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Seminars

Institute of Cell Biology Seminar Series

 

Seminars are usually held on Mondays at 12.00 noon in Lecture Theatre 1, Daniel Rutherford Building.

Please note that seminars in May will be held on Wednesdays.

Everyone is welcome to attend.

 

Semester Two: January - June 2014

 

Date

Speaker

Host

13th Jan 2014

Dr Aurelie Bertin

Institut Curie, Paris

Julie Welburn

20th Jan 2014

Dr Hervé le Hir

CNRS, Paris

Atlanta Cook

27th Jan 2014

Professor Vernonica Franklin-Tong

College of Life & Environmental Sciences, University of Birmingham

Justin Goodrich

3rd Feb 2014

Professor Jim Naismith

University of St Andrews

Laura Spagnolo

10th Feb 2014

Dr Chris Smith

University of Cambridge

Steve West

17th Feb 2014

Professor Peter Becker

Ludwig Maximilians Universität, München, Germany

Irina Stancheva

24th Feb 2014

Dr Vardis Ntoukakis

School of Life Science, University of Warwick

Gerben van Ooijen

3rd March 2014

Dr Michaela Frye

CR-UK Senior Fellow

Wellcome Trust Medical Research Council Stem Cell Institute Cambridge

Irina Stancheva

10th March 2014

Dr Marie-Hélène Verlhac

NRS, Group Leader in the Center for Interdisciplinary Research in Biology (CIRB), Paris, France

Hiro Ohkura

17th March 2014

Dr Richard McCulloch

University of Glasgow

Heidrun Interthal

24th March 2014

Dr Jesper Svejstrup

Cancer Research UK, LRI, Clare Hall

Adrian Bird

31st March 2014

Professor Holger Puchta

University Karlsruhe, Germany

Peter Doerner

7th April 2014

Dr Jens Januschke

College of Life Sciences, University of Dundee

Hiro Ohkura

14th April 2014

No seminar

 

21st April 2014

Easter Monday - No seminar

 

28th April 2014

Dr Pietro Spanu

Department of Life Sciences, Imperial College London

Gary Loake

Wed 7th May 2014

Professor Witek Filipowicz

Friedrich Miescher Institute for Biomedical Research, Switzerland

David Tollervey

Wed 14th May 2014

No seminar – ISAB

 

Wed 21st May 2014

Dr Julie Ahringer

Wellcome Trust/Cancer Research UK, Gurdon Institute, University of Cambridge

Adrian Bird

Wed 28th May 2014

Professor Sir Tom Blundell

University of Cambridge

JP Arulanandam

2nd June 2014

Professor Tamas Dalmay

Head of School of Biological Sciences, University of East Anglia

Attila Molnar

9th June 2014

Professor Darren Monckton

Institute of Molecular Cell and Systems Biology, University of Glasgow

David Finnegan

16th June 2014

Dr Iva Tolic-Norrelykke

Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany

Teuta Pilizota

23rd June 2014

Dr Iain Hagan

Cancer Research UK Manchester Institute

Andrew Goryachev

30th June 2014

Dr Wolfgang Busch

Gregor Mendel Institute of Molecular Plant Biology

Peter Doerner

 

 

 

Other seminars

Date Event
17th Feb 2014
12:00
Daniel Rutherford
G27 Lecture Theatre 1

Professor Peter Becker - Ludwig Maximilians Universität, München, Germany

WT PhD programme seminar - Get the numbers right or die: how male fruit flies get away with just one X chromosome

Eukaryotic genomes are highly evolved systems of gene expression that are challenged by sex chromosome aneuploidies, In humans and fruit flies the females bear a diploid genome with two X chromosome, but the male genome only contains a single X. This reduced dose is compensated for by an elaborate regulatory 'dosage compensation' process, which increases most of the transcription on the X in the two-fold range. The dosage compensation machinery comprises five protein subunits, amongst which three are enzymes, and a long, non-coding RNA. How does this machinery identify the X chromosome so stringently? How can transcription levels be tuned in such a fine range? Which role does the non-coding RNA play in answering these questions will reveal fundamental principles of gene regulation that are harnessed for the task of genome balancing.

Host: Irina Stancheva


10th Feb 2014
12:00
Daniel Rutherford
G27 Lecture Theatre 1

Dr Chris Smith - University of Cambridge

WT PhD programme seminar - Understanding the roles of alternative pre-mRNA splicing in shaping smooth muscle cell transcriptomes

Alternative pre-mRNA splicing is a key molecular mechanism that allows diversification of expressed proteomes far beyond the limitations suggested by a simple "gene-count" of a genome. Many examples of functionally important alternative splicing events have been described, while diseases arising from disruption of alternative splicing show that not only is RNA splicing an essential step in gene expression, but that appropriate regulation of alternative splicing programmes is essential for healthy development. Analyses of alternative splicing have employed both molecular dissection of individual alternative splicing events, as well as global profiling and computational analyses of co-regulated programmes of alternative splicing. I will describe the use of both types of approach by my lab in the analysis of alternative splicing in smooth muscle cells.

