Positive regulation of IkappaB kinase signaling by protein serine/threonine phosphatase 2A (Q24318289)

1

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Robert S Carter

2

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Kevin N Pennington

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Rey J Gomez

4

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Laura E Sanders

5

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Joan M Llanes

6

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Wasif N Khan

7

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Dean W Ballard

8

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Brian E Wadzinski

Journal of Biological Chemistry

9

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language of work or name

English

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publication date

28 October 2005

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published in

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volume

280

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page(s)

35974-82

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issue

43

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cites work

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IKK-gamma is an essential regulatory subunit of the IkappaB kinase complex

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Complementation cloning of NEMO, a component of the IkappaB kinase complex essential for NF-kappaB activation

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Type 2A protein phosphatase, the complex regulator of numerous signaling pathways

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Protein serine/threonine phosphatase 1 and 2A associate with and dephosphorylate neurofilaments.

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An anchoring factor targets protein phosphatase 2A to brain microtubules

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Protein phosphatase 2A interacts with and directly dephosphorylates RelA

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Three-dimensional structure of the catalytic subunit of protein serine/threonine phosphatase-1

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The IKK NF-kappa B system: a treasure trove for drug development

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Tetrameric oligomerization of IkappaB kinase gamma (IKKgamma) is obligatory for IKK complex activity and NF-kappaB activation

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21 January 2018

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

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7 January 2021

Activation of NF-kappa B by phosphatase inhibitors involves the phosphorylation of I kappa B alpha at phosphatase 2A-sensitive sites

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7 January 2021

IKKgamma /NEMO facilitates the recruitment of the IkappaB proteins into the IkappaB kinase complex

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The NF-kappa B activation pathway: a paradigm in information transfer from membrane to nucleus

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Cocaine and antidepressant-sensitive biogenic amine transporters exist in regulated complexes with protein phosphatase 2A.

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