Biochemical Society Symposia最新文献_第3页

Evolutionarily conserved structural and functional roles of the FYVE domain. 进化上保守的FYVE结构和功能角色。

Biochemical Society Symposia Pub Date : 2007-01-01 DOI: 10.1042/BSS0740095

Akira Hayakawa, Susan Hayes, Deborah Leonard, David Lambright, Silvia Corvera

{"title":"Evolutionarily conserved structural and functional roles of the FYVE domain.","authors":"Akira Hayakawa, Susan Hayes, Deborah Leonard, David Lambright, Silvia Corvera","doi":"10.1042/BSS0740095","DOIUrl":"https://doi.org/10.1042/BSS0740095","url":null,"abstract":"The FYVE domain is an approx. 80 amino acid motif that binds to the phosphoinositide PtdIns3P with high specificity and affinity. It is present in 38 predicted gene products within the human genome, but only in 12-13 in Caenorhabditis elegans and Drosophila melanogaster. Eight of these are highly conserved in all three organisms, and they include proteins that have not been characterized in any species. One of these, WDFY2, appears to play an important role in early endocytosis and was revealed in a RNAi (RNA interference) screen in C. elegans. Interestingly, some proteins contain FYVE-like domains in C. elegans and D. melanogaster, but have lost this domain during evolution. One of these is the homologue of Rabatin-5, a protein that, in mammalian cells, binds both Rab5 and Rabex-5, a guanine-nucleotide exchange factor for Rab5. Thus the Rabatin-5 homologue suggests that mechanisms to link PtdIns3P and Rab5 activation developed in evolution. In mammalian cells, these mechanisms are apparent in the existence of proteins that bind PtdIns3P and Rab GTPases, such as EEA1, Rabenosyn-5 and Rabip4'. Despite the comparable ability to bind to PtdIns3P in vitro, FYVE domains display widely variable abilities to interact with endosomes in intact cells. This variation is due to three distinct properties of FYVE domains conferred by residues that are not involved in PtdIns3P head group recognition: These properties are: (i) the propensity to oligomerize, (ii) the ability to insert into the membrane bilayer, and (iii) differing electrostatic interactions with the bilayer surface. The different binding properties are likely to regulate the extent and duration of the interaction of specific FYVE domain-containing proteins with early endosomes, and thereby their biological function.","PeriodicalId":55383,"journal":{"name":"Biochemical Society Symposia","volume":" 74","pages":"95-105"},"PeriodicalIF":0.0,"publicationDate":"2007-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"26496598","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 34

Understanding the biological significance of diphosphoinositol polyphosphates ('inositol pyrophosphates'). 了解二磷酸肌醇多磷酸(“焦磷酸肌醇”)的生物学意义。

Biochemical Society Symposia Pub Date : 2007-01-01 DOI: 10.1042/BSS0740211

Stephen B Shears

引用次数: 26

The cell biology of inositol lipids and phosphates. Proceedings of the 2006 Biochemical Society Annual Symposium. Birmingham, United Kingdom. March 29-30, 2006. 肌醇脂和磷酸盐的细胞生物学。2006年生化学会年会论文集。伯明翰，英国。2006年3月29-30日。

Biochemical Society Symposia Pub Date : 2007-01-01

引用次数: 0

The p53 response during DNA damage: impact of transcriptional cofactors. DNA损伤中的p53反应：转录辅助因子的影响。

Biochemical Society Symposia Pub Date : 2006-01-01 DOI: 10.1042/bss0730181

Amanda S Coutts, Nicholas La Thangue

引用次数: 0

Nucleosome dynamics. 核小体动力学。

Biochemical Society Symposia Pub Date : 2006-01-01 DOI: 10.1042/bss0730109

Chris Stockdale, Michael Bruno, Helder Ferreira, Elisa Garcia-Wilson, Nicola Wiechens, Maik Engeholm, Andrew Flaus, Tom Owen-Hughes

引用次数: 8

MOZ fusion proteins in acute myeloid leukaemia. 急性髓性白血病中MOZ融合蛋白的研究。

Biochemical Society Symposia Pub Date : 2006-01-01 DOI: 10.1042/bss0730023

Philip J F Troke, Karin B Kindle, Hilary M Collins, David M Heery

{"title":"MOZ fusion proteins in acute myeloid leukaemia.","authors":"Philip J F Troke, Karin B Kindle, Hilary M Collins, David M Heery","doi":"10.1042/bss0730023","DOIUrl":"https://doi.org/10.1042/bss0730023","url":null,"abstract":"MOZ (monocytic leukaemia zinc finger protein; also known as ZNF220 or MYST3) is a member of the MYST family of protein acetyltransferases. Chromosomal translocations involving the MOZ gene are associated with AML (acute myeloid leukaemia), suggesting that it has a role in haematopoiesis. Recurrent reciprocal translocations fuse the MOZ gene [or the gene encoding MORF (MOZ-related factor); also known as MYST4] to genes encoding the nuclear receptor co-activators CBP [CREB (cAMP response element-binding protein)-binding protein], p300 or the p160 protein TIF2 (transcription intermediary factor 2). The resulting fusion proteins can transform haematopoietic progenitors in vitro, and induce myeloproliferative disease in mice. Recent insights into the molecular mechanisms underlying these effects indicate that MOZ fusion proteins interfere with the activities of transcription factors such as nuclear receptors, p53 and Runx proteins. Our studies suggest that subverting the function of cellular CBP and p300 proteins may play a key role in this process. Here we review the recent progress in understanding the role of MOZ fusion proteins in the aetiology of AML.","PeriodicalId":55383,"journal":{"name":"Biochemical Society Symposia","volume":" 73","pages":"23-39"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25983844","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 51

