Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors.
Ding Yen Lin,Yen Sung Huang,Jen Chong Jeng,Hong Yi Kuo,Che Chang Chang,Ting Ting Chao,Chun Chen Ho,Yunching Chen,Tong Ping Lin,Hsin I. Fang,Chih Chang Hung,Ching Shu Suen,Ming-Jing Hwang,Kun Sang Chang,Gerd G. Maul,Hsiu Ming Shih +15 more
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TLDR
It is demonstrated that arsenic trioxide-induced sumoylation of PML correlates with a change of endogenous Daxx partitioning from GR-regulated gene promoter to PODs and a relief of DAXx repression on GR target gene expression, which provides mechanistic insights into DaxX in SUMO-dependent transcriptional control and subnuclear compartmentalization.About:
This article is published in Molecular Cell.The article was published on 2006-11-03 and is currently open access. It has received 421 citations till now. The article focuses on the topics: Death-associated protein 6 & SUMO protein.read more
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Concepts in sumoylation: a decade on
TL;DR: A decade has passed since SUMO was discovered to be a reversible post-translational protein modifier and many enzymes that participate in regulated SUMO-conjugation and -deconjugation pathways have been identified and characterized.
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Sumoylation: A Regulatory Protein Modification in Health and Disease
Annette Flotho,Frauke Melchior +1 more
TL;DR: Basic mechanisms and recent developments in the physiology of sumoylation are highlighted and it is not surprising that disease links are beginning to emerge and that interference withsumoylation is being considered for intervention.
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Structure, dynamics and functions of promyelocytic leukaemia nuclear bodies
TL;DR: The promyelocytic leukaemia tumour suppressor protein epitomizes the PML-nuclear body (PML-NB) and is crucially required for the proper assembly of this macromolecular nuclear structure.
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Compositional Control of Phase-Separated Cellular Bodies
Salman F. Banani,Allyson M. Rice,William B. Peeples,Yuan Lin,Saumya Jain,Roy Parker,Michael K. Rosen +6 more
TL;DR: The data suggest a conceptual framework for considering the composition and control of cellular bodies assembled through heterotypic multivalent interactions, suggesting how their compositions could be controlled by levels of PML SUMOylation or cellular mRNA concentration, respectively.
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PML Nuclear Bodies
TL;DR: PML nuclear bodies are matrix-associated domains that recruit an astonishing variety of seemingly unrelated proteins that are regulated by a specific posttranslational modification, sumoylation.
References
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Protein Modification by SUMO
TL;DR: The current understanding of how SUMO conjugation is controlled, as well as the roles of SUMO in a number of biological processes are discussed.
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SUMO: a history of modification
TL;DR: The diverse effects of SUMO modification are discussed and models proposed to explain SUMO actions.
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Pml Is Critical for Nd10 Formation and Recruits the Pml-Interacting Protein Daxx to This Nuclear Structure When Modified by Sumo-1
Alexander M. Ishov,Alexey G. Sotnikov,Dmitri Negorev,Olga Vladimirova,Norma F Neff,Tetsu Kamitani,Edward T.H. Yeh,Jerome F. Strauss,Gerd G. Maul +8 more
TL;DR: The findings identify the basic requirements for ND10 formation and suggest a dynamic mechanism for protein recruitment to these nuclear domains controlled by the SUMO-1 modification state of PML.
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Conjugation with the ubiquitin‐related modifier SUMO‐1 regulates the partitioning of PML within the nucleus
TL;DR: It is shown that, in APL cells, As2O3 triggers rapid degradation of PML–RARα and provokes the restoration of intact nuclear bodies, suggesting that post‐translational modification by SUMO‐1 may be more generally involved than previously suspected in the targeting of proteins to distinct subcellular structures.
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Structural basis for E2-mediated SUMO conjugation revealed by a complex between ubiquitin-conjugating enzyme Ubc9 and RanGAP1.
TL;DR: In this paper, structural determinants for recognition of consensus SUMO modification sequences found within SUMO-conjugated proteins were found within mammalian Ubc9 and RanGAP1.