PP2A regulates BCL-2 phosphorylation and proteasome-mediated degradation at the endoplasmic reticulum (Q24337674)

Protein phosphatase 2 regulatory subunit B'gamma

1 reference

proteasome-mediated ubiquitin-dependent protein catabolic process

1 reference

Protein phosphatase 2, regulatory subunit A, alpha

1 reference

B cell leukemia/lymphoma 2

1 reference

Protein phosphatase 2 (formerly 2A), catalytic subunit, beta isoform

1 reference

Protein phosphatase 3, catalytic subunit, alpha isoform

1 reference

Protein phosphatase 2 (formerly 2A), catalytic subunit, alpha isoform

1 reference

Protein phosphatase 2, regulatory subunit B', gamma

1 reference

6

William C Hahn

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Stanley J. Korsmeyer

7

object named as

Stanley J Korsmeyer

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author name string

Stephen S Lin

1

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Michael C Bassik

2

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Heikyung Suh

3

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Mari Nishino

4

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Jason D Arroyo

5

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Thomas M Roberts

Journal of Biological Chemistry

8

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language of work or name

English

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publication date

11 August 2006

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published in

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volume

281

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issue

32

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page(s)

23003-12

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cites work

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Life-or-death decisions by the Bcl-2 protein family.

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Cell death: critical control points

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Organelle-specific initiation of cell death pathways

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Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death

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Endoplasmic reticulum localized Bcl-2 prevents apoptosis when redistribution of cytochrome c is a late event

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BAX and BAK regulation of endoplasmic reticulum Ca2 : a control point for apoptosis

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Bcl-2 decreases the free Ca2 concentration within the endoplasmic reticulum

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Bcl-2 functionally interacts with inositol 1,4,5-trisphosphate receptors to regulate calcium release from the ER in response to inositol 1,4,5-trisphosphate.

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Proapoptotic BAX and BAK regulate the type 1 inositol trisphosphate receptor and calcium leak from the endoplasmic reticulum

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Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling

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Identification of a novel regulatory domain in Bcl-X(L) and Bcl-2.

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Inactivation of Bcl-2 by phosphorylation

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Deletion of the loop region of Bcl-2 completely blocks paclitaxel-induced apoptosis

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BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M.

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The phosphorylation status and anti-apoptotic activity of Bcl-2 are regulated by ERK and protein phosphatase 2A on the mitochondria

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Phosphorylation of BCL-2 regulates ER Ca2 homeostasis and apoptosis.

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Creation of human tumour cells with defined genetic elements

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Identification of specific PP2A complexes involved in human cell transformation

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BAD and glucokinase reside in a mitochondrial complex that integrates glycolysis and apoptosis

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Activated Ets2 is required for persistent inflammatory responses in the motheaten viable model

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Bax in murine thymus is a soluble monomeric protein that displays differential detergent-induced conformations

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Suppression of signalling through transcription factor NF-AT by interactions between calcineurin and Bcl-2.

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Reversible phosphorylation of Bcl2 following interleukin 3 or bryostatin 1 is mediated by direct interaction with protein phosphatase 2A

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Dephosphorylation of Bcl-2 by protein phosphatase 2A results in apoptosis resistance

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Delayed embryonic lethality in mice lacking protein phosphatase 2A catalytic subunit Calpha

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A functional role for the B56 alpha-subunit of protein phosphatase 2A in ceramide-mediated regulation of Bcl2 phosphorylation status and function

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Critical role for protein phosphatase 2A heterotrimers in mammalian cell survival.

21 January 2018

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Purification of type 1 protein (serine/threonine) phosphatases by microcystin-Sepharose affinity chromatography

21 January 2018

1 reference

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inferred from DOI database lookup

7 January 2021

based on heuristic

Apoptotic crosstalk between the endoplasmic reticulum and mitochondria controlled by Bcl-2

1 reference

https://api.crossref.org/works/10.1074/JBC.M602648200

inferred from DOI database lookup

7 January 2021

based on heuristic

Ceramide induces Bcl2 dephosphorylation via a mechanism involving mitochondrial PP2A

1 reference

https://api.crossref.org/works/10.1074/JBC.M602648200

inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1074/JBC.M602648200

1 reference

Consolidated OpenCitations Corpus – April 2017

1 reference

Consolidated OpenCitations Corpus – April 2017

PubMed publication ID

16717086

1 reference

Consolidated OpenCitations Corpus – April 2017