Publications
325 results found
Lallemand-Breitenbach V, Zhu J, Puvion F, et al., 2001, Role of promyelocytic leukemia (PML) sumolation in nuclear body formation, 11S proteasome recruitment, and As2O3-induced PML or PML/retinoic acid receptor alpha degradation, Journal of Experimental Medicine, Vol: 193, Pages: 1361-1371, ISSN: 0022-1007
Promyelocytic leukemia (PML) is the organizer of nuclear matrix domains, PML nuclear bodies (NBs), with a proposed role in apoptosis control. In acute promyelocytic leukemia, PML/retinoic acid receptor (RAR) α expression disrupts NBs, but therapies such as retinoic acid or arsenic trioxide (As2O3) restore them. PML is conjugated by the ubiquitin-related peptide SUMO-1, a process enhanced by As2O3 and proposed to target PML to the nuclear matrix. We demonstrate that As2O3 triggers the proteasome-dependent degradation of PML and PML/RARα and that this process requires a specific sumolation site in PML, K160. PML sumolation is dispensable for its As2O3-induced matrix targeting and formation of primary nuclear aggregates, but is required for the formation of secondary shell-like NBs. Interestingly, only these mature NBs harbor 11S proteasome components, which are further recruited upon As2O3 exposure. Proteasome recruitment by sumolated PML only likely accounts for the failure of PML-K160R to be degraded. Therefore, studying the basis of As2O3-induced PML/RARα degradation we show that PML sumolation directly or indirectly promotes its catabolism, suggesting that mature NBs could be sites of intranuclear proteolysis and opening new insights into NB alterations found in viral infections or transformation.
Dulic A, Bates PA, Zhang XD, et al., 2001, BRCT domain interactions in the heterodimeric DNA repair protein XRCC1-DNA ligase III, BIOCHEMISTRY, Vol: 40, Pages: 5906-5913, ISSN: 0006-2960
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- Citations: 55
Freemont PS, 2000, Ubiquitination: RING for destruction?, Current Biology, Vol: 10, ISSN: 0960-9822
Ubiquitination targets proteins for degradation and is a potent regulator of cellular protein function. Recent results implicate the RING finger domain in specific Ubiquitination events; it is possible that all RING proteins act as E3 ubiquitin protein ligases, with implications for a variety of biological areas. © 2000 Elsevier Science Ltd. All rights reserved.
Zhang XD, Shaw A, Bates PA, et al., 2000, Structure of the AAA ATPase p97, MOLECULAR CELL, Vol: 6, Pages: 1473-1484, ISSN: 1097-2765
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- Citations: 363
Linder B, Newman R, Jones LK, et al., 2000, Biochemical analyses of the AF10 protein: The extended LAP/PHD-finger mediates oligomerisation (vol 299, pg 369, 2000), JOURNAL OF MOLECULAR BIOLOGY, Vol: 302, Pages: 523-523, ISSN: 0022-2836
Bárdos JI, Saurin AJ, Tissot C, et al., 2000, HPC3 is a new human polycomb orthologue that interacts and associates with RING1 and Bmi1 and Has transcriptional repression properties, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 275, Pages: 28785-28792, ISSN: 0021-9258
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- Citations: 63
Huyton T, Bates PA, Zhang XD, et al., 2000, The BRCA1 C-terminal domain: structure and function, MUTATION RESEARCH-DNA REPAIR, Vol: 460, Pages: 319-332, ISSN: 0921-8777
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- Citations: 126
Linder B, Newman R, Jones LK, et al., 2000, Biochemical analyses of the AF10 protein: The extended LAP/PHD-finger mediates oligomerisation, JOURNAL OF MOLECULAR BIOLOGY, Vol: 299, Pages: 369-378, ISSN: 0022-2836
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- Citations: 64
Rothwell DG, Hang B, Gorman MA, et al., 2000, Substitution of Asp-210 in HAP1 (APE/Ref-1) eliminates endonuclease activity but stabilises substrate binding, NUCLEIC ACIDS RESEARCH, Vol: 28, Pages: 2207-2213, ISSN: 0305-1048
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- Citations: 53
Zhong S, Müller S, Ronchetti S, et al., 2000, Role of SUMO-1-modified PML in nuclear body formation, BLOOD, Vol: 95, Pages: 2748-2753, ISSN: 0006-4971
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- Citations: 461
Freemont PS, 2000, RING for destruction?, Curr Biol, Vol: 10, Pages: R84-R87, ISSN: 0960-9822
Ubiquitination targets proteins for degradation and is a potent regulator of cellular protein function. Recent results implicate the RING finger domain in specific ubiquitination events; it is possible that all RING proteins act as E3 ubiquitin protein ligases, with implications for a variety of biological areas.
