Hikeshi, a nuclear import carrier for Hsp70s, protects cells from heat shock-induced nuclear damage (Q24317693)

nuclear import signal receptor activity

GOA release 2020-03-11

1 reference

Hsp70 accelerates the recovery of nucleolar morphology after heat shock.

GOA release 2020-03-11

author name string

Shingo Kose

series ordinal

1

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Maiko Furuta

series ordinal

2

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Naoko Imamoto

series ordinal

3

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language of work or name

English

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publication date

27 April 2012

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published in

Cell

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volume

149

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issue

3

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page(s)

578-89

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cites work

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Evidence for the existence of a novel mechanism for the nuclear import of Hsc70

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hsp70: nuclear concentration during environmental stress and cytoplasmic storage during recovery.

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The heat shock response: life on the verge of death

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Transcriptional regulation of the metazoan stress protein response

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Regulating access to the genome: nucleocytoplasmic transport throughout the cell cycle

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Import and export of the nuclear protein import receptor transportin by a mechanism independent of GTP hydrolysis

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Analysis of a RanGTP-regulated gradient in mitotic somatic cells

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Molecular mechanism of the nuclear protein import cycle

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The nuclear pore complex: bridging nuclear transport and gene regulation

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The HSP70 chaperone machinery: J proteins as drivers of functional specificity

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Phosphoproteomics reveals new ERK MAP kinase targets and links ERK to nucleoporin-mediated nuclear transport

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Multiple mechanisms promote the inhibition of classical nuclear import upon exposure to severe oxidative stress

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Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded

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The direction of transport through the nuclear pore can be inverted

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Hsp70 and Hsp40 chaperone activities in the cytoplasm and the nucleus of mammalian cells

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beta-subunit of nuclear pore-targeting complex (importin-beta) can be exported from the nucleus in a Ran-independent manner

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Discovering novel interactions at the nuclear pore complex using bead halo: a rapid method for detecting molecular interactions of high and low affinity at equilibrium

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Ran-unassisted nuclear migration of a 97-kD component of nuclear pore-targeting complex

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Hydrogen peroxide inhibition of nuclear protein import is mediated by the mitogen-activated protein kinase, ERK2.

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Cellular stresses induce the nuclear accumulation of importin alpha and cause a conventional nuclear import block

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Hyperosmotic stress signaling to the nucleus disrupts the Ran gradient and the production of RanGTP

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The permeability barrier of nuclear pore complexes appears to operate via hydrophobic exclusion

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Molecular chaperones as HSF1-specific transcriptional repressors

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Heat-shock induced nuclear retention and recycling inhibition of importin alpha

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Transport between the cell nucleus and the cytoplasm

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Dissecting the signaling events that impact classical nuclear import and target nuclear transport factors

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l7Rn6 encodes a novel protein required for clara cell function in mouse lung development

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Genomic analysis of the Opi- phenotype

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