 

Host: Steve West


20th Jan 2014
12:00
Daniel Rutherford Building
G27 Lecture Theatre 1

Dr Hervé le Hir - CNRS, Paris

WT PhD programme seminar - The Exon Junction Complex, a multifaceted RNP complex dissected by different approaches from single-molecule to RNA-seq

To function properly, eukaryotic messenger RNAs (mRNAs) must contain a complete open reading frame to serve as an adequate template for protein synthesis, but also all the information that specifies their export from the nucleus, subcellular localization, translation, and stability. Much of this information is carried by the proteins composing mRNA-protein (mRNP) particles. My group is studying the multiprotein exon junction complex (EJC) deposited onto nuclear mRNAs by the splicing machinery. The EJC is composed of a dozen proteins and accompanies mRNAs to the cytoplasm to communicate with various machineries involved in export, translation, degradation, and subcellular localization. The EJC is also involved in the quality control process of nonsense-mediated mRNA decay (NMD) that eliminates aberrant mRNAs. In order to dissect EJC structure and the mechanisms by which it achieves its multiple functions, we are combining various approaches including biochemistry, structural and molecular biology, transcriptomics as well as single-molecule biophysics (magnetic tweezers). One peculiar aspect of the EJC is that it contains two RNA helicases, the DEAD-box eIF4AIII serving as an RNA clamp and Upf1 essential for NMD. Therefore, the EJC is a perfect model to understand how these ATP-dependent molecular motors are regulated by their binding partners.


Host: Atlanta Cook


16th Jan 2014
12:00
Darwin Building
G10

Maria Christophorou, Gurdon Institute, University of Cambridge

Molecular mechanisms and cellular functions controlled by citrullination

Host: David Tollervey/Robin Allshire


13th Jan 2014
12:00
Daniel Rutherford
G27 Lecture Theatre 1

Dr Aurelie Bertin - Institut Curie, Paris

WT PhD programme seminar - Septins: ultrastructural plasticity of cytoskeletal multi-tasking proteins.

Septins are cytoskeletal filaments bound to the inner cell membrane. They are ubiquitous in eukaryotes and are essential for cell division. During cytokinesis, the last step of cell division, septins are arranged circumferentially around constriction sites. Septins are involved in building diffusion barriers for transmembrane proteins or proteins anchored to the membrane. By complementary electron microscopy and cryo-electron microscopy methods we have carried out a global study from the molecule to the cell. Using single particle image analysis and cryo-tomography, we have shown that the ultrastructural organization of septins is highly variable both in vitro and in situ. First, we have determined by single particle image analysis that the budding yeast septin complex, assemble into a linear, symetric and octameric oligomer. This minimal complex can then assemble into a nonpolar paired filament in low salt conditions [1]. To mimic the septin-membrane interaction, we have used biomimetic assays. Hence, we have shown that PI(4,5)P2 interacts specifically with septins and organizes septins in a novel manner [2]. Conversely, septins are able to deform vesicles into plaque-like structures.  Besides, we have described the organization of septin filaments in situ for the first time within budding yeast dividing cells, by electron cryo-tomography [3]. Besides we have  recently shown that septins from higher eukaryotes are able to bundle and curve actin filaments.

1. Bertin, A., et al., Saccharomyces cerevisiae septins: supramolecular organization of heterooligomers and the mechanism of filament assembly. Proc Natl Acad Sci U S A, 2008. 105(24): P. 8274-9.
2. Bertin, A., et al., Phosphatidylinositol-4,5-bisphosphate promotes budding yeast septin filament assembly and organization. J Mol Biol, 2010. 404(4): P. 711-31.
3. Bertin, A., et al., Three-dimensional ultrastructure of the septin filament network in Saccharomyces cerevisiae. Mol Biol Cell, 2012. 23(3): P. 423-32.

