Bijvoet Center Progress Report 2014-2015

Total Page:16

File Type:pdf, Size:1020Kb

Bijvoet Center Progress Report 2014-2015 Bijvoet Center for Biomolecular Research Progress Report 2014-2015 “Discovering the Molecular Basis of Life” Table of Contents Contact Details Bijvoet Center Information 2UJDQL]DWLRQ 6FLHQWLILF2XWSXW *UDQWVDQG$ZDUGV %LMYRHW6FKRRO Principal Investigators $QQD$NKPDQRYD 0DDUWHQ$OWHODDU 0DUF%DOGXV &HOLD%HUNHUV 5ROI %RHOHQV $OH[DQGUH%RQYLQ *HHUW-DQ%RRQV ,QHNH%UDDNPDQ (HIMDQ%UHXNLQN *HUW)RONHUV )ULHGULFK)|UVWHU :LOOLH*HHUWV 3LHW*URV $OEHUW+HFN &DVSHU+RRJHQUDDG (ULF+XL]LQJD %HUW-DQVVHQ $QWRLQHWWH.LOOLDQ 7RRQGH.URRQ /RHV.URRQ%DWHQEXUJ 6LPRQH/HPHHU 0DUWLQ/XW] 1DWKDQLHO0DUWLQ 0DGHORQ0DXULFH :DOO\0OOHU 5RODQG3LHWHUV +ROJHU5HKPDQQ 6WHIDQ5GLJHU 5LFKDUG6FKHOWHPD 0DUF7LPPHUV 0DUNXV:HLQJDUWK Introduction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´GLVFRYHULQJ WKH 0R KROGVLJQLILFDQWSRWHQWLDOIRUGHYHORS 5REGH9ULHVRI WKH0HGLFLQDO&KHP OHFXODU%DVLVRI /LIHµ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·VZRUN &HQWHU,QWKHVDPH\HDUSURI*HHUW $YDQWL SUL]H IRU RXWVWDQGLQJ FRQWUL RQ PDNLQJ WKH FRPLQJ \HDUV DQ -DQ%RRQVDJO\FRPLFVDQGFKHPLFDO EXWLRQV WR WKH XQGHUVWDQGLQJ RI OL RWKHUPLOHVWRQHLQWKHKLVWRU\RI RXU ELRORJ\H[SHUWZDVDSSRLQWHGMRLQWO\ SLG ELRSK\VLFV ,Q $XJXVW WKH FHQWHU ZLWK WKH 8WUHFKW ,QVWLWXWH IRU 3KDU $PHULFDQ&KHPLFDO6RFLHW\KRQRXUHG PDFHXWLFDO6FLHQFHVDVDQHZSURIHV $OEHUW+HFNZLWKWKH¶$&6)UDQN+ VRUDW8WUHFKW8QLYHUVLW\7KLV\HDU )LHOGDQG-RH/)UDQNOLQ$ZDUGIRU SURI)ULHGULFK)|UVWHUDQGGU7VYL\D 2XWVWDQGLQJ $FKLHYHPHQWV LQ 0DVV =HHY%HQ0RUGHKDL WZR H[SHUWV 6SHFWURPHWU\· DQG SUHVHQWHG WKH LQ FU\RHOHFWURQ PLFURVFRS\ ZLOO ¶$UWKXU & &RSH 6FKRODU $ZDUG· WR MRLQRXUFHQWHU7KHVHQHZDGGLWLRQV *HHUW-DQ%RRQV(DUO\&DVSHU WR WKH %LMYRHW &HQWHU ZLOO IXUWKHU +RRJHQUDDG ZDV DZDUGHG WKH VWUHQJWKHQRXUVFLHQWLILFSRVLWLRQDQG ,%52.HPDOL,QWHUQDWLRQDO3UL]HIRU WKHILUVWFROODERUDWLYHSXEOLFDWLRQVDUH 5HVHDUFK LQ WKH )LHOG RI %DVLF DQG DOUHDG\HPHUJLQJ &OLQLFDO1HXURVFLHQFH Prof. dr. Marc Baldus Dr. Reinout Raijmakers 6FLHQWL¿F'LUHFWRU 0DQDJLQJ'LUHFWRU Bijvoet Center for Biomolecular Research 1 Contact Details Postal address 6FLHQWL¿F$GYLVRU\%RDUG Bijvoet Center for Biomolecular Research Padualaan 8 Prof.dr. J.F.G. Vliegenthart (chairman) Utrecht University Emeritus of Utrecht University, NL Padualaan 8 (room O604) Prof.dr. A. Bax 3584 CH Utrecht NIH, Bethesda, USA The Netherlands Prof.dr. J. Johnson, The Scripps Research Institute, La Jolla, USA Prof.dr. K. Wilson Contact details University of York, UK Dr. Reinout Raijmakers Managing Director Bijvoet Center for Biomolecular Research Visiting addresses Tel.: +31 30 253 6804 E-mail: [email protected] .UX\WJHERXZ [email protected] Padualaan 8 3584 CH Utrecht Website Bijvoet Center The Netherlands www.bijvoet-center.eu %ORHPEHUJHQJHERXZ Enter via Kruytgebouw Padualaan 8 3584 CH Utrecht The Netherlands 'DYLGGH:LHGJHERXZ Website PhD programme MLS Universiteitsweg 99 www.bijvoet-center.eu/phd-programme/ 3484 CG Utrecht The Netherlands Executive Board Prof. dr. M. Baldus (Scientific Director) Prof. dr. A.J.R. Heck Stratenum Prof. dr. P. Gros Prof. dr. I. Braakman Universiteitsweg 100 Prof. dr. A. Killian 3584 CG Utrecht Prof. dr. G.J. Boons The Netherlands Dr. R. Raijmakers (Managing Director) Colofon Design by Reinout Raijmakers, photography by Ivar Pel, Bas van Breukelen, Reinout Raijmakers, and others. 