morriswood lab

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.

Preprints:

Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats. (2020) biorXiv, peer review via Review Commons.

A modification to the life cycle of the parasite Trypanosoma brucei. (2019) biorXiv.

Journal articles:

Sajko S, Grishkovskaya I, Kostan J, Graewert M, Setiawan K, Trübestein L, Niedermüller K, Gehin C, Sponga A, Puchinger M, Gavin AC, Leonard TA, Svergun DI, Smith TK, Morriswood B, Djinovic-Carugo K. (2020) Structures of three MORN repeat proteins and a re-evaluation of the proposed lipid-binding properties of MORN repeats.  PLoS ONE

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.

Morriswood B, He CY, Sealey-Cardona M, Yelinek J, Pypaert M, Warren G. The bilobe structure of Trypanosoma brucei contains a MORN-repeat protein. (2009) Mol Biochem Parasitol 167(2):95-103.