Cellular stress regulates the nucleocytoplasmic distribution of the protein-tyrosine phosphatase TCPTP. (Q42826816)

8 November 2017

Cellular stress regulates the nucleocytoplasmic distribution of the protein-tyrosine phosphatase TCPTP. (English)

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8 November 2017

6

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8 November 2017

Lam MH

1

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8 November 2017

Michell BJ

2

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8 November 2017

Fodero-Tavoletti MT

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8 November 2017

Kemp BE

4

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8 November 2017

Tonks NK

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8 November 2017

language of work or name

English

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publication date

30 July 2001

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Journal of Biological Chemistry

8 November 2017

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8 November 2017

276

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8 November 2017

37700-37707

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8 November 2017

40

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Combinatorial control of the specificity of protein tyrosine phosphatases

8 November 2017

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Protein tyrosine phosphatases in signal transduction.

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Form, function, and regulation of protein tyrosine phosphatases and their involvement in human diseases.

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cDNA isolated from a human T-cell library encodes a member of the protein-tyrosine-phosphatase family

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Expression of a human T-cell protein-tyrosine-phosphatase in baby hamster kidney cells

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The T-cell protein tyrosine phosphatase

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Cloning and characterization of a mouse cDNA encoding a cytoplasmic protein-tyrosine-phosphatase

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Nuclear localization and cell cycle regulation of a murine protein tyrosine phosphatase

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Association of the T-cell protein tyrosine phosphatase with nuclear import factor p97

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COOH-terminal sequence motifs target the T cell protein tyrosine phosphatase to the ER and nucleus

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The protein-tyrosine phosphatase TCPTP regulates epidermal growth factor receptor-mediated and phosphatidylinositol 3-kinase-dependent signaling

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Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase

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Dealing with energy demand: the AMP-activated protein kinase

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Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST.

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Differential transcriptional activation by Oct-1 and Oct-2: interdependent activation domains induce Oct-2 phosphorylation

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The hnRNP C proteins contain a nuclear retention sequence that can override nuclear export signals

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Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm

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Role of MEKK1 in cell survival and activation of JNK and ERK pathways defined by targeted gene disruption

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Evidence for a role of CRM1 in signal-mediated nuclear protein export

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

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Exportin 1 (Crm1p) is an essential nuclear export factor

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

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Nuclear export receptors: from importin to exportin

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Leptomycin B inhibition of signal-mediated nuclear export by direct binding to CRM1

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Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region

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Nucleocytoplasmic transport: the last 200 nanometers

21 January 2018

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Nucleocytoplasmic transport: signals, mechanisms and regulation

21 January 2018

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

21 January 2018

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

21 January 2018

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5-aminoimidazole-4-carboxamide ribonucleoside. A specific method for activating AMP-activated protein kinase in intact cells?

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1 reference

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Ultraviolet light and osmotic stress: activation of the JNK cascade through multiple growth factor and cytokine receptors

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Alterations in HIV-1 Rev transport in response to cell stress

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Nuclear targeting signal recognition: a key control point in nuclear transport?

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Importin beta, transportin, RanBP5 and RanBP7 mediate nuclear import of ribosomal proteins in mammalian cells

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Importin beta recognizes parathyroid hormone-related protein with high affinity and mediates its nuclear import in the absence of importin alpha

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The importin beta/importin 7 heterodimer is a functional nuclear import receptor for histone H1.

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Karyopherins and kissing cousins.

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Evidence that AMP triggers phosphorylation as well as direct allosteric activation of rat liver AMP-activated protein kinase. A sensitive mechanism to protect the cell against ATP depletion

21 January 2018

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Identifiers

DOI

10.1074/JBC.M105128200

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release_c2qu357qsjcufakfqxnixonorq

8 November 2017

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Fatcat

https://api.fatcat.wiki/v0/release/c2qu357qsjcufakfqxnixonorq

mapped directly with Wikidata item

24 November 2022

based on heuristic

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