2 Bijvoet Center for Biomolecular Research Bijvoet Center for Biomolecular Research 3 Organization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iomolecular Mass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² WKH 'HSDUWPHQWV RI &KHPLVWU\ DQG IURP¶FHOOVWRDWRPV·²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|UVWHUZLOOVWDUWDVWKHQHZKHDGRI 7KH &U\VWDO DQG 6WUXFWXUDO &KHP EUDQHV DUH LQYROYHG LQ WKH PRGH RI WKH&U\R(0JURXS7KHJURXSIXU LVWU\ JURXS SHUIRUPV UHVHDUFK LQWR DFWLRQ RI GUXJV WR[LQV DQWLELRWLFV WKHU LQFOXGHV SULQFLSDO LQYHVWLJDWRUV WKH WKUHHGLPHQVLRQDO VWUXFWXUHV RI DQG DP\ORLG IRUPLQJ SURWHLQV 3ULQ :DOO\0OOHUDQG:LOOLH*HHUWV PROHFXOHVZKLFKGHILQHWKHPROHFXODU FLSDO LQYHVWLJDWRUV LQ WKLV JURXS DUH LQWHUDFWLRQVDQGUHDFWLRQVWKDWXQGHU $QWRLQHWWH .LOOLDQ 7RRQ GH .URRQ Timmers group OLH FRPSOH[ FKHPLFDO DQG ELRORJLFDO DQG(HIMDQ%UHXNLQN 7KH UHVHDUFK RI 0DUF 7LPPHUV IR SURFHVVHV 7KH PDLQ UHVHDUFK OLQHV FXVHVRQWKHLQWHUSOD\EHWZHHQFKUR DUHLQWKHILHOGRI SURWHLQFU\VWDOORJ &HOOXODU3URWHLQ&KHPLVWU\
Recommended publications
  • Kinesin-4 KIF21B Limits Microtubule Growth to Allow Rapid Centrosome
    RESEARCH ARTICLE Kinesin-4 KIF21B limits microtubule growth to allow rapid centrosome polarization in T cells Peter Jan Hooikaas1†, Hugo GJ Damstra1†, Oane J Gros1, Wilhelmina E van Riel1‡, Maud Martin1§, Yesper TH Smits2, Jorg van Loosdregt2, Lukas C Kapitein1, Florian Berger1*, Anna Akhmanova1* 1Cell Biology, Neurobiology and Biophysics, Department of Biology, Faculty of Science, Utrecht University, Utrecht, Netherlands; 2Center for Translational Immunology, University Medical Center Utrecht, Utrecht University, Utrecht, Netherlands Abstract When a T cell and an antigen-presenting cell form an immunological synapse, rapid dynein-driven translocation of the centrosome toward the contact site leads to reorganization of microtubules and associated organelles. Currently, little is known about how the regulation of *For correspondence: microtubule dynamics contributes to this process. Here, we show that the knockout of KIF21B, a [email protected] (FB); kinesin-4 linked to autoimmune disorders, causes microtubule overgrowth and perturbs [email protected] (AA) centrosome translocation. KIF21B restricts microtubule length by inducing microtubule pausing typically followed by catastrophe. Catastrophe induction with vinblastine prevented microtubule †These authors contributed overgrowth and was sufficient to rescue centrosome polarization in KIF21B-knockout cells. equally to this work Biophysical simulations showed that a relatively small number of KIF21B molecules can restrict ‡ Present address: Netherlands mirotubule length and promote an imbalance
    [Show full text]
  • Cell Architecture: Putting the Building Blocks Together
