Hepatopoietin interacts directly with COP9 signalosome and regulates AP-1 activity (Q28276487)

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Chengrong Lu

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Handong Wei

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Na Wang

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Xiaoxiao Chen

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Lingqiang Zhang

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Yun Zhai

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Yunping Zhu

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Yinglin Lu

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Fuchu He

Identification and characterization of receptor for mammalian hepatopoietin that is homologous to yeast ERV1

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language of work or name

English

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publication date

13 August 2004

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published in

FEBS Letters

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volume

572

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issue

1-3

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page(s)

85-91

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cites work

1 reference

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Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome

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COP9 signalosome revisited: a novel mediator of protein degradation

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COP9 signalosome-specific phosphorylation targets p53 to degradation by the ubiquitin system

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COP9 signalosome-directed c-Jun activation/stabilization is independent of JNK

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Inositol 1,3,4-trisphosphate 5/6-kinase associates with the COP9 signalosome by binding to CSN1

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Protein kinase CK2 and protein kinase D are associated with the COP9 signalosome

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Integrin LFA-1 interacts with the transcriptional co-activator JAB1 to modulate AP-1 activity

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Identification of hepatopoietin dimerization, its interacting regions and alternative splicing of its transcription

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Comparison of human COP9 signalsome and 26S proteasome lid'.

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A new group of conserved coactivators that increase the specificity of AP-1 transcription factors

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Intracellular action of the cytokine MIF to modulate AP-1 activity and the cell cycle through Jab1

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The COP9 complex, a novel multisubunit nuclear regulator involved in light control of a plant developmental switch

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Arabidopsis homologs of a c-Jun coactivator are present both in monomeric form and in the COP9 complex, and their abundance is differentially affected by the pleiotropic cop/det/fus mutations

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The COP9 signalosome: an assembly and maintenance platform for cullin ubiquitin ligases?

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