Long unfolded linkers facilitate membrane protein import through the nuclear pore complex
Autor: | Renee Otten, Bert Poolman, Frans A. A. Mulder, Annemarie Kralt, Rizqiya A. Hapsari, Anne C. Meinema, Liesbeth M. Veenhoff, Justyna K Laba, Geert van den Bogaart, C. Patrick Lusk |
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Přispěvatelé: | Enzymology, Groningen Biomolecular Sciences and Biotechnology, Zernike Institute for Advanced Materials, Molecular Dynamics, Molecular Neuroscience and Ageing Research (MOLAR) |
Jazyk: | angličtina |
Rok vydání: | 2011 |
Předmět: |
Protein Folding
Saccharomyces cerevisiae Proteins Nuclear Envelope Recombinant Fusion Proteins Molecular Sequence Data Nuclear Localization Signals Active Transport Cell Nucleus Saccharomyces cerevisiae Karyopherins Endoplasmic Reticulum Models Biological DOMAIN medicine otorhinolaryngologic diseases Inner membrane Amino Acid Sequence Nuclear pore Nuclear membrane ARCHITECTURE Multidisciplinary biology Membrane transport protein Membrane Proteins Nuclear Proteins TRANSPORT Cell biology Transport protein Protein Structure Tertiary Nuclear Pore Complex Proteins stomatognathic diseases medicine.anatomical_structure Membrane protein biology.protein INTRACELLULAR TRAFFICKING Nuclear Pore Nucleoporin Nuclear transport |
Zdroj: | Meinema, A C, Laba, J K, Hapsari, R A, Otten, R, Mulder, F A A, Kralt, A, van den Bogaart, G, Lusk, C P, Poolman, B & Veenhoff, L M 2011, ' Long unfolded linkers facilitate membrane protein import through the nuclear pore complex ', Science, vol. 333, no. 6038, pp. 90-3 . https://doi.org/10.1126/science.1205741 Science, 333(6038), 90-93. AMER ASSOC ADVANCEMENT SCIENCE |
ISSN: | 0036-8075 |
DOI: | 10.1126/science.1205741 |
Popis: | Active nuclear import of soluble cargo involves transport factors that shuttle cargo through the nuclear pore complex (NPC) by binding to phenylalanine-glycine (FG) domains. How nuclear membrane proteins cross through the NPC to reach the inner membrane is presently unclear. We found that at least a 120-residue-long intrinsically disordered linker was required for the import of membrane proteins carrying a nuclear localization signal for the transport factor karyopherin-a. We propose an import mechanism for membrane proteins in which an unfolded linker slices through the NPC scaffold to enable binding between the transport factor and the FG domains in the center of the NPC. |
Databáze: | OpenAIRE |
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