Identification of Three Major Sentrinization Sites in PML
Tetsu Kamitani,Katsumi Kito,Hung Phi Nguyen,Hiroyoshi Wada,Taeko Fukuda-Kamitani,Edward T.H. Yeh +5 more
TLDR
Sendrinization of PML, in the context of the RING finger and the B1 box, regulates nuclear body formation and it is shown that sentrinized PML-RARα could be restored by overexpression of sentrin, but not by retinoic acid treatment.About:
This article is published in Journal of Biological Chemistry.The article was published on 1998-10-09 and is currently open access. It has received 320 citations till now. The article focuses on the topics: RING finger domain & Ring finger.read more
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The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
TL;DR: It is clear now that degradation of cellular proteins is a highly complex, temporally controlled, and tightly regulated process that plays major roles in a variety of basic pathways during cell life and death as well as in health and disease.
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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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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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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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Deconstructing a Disease: RAR, Its Fusion Partners, and Their Roles in the Pathogenesis of Acute Promyelocytic Leukemia
Ari Melnick,Jonathan D. Licht +1 more
TL;DR: The elucidation of the molecular basis of acute promyelocytic leukemia emerged as a paradigm for the connection between the bench and bedside and it became apparent that APL was, among the forms of acute myeloid leukemia, uniquely sensitive to all
References
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Identification of a receptor for the morphogen retinoic acid.
TL;DR: Analysis of complementary DNA encoding a novel gene product reveals striking similarity to the steroid and thyroid hormone receptors and Binding and transcription activational studies show it to be a receptor for the vitamin A-related morphogen retinoic acid.
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Chromosomal translocation t(15;17) in human acute promyelocytic leukemia fuses RARα with a novel putative transcription factor, PML
Akira Kakizuka,Wilson H. Miller,K. Umesono,K. Umesono,Raymond P. Warrell,Stanley R. Frankel,Vundavalli V. Murty,E. Dmitrovsky,R.M. Evans,R.M. Evans +9 more
TL;DR: Because patients with APL can be induced into remission with high dose RA therapy, it is proposed that the nonliganded PML-RAR protein is a new class of dominant negative oncogene product.
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The PML-RARα fusion mRNA generated by the t(15;17) translocation in acute promyelocytic leukemia encodes a functionally altered RAR
TL;DR: In APL, the t(15;17) translocation generates an RAR mutant that could contribute to leukemogenesis through interference with promyelocytic differentiation, and this gene product contains a novel zinc finger motif common to several DNA-binding proteins.
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A Small Ubiquitin-Related Polypeptide Involved in Targeting RanGAP1 to Nuclear Pore Complex Protein RanBP2
TL;DR: It is found that the mammalian Ran GTPase-activating protein RanGAP1 is highly concentrated at the cytoplasmic periphery of the nuclear pore complex (NPC), where it associates with the 358-kDa Ran-GTP-binding protein RanBP2, indicating that GTP hydrolysis by Ran at Ran BP2 is required for nuclear protein import.
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A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex.
TL;DR: The identification and localization of a novel form of RanGAP1, a nuclear Ras-like GTPase that is required for the bidirectional transport of proteins and ribnucleoproteins across the nuclear pore complex (NPC), was reported.