FG/FxFG as well as GLFG repeats form a selective permeability barrier with self-healing properties

被引:96
作者
Frey, Steffen [1 ]
Goerlich, Dirk [1 ]
机构
[1] Max Planck Inst Biophys Chem, Dept Cellular Logist, D-37077 Gottingen, Germany
关键词
hydrogel; nucleoporin; nuclear pore complex; permeability barrier; selective phase model; NUCLEAR-PORE COMPLEX; IMPORTIN-BETA; PROTEIN IMPORT; FLUORESCENT PROTEINS; NUCLEOPORIN COMPLEX; STRUCTURAL BASIS; TRANSPORT; BINDING; EXPORT; TRANSLOCATION;
D O I
10.1038/emboj.2009.199
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The permeability barrier of nuclear pore complexes (NPCs) controls all nucleo-cytoplasmic exchange. It is freely permeable for small molecules. Objects larger than approximate to 30 kDa can efficiently cross this barrier only when bound to nuclear transport receptors (NTRs) that confer translocation-promoting properties. We had shown earlier that the permeability barrier can be reconstituted in the form of a saturated FG/FxFG repeat hydrogel. We now show that GLFG repeats, the other major FG repeat type, can also form highly selective hydrogels. While supporting massive, reversible importin-mediated cargo influx, FG/FxFG, GLFG or mixed hydrogels remained firm barriers towards inert objects that lacked nuclear transport signals. This indicates that FG hydrogels immediately reseal behind a translocating species and thus possess 'self-healing' properties. NTRs not only left the barrier intact, they even tightened it against passive influx, pointing to a role for NTRs in establishing and maintaining the permeability barrier of NPCs. The EMBO Journal (2009) 28, 2554-2567. doi: 10.1038/emboj.2009.199; Published online 13 August 2009 Subject Categories: membranes & transport
引用
收藏
页码:2554 / 2567
页数:14
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