Deutsch
    Chair of Cell and Developmental Biology (Zoology I)

    MORRISWOOD LAB

    We study the eukaryotic cytoskeleton and motor proteins

    Research synopsis

    The eukaryotic cytoskeleton is composed of three main types of filaments:

    microfilaments (actin)

    microtubules

    intermediate filaments

    These filaments can be stable or dynamic, and are responsible not only for maintaining cell architecture but also for a plethora of cellular functions that interface with the membrane trafficking and signal transduction networks amongst others. Motor proteins use the filaments as tracks for the transport of intracellular cargo, be it multiprotein complexes or vesicles.

    Trypanosomatids are a particularly interesting system for the study of the cytoskeleton for a number of reasons.

    Firstly, as the causative agents of several neglected tropical diseases (sleeping sickness, Chagas disease, Leishmaniasis) there is a need for new therapeutic strategies, and the cytoskeleton is essential to the viability of the cells. Study of the ways in which the cytoskeleton performs its many cellular functions will both add to biological knowledge and illuminate areas for possible drug development.

    Secondly, as descendants of an early-branching eukaryote they are likely to exhibit both conserved and novel features in their cytoskeleton (for instance, there are no intermediate filament proteins encoded in their genomes), making them an important reference in evolutionary cell biology studies, and a source of cytoskeletal diversity.

    Thirdly, like many parasites, they boast a streamlined cellular physiology, making them ideal model systems for a number of fundamental questions in eukaryotic biology.

     

    Recent publications

    Morriswood B, Engstler M. Let's get fISSical: fast in silico synchronization

    as a new tool for cell division cycle analysis. (2017) Parasitology. Feb 7:1-14.

    Cicova Z, Dejung M, Skalicky T, Eisenhuth N, Hanselmann S, Morriswood B, Figueiredo LM, Butter F, Janzen CJ. (2016) Two flagellar BAR domain proteins in Trypanosoma brucei with stage-specific regulation. Sci Rep. 6:35826.

    Vidilaseris K, Lesigang J, Morriswood B, Dong G. Assembly mechanism of Trypanosoma brucei BILBO1 at the flagellar pocket collar. (2015) Commun Integr Biol.8(1):e992739.  

    Morriswood B. Form, Fabric, and Function of a Flagellum-Associated Cytoskeletal Structure. (2015) Cells. 4(4):726-47.

    Morriswood B, Schmidt K. A MORN Repeat Protein Facilitates Protein Entry into the Flagellar Pocket of Trypanosoma brucei. (2015) Eukaryot Cell. 14(11):1081-93.

    Vidilaseris K, Shimanovskaya E, Esson HJ, Morriswood B, Dong G. Assembly mechanism of Trypanosoma brucei BILBO1, a multidomain cytoskeletal protein. (2014) J Biol Chem. 289(34):23870-81.

    Vidilaseris K, Morriswood B, Kontaxis G, Dong G. Structure of the TbBILBO1 protein N-terminal domain from Trypanosoma brucei reveals an essential requirement for a conserved surface patch. (2014) J Biol Chem. 289(6):3724-35.  

    Morriswood B, Warren G. Cell biology. Stalemate in the Golgi battle. (2013) Science. 341(6153):1465-6.  

    Morriswood B, Havlicek K, Demmel L, Yavuz S, Sealey-Cardona M, Vidilaseris K, Anrather D, Kostan J, Djinovic-Carugo K, Roux KJ, Warren G. Novel bilobe components in Trypanosoma brucei identified using proximity-dependent biotinylation. (2013) Eukaryot Cell. 12(2):356-67.  

    Esson HJ, Morriswood B, Yavuz S, Vidilaseris K, Dong G, Warren G. Morphology of the trypanosome bilobe, a novel cytoskeletal structure. (2012) Eukaryot Cell. 11(6):761-72.

    RESEARCH TOPICS

    The hook complex is a cytoskeleton-associated structure coiled around the flagellar pocket neck.

     

    Trypanosomes have an extremely reduced actomyosin system – but what is its function?

     

    Contact

    Lehrstuhl für Zoologie I - Zell- und Entwicklungsbiologie
    Am Hubland
    97074 Würzburg

    Phone: +49 931 31-84250
    Fax: +49 931 31-84252
    Email

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    Hubland Süd, Geb. B1 Hubland Nord, Geb. 32 Julius-von-Sachs-Platz 2 Fabrikschleichach Hubland Süd, Geb. B2 Campus Medizin