Phosphorylation of the nuclear transport machinery down-regulates nuclear protein import in vitro (Q28140841)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:10749866%20AND%20SRC:MED&resulttype=core&format=json

5 November 2019

title

Phosphorylation of the nuclear transport machinery down-regulates nuclear protein import in vitro (English)

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5 November 2019

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1

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5 November 2019

author name string

Gerace L

series ordinal

2

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5 November 2019

language of work or name

English

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publication date

1 June 2000

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Journal of Biological Chemistry

5 November 2019

published in

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5 November 2019

volume

275

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5 November 2019

issue

23

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5 November 2019

page(s)

17848-17856

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The nuclear pore complex: from molecular architecture to functional dynamics

5 November 2019

cites work

1 reference

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Transport between the cell nucleus and the cytoplasm

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Transport of proteins and RNAs in and out of the nucleus

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Nuclear targeting sequences--a consensus?

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A nuclear localization domain in the hnRNP A1 protein

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A novel receptor-mediated nuclear protein import pathway

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The HIV-1 Rev activation domain is a nuclear export signal that accesses an export pathway used by specific cellular RNAs

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CRM1 is an export receptor for leucine-rich nuclear export signals

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CRM1 is responsible for intracellular transport mediated by the nuclear export signal

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Characterization of proteins that interact with the cell-cycle regulatory protein Ran/TC4

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Protein import into nuclei: association and dissociation reactions involving transport substrate, transport factors, and nucleoporins

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Major binding sites for the nuclear import receptor are the internal nucleoporin Nup153 and the adjacent nuclear filament protein Tpr

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RanGTP targets p97 to RanBP2, a filamentous protein localized at the cytoplasmic periphery of the nuclear pore complex

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A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export

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Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region

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Interactions and three-dimensional localization of a group of nuclear pore complex proteins

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Essential role of protein phosphorylation in nuclear transport

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The peptide repeat domain of nucleoporin Nup98 functions as a docking site in transport across the nuclear pore complex

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Intranuclear filaments containing a nuclear pore complex protein.

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A nuclear pore complex protein that contains zinc finger motifs, binds DNA, and faces the nucleoplasm

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Structural analysis of the p62 complex, an assembly of O-linked glycoproteins that localizes near the central gated channel of the nuclear pore complex

21 January 2018

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Two-way trafficking with Ran.

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Regulation of nuclear localization: a key to a door

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Nuclear localization of NF-ATc by a calcineurin-dependent, cyclosporin-sensitive intramolecular interaction

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Nuclear export of NF-ATc enhanced by glycogen synthase kinase-3

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Signal-mediated nuclear transport in proliferating and growth-arrested BALB/c 3T3 cells

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Variations in signal-mediated nuclear transport during the cell cycle in BALB/c 3T3 cells

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Stimulation of nuclear import by simian virus 40-transformed cell extracts is dependent on protein kinase activity

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Phosphorylation of Srp1p, the yeast nuclear localization signal receptor, in vitro and in vivo

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Phosphorylation and glycosylation of nucleoporins

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Analysis of Ran/TC4 function in nuclear protein import

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Molecular and functional characterization of the p62 complex, an assembly of nuclear pore complex glycoproteins

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Identification of NTF2, a cytosolic factor for nuclear import that interacts with nuclear pore complex protein p62

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Nucleocytoplasmic shuttling factors including Ran and CRM1 mediate nuclear export of NFAT In vitro

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Nuclear protein import in permeabilized mammalian cells requires soluble cytoplasmic factors

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RAN/TC4 mutants identify a common requirement for snRNP and protein import into the nucleus

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Rapid targeting of nuclear proteins to the cytoplasm

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Role of kinases and the phosphatase calcineurin in the nuclear shuttling of transcription factor NF-AT4.

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Separate nuclear import pathways converge on the nucleoporin Nup153 and can be dissected with dominant-negative inhibitors

21 January 2018

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