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Molecular mechanism of translocation through nuclear pore complexes during nuclear protein import
Author(s) -
Stewart Murray,
Baker Rosanna P,
Bayliss Richard,
Clayton Lesley,
Grant Richard P,
Littlewood Trevor,
Matsuura Yoshiyuki
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02489-9
Subject(s) - nucleoporin , nuclear pore , importin , nuclear transport , cytoplasm , ran , macromolecule , biophysics , steric effects , nucleus , nuclear protein , chemistry , cell nucleus , transport protein , microbiology and biotechnology , nuclear export signal , biology , biochemistry , stereochemistry , gene , transcription factor
The trafficking of macromolecules between cytoplasm and nucleus through nuclear pore complexes is mediated by specific carrier molecules such as members of the importin‐β family. Nuclear pore proteins (nucleoporins) frequently contain sequence repeats based on FG cores and carriers appear to move their cargo through the pores by hopping between successive FG cores. A major question is why some macromolecules are transported while others are not. This selectivity may be generated by the ability to bind FG repeats, a local concentration of carrier–cargo complexes near the entrance to the pore channel, and steric hindrance produced by high concentrations of nucleoporins in the channel.