Research Topics
Genomes and Genes | Laura Trinkle-MulcahySummaryAffiliation: University of Dundee Country: UK Publications
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Publications
Displacement affinity chromatography of protein phosphatase one (PP1) complexesGreg B G Moorhead
Department of Biological Sciences, University of Calgary, 2500 University Dr, NW Calgary, AB T2N 1N4, Canada
BMC Biochem 9:28. 2008..PP1 is localized to its site of action by interacting with targeting or regulatory proteins, a majority of which contains a primary docking site referred to as the RVXF/W motif...
Nuclear organisation of NIPP1, a regulatory subunit of protein phosphatase 1 that associates with pre-mRNA splicing factorsL Trinkle-Mulcahy
Department of Biochemistry, The University, MSI WTB complex, Dow Street, Dundee DD1 5EH, Scotland, UK
J Cell Sci 112:157-68. 1999..These findings implicate the NIPP1-PP1 complex in the control of pre-mRNA splicing...
Nuclear functions in space and time: gene expression in a dynamic, constrained environmentLaura Trinkle-Mulcahy
Centre for Gene Regulation and Expression, MSI WTB complex, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom
FEBS Lett 582:1960-70. 2008..In several cases, as highlighted here, this has turned up surprising results and has forced a re-evaluation of models for nuclear structure and gene regulation...- Toward a high-resolution view of nuclear dynamicsLaura Trinkle-Mulcahy
Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK
Science 318:1402-7. 2007..Here, we review the impact of new technologies, especially in areas of fluorescence microscopy and proteomics, which are providing major insights into dynamic processes affecting both structure and function within the nucleus... - Mitotic phosphatases: no longer silent partnersLaura Trinkle-Mulcahy
Division of Gene Regulation and Expression, School of Life Sciences, University of Dundee, Dow St, Dundee DD1 5EH, UK
Curr Opin Cell Biol 18:623-31. 2006..These exciting advances show that protein phosphatases are not merely silent partners to kinases in regulating the control of cell division... - Repo-Man recruits PP1 gamma to chromatin and is essential for cell viabilityLaura Trinkle-Mulcahy
University of Dundee, Dundee DD1 5EH, Scotland, UK
J Cell Biol 172:679-92. 2006..The data indicate that Repo-Man forms an essential complex with PP1gamma and is required for the recruitment of PP1 to chromatin... - Dynamic targeting of protein phosphatase 1 within the nuclei of living mammalian cellsL Trinkle-Mulcahy
MSI WTB complex, University of Dundee, Dundee DD1 5EH, Scotland
J Cell Sci 114:4219-28. 2001..These data indicate that PP1 isoforms are highly mobile in cells and can be dynamically (re)localized through direct interaction with targeting subunits... - Time-lapse imaging reveals dynamic relocalization of PP1gamma throughout the mammalian cell cycleLaura Trinkle-Mulcahy
Wellcome Trust Biocentre, University of Dundee, Dundee DD1 5EH, United Kingdom
Mol Biol Cell 14:107-17. 2003..The changing spatio-temporal distribution of PP1gamma revealed using the stable PP1 cell lines implicates it in multiple processes, including nucleolar function, the regulation of chromosome segregation and cytokinesis... - Cajal body proteins SMN and Coilin show differential dynamic behaviour in vivoJudith E Sleeman
University of Dundee, MSI WTB complex, School of Life Sciences, Dow Street, Dundee DD1 5EH, UK
J Cell Sci 116:2039-50. 2003..This in vivo study indicates that SMN and coilin interact differentially with Cajal bodies and reveals parallels in the pathway for reassembly of nucleoli and Cajal bodies following mitosis... - FRET analyses of the U2AF complex localize the U2AF35/U2AF65 interaction in vivo and reveal a novel self-interaction of U2AF35Janet Chusainow
Wellcome Trust Biocentre, University of Dundee, Dow Street, Dundee DD1 5EH, UK
RNA 11:1201-14. 2005..The data show that FRET studies offer a valuable approach for probing interactions between pre-mRNA splicing factors in vivo... - Evidence that the tandem-pleckstrin-homology-domain-containing protein TAPP1 interacts with Ptd(3,4)P2 and the multi-PDZ-domain-containing protein MUPP1 in vivoWendy A Kimber
