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
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:
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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