The nucleoporin-like protein NLP1 (hCG1) promotes CRM1-dependent nuclear protein export
Autor: | Christiane Spillner, Inga Waldmann, Ralph H. Kehlenbach |
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Rok vydání: | 2012 |
Předmět: |
Nucleocytoplasmic Transport Proteins
Nuclear Envelope Phenylalanine Active Transport Cell Nucleus Glycine Receptors Cytoplasmic and Nuclear Biology Karyopherins environment and public health 03 medical and health sciences 0302 clinical medicine Exportin-1 Genes Reporter Humans Nuclear pore Nuclear protein Nuclear export signal 030304 developmental biology Cell Nucleus 0303 health sciences fungi Nuclear Proteins Cell Biology Cell biology Nuclear Pore Complex Proteins ran GTP-Binding Protein Biochemistry 030220 oncology & carcinogenesis Ran lipids (amino acids peptides and proteins) Nucleoporin Nuclear transport HeLa Cells Protein Binding |
Zdroj: | Journal of cell science. 125(Pt 1) |
ISSN: | 1477-9137 |
Popis: | Translocation of transport complexes across the nuclear envelope is mediated by nucleoporins, proteins of the nuclear pore complex that contain phenylalanine-glycine (FG) repeats as a characteristic binding motif for transport receptors. CRM1 (exportin 1), the major export receptor, forms trimeric complexes with RanGTP and proteins containing nuclear export sequences (NESs). We analyzed the role of the nucleoporin-like protein 1, NLP1 (also known as hCG1 and NUPL2) in CRM1-dependent nuclear transport. NLP1, which contains many FG repeats, localizes to the nuclear envelope and could also be mobile within the nucleus. It promotes the formation of complexes containing CRM1 and RanGTP, with or without NES-containing cargo proteins, that can be dissociated by RanBP1 and/or the cytoplasmic nucleoporin Nup214. The FG repeats of NLP1 do not play a major role in CRM1 binding. Overexpression of NLP1 promotes CRM1-dependent export of certain cargos, whereas its depletion by small interfering RNAs leads to reduced export rates. Thus, NLP1 functions as an accessory factor in CRM1-dependent nuclear protein export. |
Databáze: | OpenAIRE |
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