    COCEBI-1090; NO. OF PAGES 3 Available online at www.sciencedirect.com Cell architecture: putting the building blocks together Editorial overview Anna Akhmanova and Tim Stearns Current Opinion in Cell Biology 2012, 25:xx–yy 0955-0674/$ – see front matter, # 2012 Elsevier Ltd. All rights reserved. http://dx.doi.org/10.1016/j.ceb.2012.12.003 Anna Akhmanova Cell Biology, Faculty of Science, Utrecht In considering cell architecture it is important to realize that for cells, as for University, Padualaan 8, 3584 CH Utrecht, buildings, the underpinning for the external shape is provided by a complex The Netherlands internal superstructure. And for cells, this cytoskeletal underpinning must e-mail: [email protected] be highly dynamic to effect the changes in morphology and organization associated with division, growth and differentiation. Cytoskeletal elements Anna Akhmanova is Professor of Cell Biology at Utrecht University, the Netherlands, and a were some of the first components of intracellular structure described by member of EMBO. Her lab uses cell early microscopists in the late 19th century, but it was not until a century biological approaches, in vitro reconstitutions later that the remarkable complexity of the cytoskeleton, in both compo- and high-resolution microscopy to study sition and behavior, has been revealed. Advances in genomics and proteo- molecular mechanisms of microtubule mics have provided us with near-comprehensive lists of the molecular dynamics and vesicle trafficking and their players associated with the various cytoskeletal systems. The challenge contribution to mammalian development and human disease. now is to understand how these components work together, and this is one of the central themes of this issue of Current Opinion in Cell Biology.
    [Show full text]
  • EMBO Facts & Figures
    excellence in life sciences Reykjavik Helsinki Oslo Stockholm Tallinn EMBO facts & figures & EMBO facts Copenhagen Dublin Amsterdam Berlin Warsaw London Brussels Prague Luxembourg Paris Vienna Bratislava Budapest Bern Ljubljana Zagreb Rome Madrid Ankara Lisbon Athens Jerusalem EMBO facts & figures HIGHLIGHTS CONTACT EMBO & EMBC EMBO Long-Term Fellowships Five Advanced Fellows are selected (page ). Long-Term and Short-Term Fellowships are awarded. The Fellows’ EMBO Young Investigators Meeting is held in Heidelberg in June . EMBO Installation Grants New EMBO Members & EMBO elects new members (page ), selects Young EMBO Women in Science Young Investigators Investigators (page ) and eight Installation Grantees Gerlind Wallon EMBO Scientific Publications (page ). Programme Manager Bernd Pulverer S Maria Leptin Deputy Director Head A EMBO Science Policy Issues report on quotas in academia to assure gender balance. R EMBO Director + + A Conducts workshops on emerging biotechnologies and on H T cognitive genomics. Gives invited talks at US National Academy E IC of Sciences, International Summit on Human Genome Editing, I H 5 D MAN 201 O N Washington, DC.; World Congress on Research Integrity, Rio de A M Janeiro; International Scienti c Advisory Board for the Centre for Eilish Craddock IT 2 015 Mammalian Synthetic Biology, Edinburgh. Personal Assistant to EMBO Fellowships EMBO Scientific Publications EMBO Gold Medal Sarah Teichmann and Ido Amit receive the EMBO Gold the EMBO Director David del Álamo Thomas Lemberger Medal (page ). + Programme Manager Deputy Head EMBO Global Activities India and Singapore sign agreements to become EMBC Associate + + Member States. EMBO Courses & Workshops More than , participants from countries attend 6th scienti c events (page ); participants attend EMBO Laboratory Management Courses (page ); rst online course EMBO Courses & Workshops recorded in collaboration with iBiology.
