Characterization of the mUBC9-binding sites required for E2A protein degradation (Q28144956)

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M T Chin

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N E Sibinga

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S L Lee

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E Haber

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M E Lee

Journal of Biological Chemistry

6

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language of work or name

English

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publication date

1 October 1999

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published in

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volume

274

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issue

40

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page(s)

28690-6

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cites work

Regulation of the expression of cyclin-dependent kinase inhibitor p21 by E2A and Id proteins

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The E2A gene product contains two separable and functionally distinct transcription activation domains

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The AD1 transactivation domain of E2A contains a highly conserved helix which is required for its activity in both Saccharomyces cerevisiae and mammalian cells

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A new transcriptional-activation motif restricted to a class of helix-loop-helix proteins is functionally conserved in both yeast and mammalian cells

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The helix-loop-helix gene E2A is required for B cell formation

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Functional replacement of the mouse E2A gene with a human HEB cDNA.

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Interactions between heterologous helix-loop-helix proteins generate complexes that bind specifically to a common DNA sequence

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E2A proteins are required for proper B cell development and initiation of immunoglobulin gene rearrangements

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E2A deficiency leads to abnormalities in alphabeta T-cell development and to rapid development of T-cell lymphomas

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Localization of E2A mRNA expression in developing and adult rat tissues

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The protein Id: a negative regulator of helix-loop-helix DNA binding proteins

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Casein kinase II increases the transcriptional activities of MRF4 and MyoD independently of their direct phosphorylation

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Phosphorylation of E47 as a potential determinant of B-cell-specific activity

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Notch inhibition of E47 supports the existence of a novel signaling pathway

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Degradation of E2A proteins through a ubiquitin-conjugating enzyme, UbcE2A

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The mUBC9 murine ubiquitin conjugating enzyme interacts with the E2A transcription factors

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Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins

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Mammalian ubiquitin-conjugating enzyme Ubc9 interacts with Rad51 recombination protein and localizes in synaptonemal complexes

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Molecular cloning of the cDNA and chromosome localization of the gene for human ubiquitin-conjugating enzyme 9

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Associations of UBE2I with RAD52, UBL1, p53, and RAD51 proteins in a yeast two-hybrid system

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Interaction of the Ubc9 human homologue with c-Jun and with the glucocorticoid receptor

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Association of activating transcription factor 2 (ATF2) with the ubiquitin-conjugating enzyme hUBC9. Implication of the ubiquitin/proteasome pathway in regulation of ATF2 in T cells

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Direct involvement of the ubiquitin-conjugating enzyme Ubc9/Hus5 in the degradation of IkappaBalpha

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E2A-HLF-mediated cell transformation requires both the trans-activation domains of E2A and the leucine zipper dimerization domain of HLF.

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Fusion of the leucine zipper gene HLF to the E2A gene in human acute B-lineage leukemia

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MyoD binds cooperatively to two sites in a target enhancer sequence: occupancy of two sites is required for activation

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An inhibitory domain of E12 transcription factor prevents DNA binding in E12 homodimers but not in E12 heterodimers

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Regulation of hypoxia-inducible factor 1alpha is mediated by an O2-dependent degradation domain via the ubiquitin-proteasome pathway

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The polymyositis-scleroderma autoantigen interacts with the helix-loop-helix proteins E12 and E47

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Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain

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p34Cdc28-mediated control of Cln3 cyclin degradation

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A PEST-like sequence mediates phosphorylation and efficient ubiquitination of yeast uracil permease

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Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway

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Site-specific phosphorylation of IkappaBalpha by a novel ubiquitination-dependent protein kinase activity

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Reduced ubiquitin-dependent degradation of c-Jun after phosphorylation by MAP kinases

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The ubiquitin-like protein Smt3p is activated for conjugation to other proteins by an Aos1p/Uba2p heterodimer

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Ubc9p is the conjugating enzyme for the ubiquitin-like protein Smt3p

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Preferential interaction of sentrin with a ubiquitin-conjugating enzyme, Ubc9.

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Ubch9 conjugates SUMO but not ubiquitin

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The ubiquitin-like proteins SMT3 and SUMO-1 are conjugated by the UBC9 E2 enzyme

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A small ubiquitin-related polypeptide involved in targeting RanGAP1 to nuclear pore complex protein RanBP2

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SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation

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Synthetic signals for ubiquitin-dependent proteolysis

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Crystal structure of murine/human Ubc9 provides insight into the variability of the ubiquitin-conjugating system

21 January 2018

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Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae

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In vivo degradation of a transcriptional regulator: the yeast alpha 2 repressor

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