246 results found
Huyton T, Pye VE, Briggs LC, et al., 2003, The crystal structure of murine p97/VCP at 3.6 angstrom, JOURNAL OF STRUCTURAL BIOLOGY, Vol: 144, Pages: 337-348, ISSN: 1047-8477
Tan K, Shaw AL, Madsen B, et al., 2003, Human PLU-1 has transcriptional repression properties and interacts with the developmental transcription factors BF-1 and PAX9, JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 278, Pages: 20507-20513, ISSN: 0021-9258
Jones B, Jones EL, Bonney SA, et al., 2003, Mutations in a Sar1 GTPase of COPII vesicles are associated with lipid absorption disorders, NATURE GENETICS, Vol: 34, Pages: 29-31, ISSN: 1061-4036
Sternsdorf T, Jensen K, Freemont PS, 2003, SUMO, CURRENT BIOLOGY, Vol: 13, Pages: R258-R259, ISSN: 0960-9822
Beuron F, Flynn TC, Ma JP, et al., 2003, Motions and negative cooperativity between p97 domains revealed by cryo-electron microscopy and quantised elastic deformational model, JOURNAL OF MOLECULAR BIOLOGY, Vol: 327, Pages: 619-629, ISSN: 0022-2836
Uchiyama K, Jokitalo E, Kano F, et al., 2002, VCIP135, a novel essential factor for p97/p47-mediated membrane fusion, is required for Golgi and ER assembly in vivo, Journal of Cell Biology, Vol: 159, Pages: 855-866, ISSN: 0021-9525
NSF and p97 are ATPases required for the heterotypic fusion of transport vesicles with their target membranes and the homotypic fusion of organelles. NSF uses ATP hydrolysis to dissociate NSF/SNAPs/SNAREs complexes, separating the v- and t-SNAREs, which are then primed for subsequent rounds of fusion. In contrast, p97 does not dissociate the p97/p47/SNARE complex even in the presence of ATP. Now we have identified a novel essential factor for p97/p47-mediated membrane fusion, named VCIP135 (valosin-containing protein [VCP][p97]/p47 complex-interacting protein, p135), and show that it binds to the p97/p47/syntaxin5 complex and dissociates it via p97 catalyzed ATP hydrolysis. In living cells, VCIP135 and p47 are shown to function in Golgi and ER assembly.
Hickabottom M, Parker GA, Freemont P, et al., 2002, Two nonconsensus sites in the Epstein-Barr virus oncoprotein EBNA3A cooperate to bind the co-repressor carboxyl-terminalbinding protein (CtBP), JOURNAL OF BIOLOGICAL CHEMISTRY, Vol: 277, Pages: 47197-47204, ISSN: 0021-9258
Madsen B, Spencer-Dene B, Poulsom R, et al., 2002, Characterisation and developmental expression of mouse Plu-1, a homologue of a human nuclear protein (PLU-1) which is specifically up-regulated in breast cancer, MECHANISMS OF DEVELOPMENT, Vol: 119, Pages: S239-S246, ISSN: 0925-4773
Madsen B, Spencer-Dene B, Poulsom R, et al., 2002, Characterisation and developmental expression of mouse Plu-1, a homologue of a human nuclear protein (PLU-1) which is specifically up-regulated in breast cancer., Gene Expr Patterns, Vol: 2, Pages: 275-282, ISSN: 1567-133X
PLU-1 is a novel breast cancer associated nuclear protein containing highly conserved domains including the PLU domain, putative DNA/chromatin binding motifs, and PHD/LAP domains. Here we report the cloning of the mouse homologue (Plu-1), and document its expression in adult tissues, mammary tumours and the embryo. The overall homology with human PLU-1 is 94% at the protein level, with almost 100% identity in the conserved domains, suggesting functional conservation. As with human PLU-1 the expression of Plu-1 in adult tissues is restricted, with high expression being seen only in testis, while expression in mammary tumours from c-neu transgenic mice is high. Plu-1 is also differentially expressed in the adult mammary gland. In the developing embryo Plu-1 is expressed in a temporally restricted fashion with tissue specific expression being limited to parts of the developing brain, whisker follicle, mammary bud, thymus, limbs, intervertebral disc, olfactory epithelium, teeth, eye, and stomach. The temporal and spatial expression patterns of the transcription factors Bf-1 and Pax9, recently found to bind to PLU-1 through the PLU domain overlap with Plu-1 expression during development. Thus Plu-1 appears to play an important role in mouse embryonic development which may involve interaction with Pax9 and Bf-1.
Zhang XD, Beuron F, Freemont PS, 2002, Machinery of protein folding and unfolding, CURRENT OPINION IN STRUCTURAL BIOLOGY, Vol: 12, Pages: 231-238, ISSN: 0959-440X
Shiels C, Islam SA, Vatcheva R, et al., 2001, PML bodies associate specifically with the MHC gene cluster in interphase nuclei, Journal of Cell Science, Vol: 114, Pages: 3705-3716, ISSN: 0021-9533
Promyelocytic leukemia (PML) bodies are nuclear multiprotein domains. The observations that viruses transcribe their genomes adjacent to PML bodies and that nascent RNA accumulates at their periphery suggest that PML bodies function in transcription. We have used immuno-FISH in primary human fibroblasts to determine the 3D spatial organisation of gene-rich and gene-poor chromosomal regions relative to PML bodies. We find a highly non-random association of the gene-rich major histocompatibility complex (MHC) on chromosome 6 with PML bodies. This association is specific for the centromeric end of the MHC and extends over a genomic region of at least 1.6 megabases. We also show that PML association is maintained when a subsection of this region is integrated into another chromosomal location. This is the first demonstration that PML bodies have specific chromosomal associations and supports a model for PML bodies as part of a functional nuclear compartment.
Jensen K, Shiels C, Freemont PS, 2001, PML protein isoforms and the RBCC/TRIM motif, ONCOGENE, Vol: 20, Pages: 7223-7233, ISSN: 0950-9232
Shiels C, Islam SA, Vatcheva R, et al., 2001, PML bodies associate specifically with the MHC gene cluster in interphase nuclei, JOURNAL OF CELL SCIENCE, Vol: 114, Pages: 3705-3716, ISSN: 0021-9533
Morera S, Lariviere L, Kurzeck J, et al., 2001, High resolution crystal structures of T4 phage beta-glucosyltransferase: Induced fit and effect of substrate and metal binding, JOURNAL OF MOLECULAR BIOLOGY, Vol: 311, Pages: 569-577, ISSN: 0022-2836
Yuan XM, Shaw A, Zhang XD, et al., 2001, Solution structure and interaction surface of the C-terminal domain from p47: A major p97-cofactor involved in SNARE disassembly, JOURNAL OF MOLECULAR BIOLOGY, Vol: 311, Pages: 255-263, ISSN: 0022-2836
Wu PJ, Bardos JI, Sheer D, et al., 2001, Expression and association of the human trithorax and polycomb group of proteins, BRITISH JOURNAL OF CANCER, Vol: 85, Pages: 109-109, ISSN: 0007-0920
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
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.
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
Bardos 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
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
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
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
Zhong S, Muller 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
Freemont PS, 2000, Ubiquitination: RING for destruction?, CURRENT BIOLOGY, Vol: 10, Pages: R84-R87, ISSN: 0960-9822
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.
Zhong S, Muller 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
Muller 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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