Protein phosphatase 1 interacts with p53BP2, a protein which binds to the tumour suppressor p53 (Q28272482)

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H M Barker

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S J Elledge

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P T Cohen

Cancer. p53, guardian of the genome

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language of work or name

English

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publication date

27 December 1995

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published in

FEBS Letters

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volume

377

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issue

3

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page(s)

295-300

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cites work

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Mutation of the casein kinase II phosphorylation site abolishes the anti-proliferative activity of p53.

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Two distinct signaling pathways activate the latent DNA binding function of p53 in a casein kinase II-independent manner.

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On target with a new mechanism for the regulation of protein phosphorylation

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Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1M.

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The structure and regulation of protein phosphatases

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Mitotic regulation of protein phosphatases by the fission yeast sds22 protein.

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Interaction of the ribosomal protein, L5, with protein phosphatase type 1

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Cloning of the complete coding region for human protein phosphatase inhibitor 2 using the two hybrid system and expression of inhibitor 2 in E. coli

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Sequence of human protein serine/threonine phosphatase 1 gamma and localization of the gene (PPP1CC) encoding it to chromosome bands 12q24.1-q24.2.

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Inhibitor-2 functions like a chaperone to fold three expressed isoforms of mammalian protein phosphatase-1 into a conformation with the specificity and regulatory properties of the native enzyme.

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Regulation of the specific DNA binding function of p53

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The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit

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Distinct residues of human p53 implicated in binding to DNA, simian virus 40 large T antigen, 53BP1, and 53BP2.

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