Host: Julie Welburn


29th Nov 2013
14:00
Michael Swann Building
S7.15

Andrew McAinsh, University of Warwick

Unique properties of the human kinesin-12 Kif15

Host: Julie Welburn


19th Nov 2013
11:00
Darwin Building
G10

Philipp Voigt, NYU School of Medicine/Howard Hughes Medical Institute

Nucleosomal asymmetry and bivalent domains in embryonic stem cells

Posttranslational modifications of histone proteins are key elements in the regulation of gene expression. The basic units of chromatin are the nucleosomes, which contain two copies each of the four core histones. Despite extensive research on histone marks, it has remained unclear whether the sister histones within a nucleosome carry identical modifications in vivo or not. The symmetry state of histone modifications directly affects their potential inheritance and readout by effector proteins. Moreover, asymmetric modification may provide means to establish co-occurrence within a nucleosome of marks that are commonly assumed to be mutually exclusive within histones. With an approach based on modification-specific antibodies and mass spectrometry, we were able to show that chromatin consists of both symmetric and asymmetric mononucleosome populations in vivo. For both H3K27me2/3 and H4K20me1, we observed a combination of symmetric and asymmetric nucleosomes for embryonic stem (ES) cells, HeLa cells, and embryonic fibroblasts.

To begin exploring implications of nucleosomal asymmetry, we analyzed co-occurrence of the histone marks on single nucleosomes. A hallmark of ES cell chromatin is the presence of promoters that simultaneously feature the activating mark H3K4me3 and the repressive mark H3K27me3. These ‘bivalent domains’ are presumed to poise developmental genes for activation, facilitating rapid and robust expression upon appropriate differentiation cues while keeping them repressed in ES cells. However, it remains unclear how bivalency is attained at genomic loci. We found that sizable amounts of nucleosomes (as opposed to histones) exist in ES cells that carry both H3K4me3 and H3K27me3. Notably, within these bivalent nucleosomes, each copy of H3 carries one of the two marks in an asymmetric conformation. We further demonstrated that Polycomb Repressive Complex 2 (PRC2), which catalyzes H3K27me3, is inhibited by H3K4me3 if present in symmetrical but not asymmetrical fashion, allowing for the generation of asymmetric bivalent nucleosomes. These findings uncover a potential mechanism for the incorporation of bivalent features into nucleosomes and show how asymmetry might set the stage to diversify functional nucleosome states.

Host: Robin Allshire/David Tollervey


26th Jun 2013
16:00
Michael Swann Building
Main Lecture Theatre

Professor Adrian Bird

Wellcome Trust PhD Programme in Cell Biology Symposium Lecture - Epigenetics and Rett syndrome

Autism is genetically complex, but several conditions within the autistic spectrum have simple causes. Because of their known origin, single gene disorders of this kind are more straightforward to understand and may hold lessons that apply broadly. An example is Rett syndrome, a profound autism spectrum disorder, which almost exclusively results from mutations in the MECP2 gene. Normally this gene makes a protein that binds to sites on DNA that are chemically altered by DNA methylation. In fact the MECP2 protein appears to interpret this “epigenetic” mark to affect gene expression. Why should loss of this function affect the brain? Are the resulting defects reversible? What are the prospects for therapy for this and perhaps related conditions? Professor Bird will draw upon the latest research that addresses these questions.

Host: Wellcome Trust PhD Programme in Cell Biology


29th May 2013
12:00
Daniel Rutherford
LT1 G27

Ronald T. Hay - Centre for Gene Regulation and Expression, University of Dundee

WT PhD programme seminar - Decoding the SUMO Signal

Small Ubiquitin-like Modifier (SUMO) emerged from the shadow of the well-established ubiquitin some 15 years ago when it was shown that a distinct conjugation pathway was responsible for SUMO modification. Since then it has been established that SUMO modifies over a thousand substrates and plays diverse roles in many important biological processes. Recognition of SUMO is mediated by short peptide sequences known as SUMO Interaction Motifs (SIMs) that allow effector proteins to engage SUMO modified substrates. Like ubiquitin, SUMO can form polymeric chains and these chains can be recognized by proteins containing multiple SIMs. One protein that contains such a sequence of SIMs also contains a RING domain that is the hallmark of a ubiquitin E3 ligase. This ubiquitin ligase known as RNF4 has the unique property that it can recognize SUMO modified proteins and target them for ubiquitin mediated proteolysis. Structural and biochemical analyses of RNF4 has shed light on the long sought after mechanism of ubiquitin transfer and illustrates how its RING domain primes the ubiquitin loaded E2 for catalysis.

Plechanovová A, Jaffray EG, Tatham MH, Naismith JH, Hay RT. (2012)  Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis.  Nature 489, 115-120

Plechanovová A, Jaffray EG, McMahon SA, Johnson KA, Navratilova I, Naismith JH, Hay RT. (2011) Mechanism of ubiquitylation by dimeric RING ligase RNF4. Nature Structural and Molecular Biology 18:1052-9

Host: WCB