Freemont PS, 2000, Ubiquitination: RING for destruction?, CURRENT BIOLOGY, Vol: 10, Pages: R84-R87, ISSN: 0960-9822
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- Citations: 437
Lariviere L, Rueger W, Freemont P, et al., 2000, β-Glucosyltranferase: Substrate Binding and metal site., Publisher: INT UNION CRYSTALLOGRAPHY, Pages: S242-S242, ISSN: 2053-2733
Zhong S, Müller S, Ronchetti S, et al., 1999, PML is essential for proper formation of the nuclear body., BLOOD, Vol: 94, Pages: 489A-489A, ISSN: 0006-4971
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- Citations: 2
Müller JMM, Rabouille C, Newman R, et al., 1999, An NSF function distinct from ATPase-dependent SNARE disassembly is essential for Golgi membrane fusion, NATURE CELL BIOLOGY, Vol: 1, Pages: 335-340, ISSN: 1465-7392
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- Citations: 54
Moréra S, Imberty A, Aschke-Sonnenborn U, et al., 1999, T4 phage β-glucosyltransferase:: Substrate binding and proposed catalytic mechanism, JOURNAL OF MOLECULAR BIOLOGY, Vol: 292, Pages: 717-730, ISSN: 0022-2836
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- Citations: 99
Imberty A, Monier C, Bettler E, et al., 1999, Fold recognition study of α3-galactosyltransferase and molecular modeling of the nucleotide sugar-binding domain, GLYCOBIOLOGY, Vol: 9, Pages: 713-722, ISSN: 0959-6658
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- Citations: 16
Karow JK, Newman RH, Freemont PS, et al., 1999, Oligomeric ring structure of the Bloom's syndrome helicase, CURRENT BIOLOGY, Vol: 9, Pages: 597-600, ISSN: 0960-9822
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- Citations: 126
Lu PJ, Sundquist K, Baeckstrom D, et al., 1999, A novel gene (<i>PLU-1</i>) containing highly conserved putative DNA chromatin binding motifs is specifically up-regulated in breast cancer, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 274, Pages: 15633-15645, ISSN: 0021-9258
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- Citations: 192
Soulez M, Saurin AJ, Freemont PS, et al., 1999, SSX and the synovial-sarcoma-specific chimaeric protein SYT-SSX co-localize with the human Polycomb group complex, ONCOGENE, Vol: 18, Pages: 2739-2746, ISSN: 0950-9232
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- Citations: 87
Assier E, Bouzinba-Segard H, Stolzenberg MC, et al., 1999, Isolation, sequencing and expression of RED, a novel human gene encoding an acidic-basic dipeptide repeat, GENE, Vol: 230, Pages: 145-154, ISSN: 0378-1119
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- Citations: 29
Allford S, Grimwade D, Langabeer S, et al., 1999, Identification of the t(15;17) in AML FAB types other than M3:: evaluation of the role of molecular screening for the <i>PML/RAR</i>α rearrangement in newly diagnosed AML, BRITISH JOURNAL OF HAEMATOLOGY, Vol: 105, Pages: 198-207, ISSN: 0007-1048
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- Citations: 36
Allford S, Grimwade D, Langabeer S, et al., 1999, Identification of the t(15;17) in AML FAB types other than M3: evaluation of the role of molecular screening for the PML/RARalpha rearrangement in newly diagnosed AML. The Medical Research Council (MRC) Adult Leukaemia Working Party., Br J Haematol, Vol: 105, Pages: 198-207, ISSN: 0007-1048
