期刊
EUROPEAN JOURNAL OF CELL BIOLOGY
卷 90, 期 9, 页码 751-758出版社
ELSEVIER GMBH, URBAN & FISCHER VERLAG
DOI: 10.1016/j.ejcb.2011.04.004
关键词
Nuclear pore complex; Nuclear transport; Transport model; Nuclear transport receptor; FG repeats; Super-resolution microscopy
类别
资金
- Deutsche Forschungsgemeinschaft [SFB431]
It is generally accepted that transport through the nuclear pore complex (NPC) involves an abundance of phenylalanine-glycine rich protein domains (FG-domains) that serve as docking sites for soluble nuclear transport receptors (NTRs) and their cargo complexes. But the precise mechanism of translocation through the NPC allowing for high speed and selectivity is still vividly debated. To ultimately decipher the underlying gating mechanism it is indispensable to shed more light on the molecular arrangement of FG-domains and the distribution of NTR-binding sites within the central channel of the NPC. In this review we revisit current transport models, summarize recent results regarding translocation through the NPC obtained by super-resolution microscopy and finally discuss the status and potential of optical methods in the analysis of the NPC. (C) 2011 Elsevier GmbH. All rights reserved.
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