RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1 (Q24321958)

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English	RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1	scientific article

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RBBP6 interacts with multifunctional protein YB-1 through its RING finger domain, leading to ubiquitination and proteosomal degradation of YB-1 (English)

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RB binding protein 6, ubiquitin ligase

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GOA release 2020-03-11

ubiquitin-dependent protein catabolic process

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GOA release 2020-03-11

protein ubiquitination

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based on heuristic

inferred from title

object named as

Mervin Meyer

2

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object named as

D Jasper G Rees

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author name string

Moredreck Chibi

1

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Amanda Skepu

3

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Johanna C Moolman-Smook

5

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David J R Pugh

6

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language of work or name

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publication date

26 December 2008

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Journal of Molecular Biology

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384

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4

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908-16

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The pleiotropic functions of the Y-box-binding protein, YB-1.

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Functional potential of P2P-R: a role in the cell cycle and cell differentiation related to its interactions with proteins that bind to matrix associated regions of DNA?

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P2P-R protein localizes to the nucleolus of interphase cells and the periphery of chromosomes in mitotic cells which show maximum P2P-R immunoreactivity

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P2P-R protein overexpression restricts mitotic progression at prometaphase and promotes mitotic apoptosis

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cDNA sequence and chromosomal localization of a novel human protein, RBQ-1 (RBBP6), that binds to the retinoblastoma gene product

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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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Preclinical studies of molecular-targeting diagnostic and therapeutic strategies against breast cancer

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Proteasomal degradation of the multifunctional regulator YB-1 is mediated by an F-Box protein induced during programmed cell death

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PACT: cloning and characterization of a cellular p53 binding protein that interacts with Rb

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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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Y-box factor YB1 controls p53 apoptotic function

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PACT is a negative regulator of p53 and essential for cell growth and embryonic development

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Structure and cell cycle-regulated transcription of the human cyclin A gene

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The proliferation potential protein-related (P2P-R) gene with domains encoding heterogeneous nuclear ribonucleoprotein association and Rb1 binding shows repressed expression during terminal differentiation

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Splicing factor SRp30c interaction with Y-box protein-1 confers nuclear YB-1 shuttling and alternative splice site selection

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

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BTB domain-containing speckle-type POZ protein (SPOP) serves as an adaptor of Daxx for ubiquitination by Cul3-based ubiquitin ligase.

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Polysome-bound endonuclease PMR1 is targeted to stress granules via stress-specific binding to TIA-1.

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DWNN, a novel ubiquitin-like domain, implicates RBBP6 in mRNA processing and ubiquitin-like pathways.

1 reference

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10.1016/J.JMB.2008.09.060

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