    [Show full text]
  • Meeting Booklet
    LS2 Annual Meeting 2019 “Cell Biology from Tissue to Nucleus” Meeting Booklet 14-15 February, University of Zurich, Campus Irchel LS 2 - Life Sciences Switzerland Design by Dagmar Bocakova - [email protected] 2019 WELCOME ADDRESS Dear colleagues and friends It is with great pleasure that we invite you to the LS² Annual Meeting 2019, held on the 14th and 15th of February, 2019 at the Irchel Campus of the University of Zurich. This is a special year, as it is the 50th anniversary of USGEB/LS2, which we will celebrate with a Jubilee Apéro on Thursday 14th. The LS² Annual Meeting brings together scientists from all nations and backgrounds to discuss a variety of Life Science subjects. The meeting this year focusses on the cell in health and disease, with plenary talks on different aspects of cell biology and a symposium on live cell imaging approaches. You will be able to hear the latest, most exciting findings in several fields, from Molecular and Cellular Biosciences, Proteomics, Chemical Biology, Physiology, Pharmacology and more, presented by around 30 invited speakers and 45 speakers selected from abstracts in one of the seven scientific symposia and five plenary lectures. Two novelties highlight the meeting this year: The "PIs of Tomorrow" session, in which selected postdocs will present their research to a jury of professors, will be for the first time a plenary session. In addition, poster presenters will be selected to give flash talks in the symposia with the spirit to further promote young scientists. Join us for the poster session with more than 130 posters, combined with a large industry exhibition and the Jubilee Apéro.
    [Show full text]
  • Connecting the Nucleus to the Cytoskeleton by SUN–KASH
    COCEBI-1074; NO. OF PAGES 6 Available online at www.sciencedirect.com Connecting the nucleus to the cytoskeleton by SUN–KASH bridges across the nuclear envelope Erin C Tapley and Daniel A Starr The nuclear–cytoskeleton connection influences many aspects with a wide variety of cytoskeletal components [11]. of cellular architecture, including nuclear positioning, the Mutations in mammalian SUN and KASH proteins lead stiffness of the global cytoskeleton, and mechanotransduction. to developmental defects in neurogenesis, gametogen- Central to all of these processes is the assembly and function of esis, myogenesis, cilliogenesis, and retina formation and conserved SUN–KASH bridges, or LINC complexes, that span contribute to human diseases, including muscular dystro- the nuclear envelope. Recent studies provide details of the phy, ataxia, Progeria, lissencephaly, and cancer higher order assembly and targeting of SUN proteins to the [11,17,18,19,20 ]. inner nuclear membrane. Structural studies characterize SUN– KASH interactions that form the central link of the nuclear- The rapidly growing field of nuclear–cytoskeletal inter- envelope bridge. KASH proteins at the outer nuclear membrane actions has recently been reviewed [11–13]. Here, with link the nuclear envelope to the cytoskeleton where forces are apologies to the rest of the field, we focus on five major generated to move nuclei. Significantly, SUN proteins were findings reported over the past two years. The first step of recently shown to contribute to the progression of building the SUN–KASH bridge is recruiting SUN laminopathies. proteins to the inner nuclear membrane. Surprisingly, trafficking SUN proteins to the inner nuclear membrane Address involves multiple, partially redundant mechanisms Department of Molecular and Cellular Biology, University of California, [21 ,22 ,23 ].
