Interaction of the tumor suppressor PTEN/MMAC with a PDZ domain of MAGI3, a novel membrane-associated guanylate kinase (Q22253438)

intracellular signal transduction

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

Y Wu

1

Y

Wu

1 reference

28 March 2023

D Dowbenko

2

D

Dowbenko

1 reference

28 March 2023

S Spencer

3

S

Spencer

1 reference

28 March 2023

R Laura

4

R

Laura

1 reference

28 March 2023

J Lee

5

J

Lee

1 reference

28 March 2023

Q Gu

6

Q

Gu

1 reference

28 March 2023

L A Lasky

7

L A

Lasky

1 reference

Journal of Biological Chemistry

28 March 2023

language of work or name

English

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publication date

14 July 2000

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published in

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volume

275

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issue

28

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page(s)

21477-85

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cites work

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Identification of a candidate tumour suppressor gene, MMAC1, at chromosome 10q23.3 that is mutated in multiple advanced cancers

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Growth suppression of glioma cells by PTEN requires a functional phosphatase catalytic domain

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PTEN/MMAC1/TEP1 suppresses the tumorigenicity and induces G1 cell cycle arrest in human glioblastoma cells

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Inhibition of cell migration, spreading, and focal adhesions by tumor suppressor PTEN

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Tumor suppressor PTEN inhibits integrin- and growth factor-mediated mitogen-activated protein (MAP) kinase signaling pathways

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The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate

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The lipid phosphatase activity of PTEN is critical for its tumor supressor function

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Mechanisms and consequences of activation of protein kinase B/Akt

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Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN

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Protein kinase B (PKB/Akt) activity is elevated in glioblastoma cells due to mutation of the tumor suppressor PTEN/MMAC.

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Inactivation of the tumor suppressor PTEN/MMAC1 in advanced human prostate cancer through loss of expression

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The PTEN/MMAC1 tumor suppressor phosphatase functions as a negative regulator of the phosphoinositide 3-kinase/Akt pathway

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Protein-protein interactions: PDZ domain networks

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PDZ proteins organize synaptic signaling pathways

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MAGI-1, a membrane-associated guanylate kinase with a unique arrangement of protein-protein interaction domains

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Atrophin-1, the DRPLA gene product, interacts with two families of WW domain-containing proteins

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A novel multiple PDZ domain-containing molecule interacting with N-methyl-D-aspartate receptors and neuronal cell adhesion proteins

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Organizing a functional junctional complex requires specific domains of the Drosophila MAGUK Discs large

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PTEN and inherited hamartoma-cancer syndromes

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21 January 2018

Identifiers

DOI

10.1074/JBC.M909741199

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