Akt phosphorylates the Y-box binding protein 1 at Ser102 located in the cold shock domain and affects the anchorage-independent growth of breast cancer cells. (Q46418293)

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English	Akt phosphorylates the Y-box binding protein 1 at Ser102 located in the cold shock domain and affects the anchorage-independent growth of breast cancer cells.	scientific article

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10 January 2020

Akt phosphorylates the Y-box binding protein 1 at Ser102 located in the cold shock domain and affects the anchorage-independent growth of breast cancer cells (English)

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10 January 2020

phosphorylation

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Maggie Chon U Cheang

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Catherine J. Pallen

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Kathy D. Miller

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Kathy Miller

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H. Leighton Grimes

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H Leighton Grimes

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Colleen Nelson

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Brent W Sutherland

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Jill Kucab

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Joyce Wu

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10 January 2020

Cathy Lee

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Erika Yorida

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Dmitry Turbin

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Michael Pollak

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Sunil Badve

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David Huntsman

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C Blake-Gilks

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Min Chen

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Sandra E Dunn

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1 June 2005

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4281-4292

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10 January 2020

https://scigraph.springernature.com/pub.10.1038/sj.onc.1208590

0 references

Heregulin induces phosphorylation of BRCA1 through phosphatidylinositol 3-Kinase/AKT in breast cancer cells

1 reference

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7 January 2021

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Y box-binding protein 1 induces resistance to oncogenic transformation by the phosphatidylinositol 3-kinase pathway

1 reference

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Nuclear localization and increased levels of transcription factor YB-1 in primary human breast cancers are associated with intrinsic MDR1 gene expression

1 reference

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7 January 2021

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Ten years of protein kinase B signalling: a hard Akt to follow

1 reference

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7 January 2021

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Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor

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Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase

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Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase

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Interferon-gamma interferes with transforming growth factor-beta signaling through direct interaction of YB-1 with Smad3.

1 reference

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Inhibition of protein kinase B/Akt. implications for cancer therapy

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Y-box factor YB-1 predicts drug resistance and patient outcome in breast cancer independent of clinically relevant tumor biologic factors HER2, uPA and PAI-1.

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YB-1 as a Cell Cycle-regulated Transcription Factor Facilitating Cyclin A and Cyclin B1 Gene Expression

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The solution structure and DNA-binding properties of the cold-shock domain of the human Y-box protein YB-1

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HER2/PI-3K/Akt activation leads to a multidrug resistance in human breast adenocarcinoma cells.

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Nuclear translocation of the Y-box binding protein by ultraviolet irradiation

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Direct control of the Forkhead transcription factor AFX by protein kinase B

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The Y-box-binding protein, YB1, is a potential negative regulator of the p53 tumor suppressor

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Hierarchical clustering analysis of tissue microarray immunostaining data identifies prognostically significant groups of breast carcinoma

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Nuclear expression of Y-box-binding protein-1 correlates with P-glycoprotein and topoisomerase II alpha expression, and with poor prognosis in synovial sarcoma.

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Direct interaction of p53 with the Y-box binding protein, YB-1: a mechanism for regulation of human gene expression

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Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino acids arginine 211 and serine 343

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Enhanced coexpression of YB-1 and DNA topoisomerase II alpha genes in human colorectal carcinomas

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PKB/Akt mediates cell-cycle progression by phosphorylation of p27(Kip1) at threonine 157 and modulation of its cellular localization

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