BS69 negatively regulates the canonical NF-kappaB activation induced by Epstein-Barr virus-derived LMP1 (Q24317586)

1

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Yuichi Sekine

2

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Akihiro Mizushima

3

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Kenji Oritani

4

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Teruhito Yasui

5

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Masahiro Fujimuro

6

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Ryuta Muromoto

7

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Tadashi Matsuda

Epstein-Barr virus latent membrane protein 1: structure and functions

9

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language of work or name

English

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publication date

19 May 2009

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published in

FEBS Letters

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volume

583

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issue

10

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page(s)

1567-74

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cites work

1 reference

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Tumor necrosis factor receptor associated factor 2 is a mediator of NF-kappa B activation by latent infection membrane protein 1, the Epstein-Barr virus transforming protein

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The Epstein-Barr virus transforming protein LMP1 engages signaling proteins for the tumor necrosis factor receptor family

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The Epstein-Barr virus oncogene product latent membrane protein 1 engages the tumor necrosis factor receptor-associated death domain protein to mediate B lymphocyte growth transformation and activate NF-kappaB

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BS69, a specific adaptor in the latent membrane protein 1-mediated c-Jun N-terminal kinase pathway

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Epstein-Barr virus latent infection membrane protein 1 TRAF-binding site induces NIK/IKK alpha-dependent noncanonical NF-kappaB activation

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Activation of the p38 mitogen-activated protein kinase pathway by Epstein-Barr virus-encoded latent membrane protein 1 coregulates interleukin-6 and interleukin-8 production

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Activation of the cJun N-terminal kinase (JNK) pathway by the Epstein-Barr virus-encoded latent membrane protein 1 (LMP1).

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BRAM1, a BMP receptor-associated molecule involved in BMP signalling

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STAP-2 negatively regulates both canonical and noncanonical NF-kappaB activation induced by Epstein-Barr virus-derived latent membrane protein 1.

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Cross-talk between transforming growth factor-beta and estrogen receptor signaling through Smad3.

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Negative regulation of Epstein-Barr virus latent membrane protein 1-mediated functions by the bone morphogenetic protein receptor IA-binding protein, BRAM1.

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The human papillomavirus type 16 E7 gene encodes transactivation and transformation functions similar to those of adenovirus E1A.

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BS69, an adenovirus E1A-associated protein, inhibits the transcriptional activity of c-Myb

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B-myb rescues ras-induced premature senescence, which requires its transactivation domain

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Binding of EMSY to HP1beta: implications for recruitment of HP1beta and BS69

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The adenovirus E1A binding protein BS69 is a corepressor of transcription through recruitment of N-CoR

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New insights into BS69 functions

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The conserved Mynd domain of BS69 binds cellular and oncoviral proteins through a common PXLXP motif

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Localization of the major NF-kappaB-activating site and the sole TRAF3 binding site of LMP-1 defines two distinct signaling motifs

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Orientation and patching of the latent infection membrane protein encoded by Epstein-Barr virus

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Association of TRAF1, TRAF2, and TRAF3 with an Epstein-Barr virus LMP1 domain important for B-lymphocyte transformation: role in NF-kappaB activation

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The Epstein-Barr virus oncoprotein latent membrane protein 1 engages the tumor necrosis factor receptor-associated proteins TRADD and receptor-interacting protein (RIP) but does not induce apoptosis or require RIP for NF-kappaB activation

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Modulation of TLR4 signaling by a novel adaptor protein signal-transducing adaptor protein-2 in macrophages

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7 January 2021