The Ste20-like kinase SLK is required for ErbB2-driven breast cancer cell motility. - Wikidata - awgldk - TriplyDB

The Ste20-like kinase SLK is required for ErbB2-driven breast cancer cell motility.

The Ste20-like kinase SLK is required for ErbB2-driven breast cancer cell motility.

http://www.wikidata.org/entity/Q39838037

about

SLK-mediated phosphorylation of paxillin is required for focal adhesion turnover and cell migration Regulation of the Ste20-like kinase, SLK: involvement of activation segment phosphorylation SLK/LOSK kinase regulates cell motility independently of microtubule organization and Golgi polarization Ste20-like protein kinase SLK (LOSK) regulates microtubule organization by targeting dynactin to the centrosome Breast cancer metastasis driven by ErbB2 and 14-3-3zeta: A division of labor.Loss of the multifunctional RNA-binding protein RBM47 as a source of selectable metastatic traits in breast cancer.Activation of diverse signalling pathways by oncogenic PIK3CA mutations.Distinct roles for Ste20-like kinase SLK in muscle function and regeneration.Germinal center kinases in immune regulation.Complex changes in alternative pre-mRNA splicing play a central role in the epithelial-to-mesenchymal transition (EMT).Ste20-like kinase SLK, at the crossroads: a matter of life and death The RNA-binding protein Rbfox2: an essential regulator of EMT-driven alternative splicing and a mediator of cellular invasion.A network-based analysis of colon cancer splicing changes reveals a tumorigenesis-favoring regulatory pathway emanating from ELK1 Transforming growth factor β-induced epithelial to mesenchymal transition requires the Ste20-like kinase SLK independently of its catalytic activity.

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P2860

The Ste20-like kinase SLK is required for ErbB2-driven breast cancer cell motility.

http://www.wikidata.org/entity/Q39838037

description

2009 nî lūn-bûn

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2009年の論文

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2009年学术文章

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2009年学术文章

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2009年学术文章

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2009年学术文章

@zh-my

2009年学术文章

@zh-sg

2009年學術文章

@yue

2009年學術文章

@zh

2009年學術文章

@zh-hant

name

The Ste20-like kinase SLK is required for ErbB2-driven breast cancer cell motility.

@en

The Ste20-like kinase SLK is required for ErbB2-driven breast cancer cell motility.

@nl

type

label

The Ste20-like kinase SLK is required for ErbB2-driven breast cancer cell motility.

@en

The Ste20-like kinase SLK is required for ErbB2-driven breast cancer cell motility.

@nl

prefLabel

The Ste20-like kinase SLK is required for ErbB2-driven breast cancer cell motility.

@en

The Ste20-like kinase SLK is required for ErbB2-driven breast cancer cell motility.

@nl

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The Ste20-like kinase SLK is required for ErbB2-driven breast cancer cell motility.

@en

P2093

C J Storbeck

http://www.w3.org/2001/XMLSchema#string

J Chmielecki

http://www.w3.org/2001/XMLSchema#string

J J Northey

http://www.w3.org/2001/XMLSchema#string

K Roovers

http://www.w3.org/2001/XMLSchema#string

L A Sabourin

http://www.w3.org/2001/XMLSchema#string

P M Siegel

http://www.w3.org/2001/XMLSchema#string

P O'Reilly

http://www.w3.org/2001/XMLSchema#string

S Wagner

http://www.w3.org/2001/XMLSchema#string

V Lo

http://www.w3.org/2001/XMLSchema#string

W J Muller

http://www.w3.org/2001/XMLSchema#string

P2860

Integrin-regulated FAK-Src signaling in normal and cancer cells

LOK is a novel mouse STE20-like protein kinase that is expressed predominantly in lymphocytes

Newest findings on the oldest oncogene; how activated src does it

Caspase 3 cleavage of the Ste20-related kinase SLK releases and activates an apoptosis-inducing kinase domain and an actin-disassembling region

Ste20-related protein kinase LOSK (SLK) controls microtubule radial array in interphase.

FAK integrates growth-factor and integrin signals to promote cell migration

mDia mediates Rho-regulated formation and orientation of stable microtubules

Expression of the neu protooncogene in the mammary epithelium of transgenic mice induces metastatic disease.

Distinct tyrosine autophosphorylation sites negatively and positively modulate neu-mediated transformation

FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly

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2839-2848

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scholarly article

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10.1038/ONC.2009.146

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31

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