boer,L Ka...
[12,26]. The Nup214-Nup88 subcomplex facilitates nuclear export by directly binding to the nuclear export receptor Crm1 [67]. The FG domain in the extreme C terminal of Nup214 also interacts with the mRNA export protein Nxf1 [68]. Nup42 interacts with the shuttling mRNA export mediator ...
accumulates at the perinuclear cellular compartment and co-localizes with the nuclear pore complex Nup62 protein, suggesting a role in nuclear membrane ... D Bertozzi,R Iurlaro,O Sordet,... - 《Taylor & Francis》 被引量: 39发表: 0年 [Structure and function of nuclear pore complex]. Auth...
Nup98/RAE1 and Nup42/Gle1/DDX19, are recruited to the vicinity using long linkers. The Nup214 complex thus localize critical factors to remove mRNA from its export factors in the final step of mRNA export.73Unlike Nup358-mediated protein export termination, this process is independent of Ran...
In Xenopus laevis, full-length Nup160 consists of a seven-bladed β-propeller followed by an extended α-helical domain, and its C-terminal fragment is located at the vertex of the Y complex and sandwiched between Sec13 homolog 1 (Seh1) and SEC13-like protein 1 (Sec13) (Zhu et al. ...
The molecular mechanisms that allow HIV to integrate into particular sites of the host genome are poorly understood. Here we tested if the nuclear pore complex (NPC) facilitates the targeting of HIV integration by acting on chromatin topology. We show th
Mechanism of mRNA Transport Through the Nuclear Pore Nuclear export of mRNA is an essential process in eukaryotic gene expression. Immediately after initiation of transcription, mRNA binds to various proteins to form an mRNA–protein complex (messenger ribonucleoprotein: mRNP) [35,36]. The mRNA precu...