NESdb: a database of NES-containing CRM1 cargoes
نویسندگان
چکیده
منابع مشابه
NESdb: a database of NES-containing CRM1 cargoes
The leucine-rich nuclear export signal (NES) is the only known class of targeting signal that directs macromolecules out of the cell nucleus. NESs are short stretches of 8-15 amino acids with regularly spaced hydrophobic residues that bind the export karyopherin CRM1. NES-containing proteins are involved in numerous cellular and disease processes. We compiled a database named NESdb that contain...
متن کاملSequence and structural analyses of nuclear export signals in the NESdb database
We compiled >200 nuclear export signal (NES)-containing CRM1 cargoes in a database named NESdb. We analyzed the sequences and three-dimensional structures of natural, experimentally identified NESs and of false-positive NESs that were generated from the database in order to identify properties that might distinguish the two groups of sequences. Analyses of amino acid frequencies, sequence logos...
متن کاملA 2.1-Å-resolution crystal structure of unliganded CRM1 reveals the mechanism of autoinhibition.
CRM1 mediates nuclear export of numerous proteins and ribonucleoproteins containing a leucine-rich nuclear export signal (NES). Binding of RanGTP to CRM1 in the nucleus stabilizes cargo association with CRM1, and vice versa, but the mechanism underlying the positive cooperativity in RanGTP and NES binding to CRM1 remains incompletely understood. Herein we report a 2.1-Å-resolution crystal struc...
متن کاملRanGTP-regulated interactions of CRM1 with nucleoporins and a shuttling DEAD-box helicase.
CRM1 is an export receptor mediating rapid nuclear exit of proteins and RNAs to the cytoplasm. CRM1 export cargoes include proteins with a leucine-rich nuclear export signal (NES) that bind directly to CRM1 in a trimeric complex with RanGTP. Using a quantitative CRM1-NES cargo binding assay, significant differences in affinity for CRM1 among natural NESs are demonstrated, suggesting that the st...
متن کاملCRM1 and Ran are present but a NES-CRM1-RanGTP complex is not required in Balbiani ring mRNP particles from the gene to the cytoplasm.
Messenger RNA is formed from precursors known as pre-mRNA. These precursors associate with proteins to form pre-mRNA-protein (pre-mRNP) complexes. Processing machines cap, splice and polyadenylate the pre-mRNP and in this way build the mRNP. These processing machines also affect the export of the mRNP complexes from the nucleus to the cytoplasm. Export to the cytoplasm takes place through a str...
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ژورنال
عنوان ژورنال: Molecular Biology of the Cell
سال: 2012
ISSN: 1059-1524,1939-4586
DOI: 10.1091/mbc.e12-01-0045