MRC Protein Phosphorylation Unit, MSI WTB complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, UK
Biochem J 361:525-36. 2002.... - Establishment of a protein frequency library and its application in the reliable identification of specific protein interaction partnersSéverine Boulon
The Wellcome Trust Centre for Gene Regulation and Expression, University of Dundee, Dundee DD1 5EH, Scotland, United Kingdom
Mol Cell Proteomics 9:861-79. 2010.... - NOPdb: Nucleolar Proteome DatabaseAnthony Kar Lun Leung
Division of Gene Regulation and Expression, Wellcome Trust Biocentre, School of Life Sciences, University of Dundee, Dundee DD1 5EH, UK
Nucleic Acids Res 34:D218-20. 2006..g. LocusLink, OMIM and PubMed)... - Alternative splicing regulates the production of ARD-1 endoribonuclease and NIPP-1, an inhibitor of protein phosphatase-1, as isoforms encoded by the same geneA C Chang
MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee, UK
Gene 240:45-55. 1999..Our results establish the process by which functionally disparate ARD-1 and NIPP-1 peptides are generated from the protein-coding sequence of the same gene in human cells... - Identifying specific protein interaction partners using quantitative mass spectrometry and bead proteomesLaura Trinkle-Mulcahy
Wellcome Trust Centre for Gene Regulation and Expression, University of Dundee, Dundee, Scotland, UK
J Cell Biol 183:223-39. 2008..These data provide a specificity filter to distinguish specific protein binding partners in both quantitative and nonquantitative pull-down and immunoprecipitation experiments... - Visualization of intracellular PP1 targeting through transiently and stably expressed fluorescent protein fusionsLaura Trinkle Mulcahy
Division of Gene Regulation and Expression, School of Life Sciences, MSI WTB complex, University of Dundee, UK
Methods Mol Biol 365:133-54. 2007..Interactions with targeting subunits can be visualized in vivo by fluorescence resonance energy transfer (FRET), using techniques such as sensitized emission, acceptor photobleaching, or fluorescence lifetime imaging... - Characterization of a novel phosphatidylinositol 3-phosphate-binding protein containing two FYVE fingers in tandem that is targeted to the GolgiP C Cheung
MRC Protein Phosphorylation Unit, MSI WTB complex, University of Dundee, Dow Street, Dundee DD1 5EH, Scotland, U K
Biochem J 355:113-21. 2001..Cell localization studies using a green fluorescent protein fusion show that TAFF1 is localized to the Golgi, and that the Golgi targeting sequence is located within the N-terminal 187 residues and not in either FYVE domain... - The nucleolusYun Wah Lam
Wellcome Trust Biocentre, MSI/WTB Complex, University of Dundee, Dundee, DD1 5EH, UK
J Cell Sci 118:1335-7. 2005 - Condensin and Repo-Man-PP1 co-operate in the regulation of chromosome architecture during mitosisPaola Vagnarelli
Wellcome Trust Centre for Cell Biology, Institute of Cell Biology, University of Edinburgh, Swann Building, King s Buildings, Mayfield Road, Edinburgh EH9 3JR, UK
Nat Cell Biol 8:1133-42. 2006..This activity, provisionally termed 'regulator of chromosome architecture' (RCA), cooperates with condensin to preserve the characteristic chromosome architecture during mitosis... - Emerging roles of nuclear protein phosphatasesGreg B G Moorhead
Department of Biological Sciences, University of Calgary, 2500 University Drive NW, Calgary Alberta, Canada T2N 1N4
Nat Rev Mol Cell Biol 8:234-44. 2007.... - The nuclear PP1 interacting protein ZAP3 (ZAP) is a putative nucleoside kinase that complexes with SAM68, CIA, NF110/45, and HNRNP-GAnnegret Ulke-Lemee
Department of Biological Sciences, University of Calgary, 2500 University Drive NW, Calgary, Alberta, Canada
Biochim Biophys Acta 1774:1339-50. 2007..In ZAP3, although this domain is present, it now appears degenerate and functions to bind PP1 through an RVRW docking site located within the domain...