The relationship between higher-order chromatin structure and transcription. 高阶染色质结构与转录的关系。

Biochemical Society Symposia Pub Date : 2006-01-01 DOI: 10.1042/bss0730059

Nick Gilbert, Wendy A Bickmore

引用次数: 13

Activation by c-Myc of transcription by RNA polymerases I, II and III. 通过c-Myc激活RNA聚合酶I, II和III的转录。

Biochemical Society Symposia Pub Date : 2006-01-01 DOI: 10.1042/bss0730141

Natividad Gomez-Roman, Zoë A Felton-Edkins, Niall S Kenneth, Sarah J Goodfellow, Dimitris Athineos, Jingxin Zhang, Ben A Ramsbottom, Fiona Innes, Theodoros Kantidakis, Elaine R Kerr, Jacqueline Brodie, Carla Grandori, Robert J White

{"title":"Activation by c-Myc of transcription by RNA polymerases I, II and III.","authors":"Natividad Gomez-Roman, Zoë A Felton-Edkins, Niall S Kenneth, Sarah J Goodfellow, Dimitris Athineos, Jingxin Zhang, Ben A Ramsbottom, Fiona Innes, Theodoros Kantidakis, Elaine R Kerr, Jacqueline Brodie, Carla Grandori, Robert J White","doi":"10.1042/bss0730141","DOIUrl":"https://doi.org/10.1042/bss0730141","url":null,"abstract":"The proto-oncogene product c-Myc can induce cell growth and proliferation. It regulates a large number of RNA polymerase II-transcribed genes, many of which encode ribosomal proteins, translation factors and other components of the biosynthetic apparatus. We have found that c-Myc can also activate transcription by RNA polymerases I and III, thereby stimulating production of rRNA and tRNA. As such, c-Myc may possess the unprecedented capacity to induce expression of all ribosomal components. This may explain its potent ability to drive cell growth, which depends on the accumulation of ribosomes. The activation of RNA polymerase II transcription by c-Myc is often inefficient, but its induction of rRNA and tRNA genes can be very strong in comparison. We will describe what is known about the mechanisms used by c-Myc to activate transcription by RNA polymerases I and II.","PeriodicalId":55383,"journal":{"name":"Biochemical Society Symposia","volume":" 73","pages":"141-54"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1042/bss0730141","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25983212","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 89

Convergence of the SUMO and MAPK pathways on the ETS-domain transcription factor Elk-1. ets结构域转录因子Elk-1上SUMO和MAPK通路的收敛。

Biochemical Society Symposia Pub Date : 2006-01-01 DOI: 10.1042/bss0730121

Shen-Hsi Yang, Andrew D Sharrocks

引用次数: 49

Fluorescence resonance energy transfer as a method for dissecting in vivo mechanisms of transcriptional activation. 荧光共振能量转移作为解剖体内转录激活机制的一种方法。

Biochemical Society Symposia Pub Date : 2006-01-01

Sara K Evans, David P Aiello, Michael R Green

{"title":"Fluorescence resonance energy transfer as a method for dissecting in vivo mechanisms of transcriptional activation.","authors":"Sara K Evans, David P Aiello, Michael R Green","doi":"","DOIUrl":"","url":null,"abstract":"The first step in transcriptional activation of protein-coding genes involves the assembly on the promoter of a large PIC (pre-initiation complex) comprising RNA polymerase II and a suite of general transcription factors. Transcription is greatly enhanced by the action of promoter-specific activator proteins (activators) that function, at least in part, by increasing PIC formation. Activator-mediated stimulation of PIC assembly is thought to result from a direct interaction between the activator and one or more components of the transcription machinery, termed the 'target'. The unambiguous identification of direct, physiologically relevant in vivo targets of activators has been a considerable challenge in the transcription field. The major obstacle has been the lack appropriate experimental methods to measure direct interactions with activators in vivo. The development of spectral variants of green fluorescent protein has made it possible to perform FRET (fluorescence resonance energy transfer) analysis in living cells, thereby allowing the detection of direct protein-protein interactions in vivo. Here we discuss how FRET can be used to identify activator targets and to dissect in vivo mechanisms of transcriptional activation.","PeriodicalId":55383,"journal":{"name":"Biochemical Society Symposia","volume":" 73","pages":"217-24"},"PeriodicalIF":0.0,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"25983703","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0