    [Show full text]
  • Tubulin Depolymerization May Be an Ancient Biological Motor
    Commentary 3425 Tubulin depolymerization may be an ancient biological motor J. Richard McIntosh1,*, Vladimir Volkov1,2, Fazly I. Ataullakhanov2,3 and Ekaterina L. Grishchuk4 1Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder, CO 80309, USA 2Center for Theoretical Problems of Physicochemical Pharmacology, Russian Academy of Sciences, Moscow, 119991, Russia 3National Center for Hematology, Moscow, 125167, Russia 4Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA *Author for correspondence ([email protected]) Journal of Cell Science 123, 3425-3434 © 2010. Published by The Company of Biologists Ltd doi:10.1242/jcs.067611 Summary The motions of mitotic chromosomes are complex and show considerable variety across species. A wealth of evidence supports the idea that microtubule-dependent motor enzymes contribute to this variation and are important both for spindle formation and for the accurate completion of chromosome segregation. Motors that walk towards the spindle pole are, however, dispensable for at least some poleward movements of chromosomes in yeasts, suggesting that depolymerizing spindle microtubules can generate mitotic forces in vivo. Tubulin protofilaments that flare outward in association with microtubule shortening may be the origin of such forces, because they can move objects that are appropriately attached to a microtubule wall. For example, some kinetochore-associated proteins can couple experimental objects, such as microspheres, to shortening microtubules in vitro, moving them over many micrometers. Here, we review recent evidence about such phenomena, highlighting the force-generation mechanisms and different coupling strategies. We also consider bending filaments of the tubulin-like protein FtsZ, which form rings girding bacteria at their sites of cytokinesis.
    [Show full text]
  • Regulation of Microtubule Dynamics by Protein Interaction Networks At
    Regulati on of Microtubule Dynamics by Protein Interacti on Networks at Microtubule Tips Babet van der Vaart © B. van der Vaart This thesis was printed by CPI-Wörhmann Print Service, Zutphen The research presented in this thesis was performed at the Department of Cell Biology of the Erasmus Medical Center in Rott erdam, The Netherlands. This research was supported by the Netherlands Organizati on for Scienti fi c Research ALW open program and ALW-VICI grants. Cover: Geometric shape representi ng an interacti on network surrounding a plus Regula ti on of Microtubule Dynamics by Protein Interacti on Networks at Microtubule Tips Regulati e van microtubuli dynamiek door eiwit interacti e netwerken op microtubuli uiteinden Proefschrift ter verkrijging van de graad van doctor aan de Erasmus Universiteit Rott erdam op gezag van de rector magnifi cus Prof.dr. H.G. Schmidt en volgens besluit van het College voor Promoti es De openbare verdediging zal plaatsvinden op woensdag 8 juni 2011 om 13:30 uur door Babet van der Vaart geboren te Vlaardingen Promoti ecommissie: Promotoren: Prof.dr. F. G. Grosveld Prof.dr. A. Akhmanova Overige leden: Prof.dr. C.C. Hoogenraad Dr.ir. N.J. Galjart Dr. M.O. Steinmetz Table of contents Scope of this thesis 7 Chapter 1. Introducti on: Regulati on of microtubule dynamic instability 11 Biochemical Society Transacti ons. 2009 Oct;37(Pt 5):1007-13. Chapter 2. STIM1 is a MT-plus-end tracking protein involved in 21 remodelling of the ER Current Biology. 2008 18:177-82 Chapter 3. SLAIN2 links microtubule plus-end tracking proteins and 37 controls microtubule growth in interphase The Journal of Cell Biology.
    [Show full text]
  • Insights Into Enhanced Complement Activation by Structures Of
    University of Groningen Insights Into Enhanced Complement Activation by Structures of Properdin and Its Complex With the C-Terminal Domain of C3b COMBAT Consortium; van den Bos, Ramon M.; Pearce, Nicholas M.; Granneman, Joke; Brondijk, T. Harma C.; Gros, Piet; Berger, S.; van den Born, J.; van den Heuvel, L.; van de Kar, N. Published in: Frontiers in Immunology DOI: 10.3389/fimmu.2019.02097 IMPORTANT NOTE: You are advised to consult the publisher's version (publisher's PDF) if you wish to cite from it. Please check the document version below. Document Version Publisher's PDF, also known as Version of record Publication date: 2019 Link to publication in University of Groningen/UMCG research database Citation for published version (APA): COMBAT Consortium, van den Bos, R. M., Pearce, N. M., Granneman, J., Brondijk, T. H. C., Gros, P., ... Gros, P. (2019). Insights Into Enhanced Complement Activation by Structures of Properdin and Its Complex With the C-Terminal Domain of C3b. Frontiers in Immunology, 10, [2097]. https://doi.org/10.3389/fimmu.2019.02097 Copyright Other than for strictly personal use, it is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license (like Creative Commons). Take-down policy If you believe that this document breaches copyright please contact us providing details, and we will remove access to the work immediately and investigate your claim. Downloaded from the University of Groningen/UMCG research database (Pure): http://www.rug.nl/research/portal.
