The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo.

doi:10.1083/jcb.200407156

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Article

The FG-repeat asymmetry of the nuclear pore complex is dispensable for bulk nucleocytoplasmic transport in vivo.

The Journal of cell biology - 22 Nov 2004

Zeitler Bryan, Weis Karsten

Abstract excerpt

Nucleocytoplasmic transport occurs through gigantic proteinaceous channels called nuclear pore complexes (NPCs). Translocation through the NPC is exquisitely selective and is mediated by interactions between soluble transport carriers and insoluble NPC proteins that contain phenylalanine-glycine (FG) repeats. Although most FG nucleoporins (Nups) are organized symmetrically about the planar axis of the nuclear...

Topics

Active Transport, Cell Nucleus
Amino Acid Motifs
Binding Sites
Cytoplasm
Glycine
Karyopherins
Membrane Transport Proteins
Mutation
Nuclear Pore
Nuclear Pore Complex Proteins
Phenylalanine

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Binding

Protein Transport

RNA, Messenger

Receptors, Cytoplasmic and Nuclear

Saccharomyces cerevisiae

Saccharomyces cerevisiae Proteins

Trinucleotide Repeats

Source

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Identifiers

PMID: 15557115
DOI: 10.1083/jcb.200407156
PMCID: PMC2172579

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