Acute promyelocytic leukaemia (APL) is characterized by the t(15;17) leading to the formation of PML-RARalpha and RARalpha-PML fusion genes; this rearrangement has been considered both diagnostic for, and restricted to, this subtype of acute myeloid leukaemia (AML FAB M3). We describe two cases of AML with the t(15;17) associated with a PML/RARalpha rearrangement which lacked typical APL morphology, classified as FAB M1 and M2 respectively. In both cases morphological review revealed small populations of cells which exhibited some features associated with APL. In the case classified as M1, PML immunofluorescence studies revealed the classic microparticulate nuclear staining pattern as observed in typical cases of APL with the t(15;17). Similarly, blasts from this case were found to be sensitive to ATRA in vitro as determined by NBT reduction test and by normalization of the PML nuclear body staining pattern. To determine the frequency of PML/RARalpha rearrangements in FAB subtypes other than M3, 530 patients from the MRC AML trials were screened using nested RT-PCR. Only one individual, initially classified as M5 with a normal karyotype, was found to have a PML/RARalpha rearrangement. The diagnosis was revised to M3 variant on subsequent morphological review. In conclusion, this study demonstrates that, in rare cases, the t(15;17) is not restricted to patients with M3 morphology as defined by current FAB criteria. Therefore, although we consider cytogenetic analysis of newly diagnosed cases of AML to be mandatory, our data suggests that routine molecular screening for PML/RARalpha rearrangements is not justified and should be reserved for those cases displaying features which may be suspicious of APL even if such cells comprise only a minority of the total population.
Duprez E, Saurin AJ, Desterro JM, et al., 1999, SUMO-1 modification of the acute promyelocytic leukaemia protein PML:: implications for nuclear localisation, JOURNAL OF CELL SCIENCE, Vol: 112, Pages: 381-393, ISSN: 0021-9533
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- Citations: 262
Lally JM, Dokurno P, Taylor-Papadimitriou J, et al., 1999, CRYSTAL STRUCTURE OF THE SM3 ANTIBODY AGAINST POLYMORPHIC EPITHELIAL MUCIN, Publisher: INT UNION CRYSTALLOGRAPHY, Pages: 351-351, ISSN: 2053-2733
Zhang X, Morera S, Bates PA, et al., 1999, STRUCTURE OF AN XRCC1 BRCT DOMAIN: A NEW PROTEIN PROTEIN INTERACTION MODULE., Publisher: INT UNION CRYSTALLOGRAPHY, Pages: 292-292, ISSN: 2053-2733
Dokurno P, Bates PA, Band HA, et al., 1998, Crystal structure at 1.95 Å resolution of the breast tumour-specific antibody SM3 complexed with its peptide epitope reveals novel hypervariable loop recognition, JOURNAL OF MOLECULAR BIOLOGY, Vol: 284, Pages: 713-728, ISSN: 0022-2836
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- Citations: 64
Bates PA, Dokurno P, Freemont PS, et al., 1998, Conformational analysis of the first observed non-proline <i>cis</i>-peptide bond occurring within the complementarity determining region (CDR) of an antibody, JOURNAL OF MOLECULAR BIOLOGY, Vol: 284, Pages: 549-555, ISSN: 0022-2836
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- Citations: 22
Zhang XD, Moréra S, Bates PA, et al., 1998, Structure of an XRCC1 BRCT domain:: a new protein-protein interaction module, EMBO JOURNAL, Vol: 17, Pages: 6404-6411, ISSN: 0261-4189
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- Citations: 208
Hodges M, Tissot C, Freemont PS, 1998, Protein regulation: Tag wrestling with relatives of ubiquitin, CURRENT BIOLOGY, Vol: 8, Pages: R749-R752, ISSN: 0960-9822
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- Citations: 32
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