    [Show full text]
  • Microtubule +Tips at a Glance Anna Akhmanova and Michel O
    Cell Science at a Glance 3415 Microtubule +TIPs at a modifications of microtubules’ by Dorota Wloga and diverse group of proteins that are distinguished Jacek Gaertig (J. Cell Sci. 123, pp. 3447-3455). by their specific accumulation at microtubule glance plus ends (Mimori-Kiyosue et al., 2000; Perez et Microtubules are highly dynamic hollow tubes al., 1999; Schuyler and Pellman, 2001). +TIPs Anna Akhmanova1 and Michel O. that are involved in many vital cellular typically target growing but not shrinking Steinmetz2 activities, including maintenance of cell shape, microtubule ends; however +TIP association 1 Department of Cell Biology, Erasmus Medical division, migration and intracellular transport. with depolymerizing ends can occur and, in Center, PO Box 2040, 3000 CA Rotterdam, The Netherlands They are assembled from heterodimers of - some organisms such as budding yeast, is even 2Biomolecular Research, Structural Biology, Paul and -tubulin that align in a head-to-tail fashion. quite common. In this Cell Science at a Glance Scherrer Insititut, CH-5232 Villigen PSI, Switzerland Microtubules are, thus, intrinsically polar article we review and illustrate the current ([email protected]; [email protected]) because they contain two structurally distinct knowledge of these peculiar proteins, ends: a slow-growing minus end, exposing - summarize their structural and functional Journal of Cell Science 123, 3415-3419 © 2010. Published by The Company of Biologists Ltd tubulin subunits; and a fast-growing plus end, properties, and discuss the proposed molecular doi:10.1242/jcs.062414 exposing -tubulin subunits (for a review, see mechanisms that they use to track microtubule Nogales and Wang, 2006).
    [Show full text]
  • Emergent Properties of the Cytoskeleton: Molecules to Cells Hotel Eden Roc, Sant Feliu De Guixols (Costa Brava)  Spain 3-8 October 2010
    RESEARCH CONFERENCES ESF-EMBO Symposium Emergent Properties of the Cytoskeleton: Molecules to Cells Hotel Eden Roc, Sant Feliu de Guixols (Costa Brava) Spain 3-8 October 2010 With support from The cytoskeletal field is fast moving and changing very quickly. As well as new discoveries in how proteins are assembled, regulated and interact to contribute to cell behaviour and function, there are new developments in imaging technology, and in chemical biology that are pushing forward the frontiers of research into the cytoskeleton and cell behaviour. Indeed, cytoskeletal research often works as a paradigm for the development of new imaging techniques and experimental approaches, because of its well characterized cellular structure. This conference will address the best and the newest developments in this research area. It brings together researchers from a broad range of scientific backgrounds, but with a common aim of understanding the basic Chair: Michelle Peckham - University of Leeds, UK properties of the cytoskeleton, and how Co-Chair: Claudia Veigel - National Institute of Medical Research, UK it is organised and utilised by cells and tissues. Invited Speakers will include: This meeting intends to capitalize on the Plenary Lecture on Photo- Single Molecules & Forces cross-fertilization of ideas between activated Localization Microscopy - Marileen Dogterom - AMOLF-Amsterdam, NL - Matthias Rief - U. Munich, DE researchers from different experimental - Jennifer Lippincott Schwartz - NIH, US backgrounds to generate new - Claudia Veigel - NIMR, UK Cytoskeletal Motors Microtubule Dynamics & Regulation in collaborations and ideas. The topics to - Stan Burgess - Leeds U., UK be covered include subjects from - Anne Houdusse - Institute Curie, FR the Cell passive mechanical properties of the - Carolyn Moores - Birkbeck, London, UK - Anna Akhmanova - EMC Dept.
