14-3-3-dependent inhibition of the deubiquitinating activity of UBPY and its cancellation in the M phase
- 1 October 2007
- journal article
- Published by Elsevier BV in Experimental Cell Research
- Vol. 313 (16), 3624-3634
- https://doi.org/10.1016/j.yexcr.2007.07.028
Abstract
No abstract availableKeywords
Funding Information
- Kato Memorial Bioscience Foundation
- Ministry of Education, Culture, Sports, Science and Technology (16004686, 17370045, 17570156, 18050011)
This publication has 32 references indexed in Scilit:
- Identification of 14-3-3ε Substrates from Embryonic Murine BrainJournal of Proteome Research, 2006
- Cytokinesis in plant and animal cells: Endosomes ‘shut the door’Developmental Biology, 2006
- Regulation of ubiquitin-binding proteins by monoubiquitinationNature, 2006
- Regulation of Epidermal Growth Factor Receptor Down-Regulation by UBPY-mediated Deubiquitination at EndosomesMolecular Biology of the Cell, 2005
- AMSH is an endosome-associated ubiquitin isopeptidaseThe Journal of cell biology, 2004
- Identification of 14‐3‐3ζ as an EGF receptor interacting proteinFEBS Letters, 2004
- A Deubiquitinating Enzyme UBPY Interacts with the Src Homology 3 Domain of Hrs-binding Protein via a Novel Binding Motif PX(V/I)(D/N)RXXKPPublished by Elsevier BV ,2000
- Phosphorylated nitrate reductase from spinach leaves is inhibited by 14-3-3 proteins and activated by fusicoccinCurrent Biology, 1996
- The inhibitor protein of phosphorylated nitrate reductase from spinach (Spinacia oleracea) leaves is a 14‐3‐3 proteinFEBS Letters, 1996
- Interaction of 14-3-3 with Signaling Proteins Is Mediated by the Recognition of PhosphoserineCell, 1996