    [Show full text]
  • Generation and Regulation of Microtubule Network Asymmetry to Drive Cell Polarity Joyce C
    Available online at www.sciencedirect.com ScienceDirect Generation and regulation of microtubule network asymmetry to drive cell polarity Joyce C. M. Meiring, Boris I. Shneyer and Anna Akhmanova Abstract are associated with the generation of cellular asymme- Microtubules control cell architecture by serving as a scaffold tries. Microtubule networks participate in these pro- for intracellular transport, signaling, and organelle positioning. cesses by responding and contributing to cell polarity. Microtubules are intrinsically polarized, and their orientation, Microtubules themselves are intrinsically polarized density, and post-translational modifications both respond and because they are built of directionally aligned polarized contribute to cell polarity. Animal cells that can rapidly reorient subunits, ab-tubulin dimers. Microtubules thus have their polarity axis, such as fibroblasts, immune cells, and two distinct ends, the minus end and the plus end. The cancer cells, contain radially organized microtubule arrays minus ends exhibit slow dynamics and can be stably anchored at the centrosome and the Golgi apparatus, whereas anchored at a variety of microtubule-organizing centers stably polarized cells often acquire non-centrosomal microtu- (MTOCs), whereas the plus ends can grow and shrink bule networks attached to the cell cortex, nucleus, or other rapidly and interact with different intracellular struc- structures. Microtubule density, longevity, and post- tures [1e3]. Motors that carry cargos along microtu- translational modifications strongly depend on the dynamics of bules, kinesins, and dyneins can typically only move in their plus ends. Factors controlling microtubule plus-end dy- one direction [4], and microtubule orientation thus namics are often part of cortical assemblies that integrate strongly determines the logistics of intracellular cytoskeletal organization, cell adhesion, and secretion and are transport.
    [Show full text]
  • A Structural Model for Microtubule Minus-End Recognition and Protection by CAMSAP Proteins
    HHS Public Access Author manuscript Author ManuscriptAuthor Manuscript Author Nat Struct Manuscript Author Mol Biol. Author Manuscript Author manuscript; available in PMC 2018 September 12. Published in final edited form as: Nat Struct Mol Biol. 2017 November ; 24(11): 931–943. doi:10.1038/nsmb.3483. A structural model for microtubule minus-end recognition and protection by CAMSAP proteins Joseph Atherton#1, Kai Jiang#2, Marcel M. Stangier3, Yanzhang Luo4, Shasha Hua2, Klaartje Houben4, Jolien J.E. van Hooff5,6,7, Agnel-Praveen Joseph1, Guido Scarabelli8, Barry J. Grant8, Anthony J. Roberts1, Maya Topf1, Michel O. Steinmetz3,9, Marc Baldus4, Carolyn A. Moores1,#, and Anna Akhmanova2,# 1Institute of Structural and Molecular Biology, Birkbeck, University of London, London, United Kingdom 2Cell Biology, Department of Biology, Faculty of Science, Utrecht University, Utrecht, the Netherlands 3Laboratory of Biomolecular Research, Division of Biology and Chemistry, Paul Scherrer Institut, Villigen PSI, Switzerland 4NMR Spectroscopy, Bijvoet Center for Biomolecular Research, Utrecht University, Utrecht, the Netherlands 5Hubrecht Institute, Utrecht, the Netherlands 6Theoretical Biology and Bioinformatics, Department of Biology, Faculty of Science, Utrecht University, Utrecht, The Netherlands 7Molecular Cancer Research, University Medical Center Utrecht, Utrecht, the Netherlands 8Department of Computational Medicine and Bioinformatics, University of Michigan Medical School, Ann Arbor, Michigan, USA. 9University of Basel, Biozentrum, Basel, Switzerland # These authors contributed equally to this work. Abstract CAMSAP and Patronin family members regulate microtubule minus-end stability and localization and thus organize non-centrosomal microtubule networks, which are essential for cell division, polarization and differentiation. Here, we show that the C-terminal CKK domain of CAMSAPs is widely present among eukaryotes and autonomously recognizes microtubule minus ends.
    [Show full text]