@article{Morriswood2015,
  author    = {Morriswood, Brooke},
  title     = {Form, fabric, and function of a flagellum-associated cytoskeletal structure.},
  series = {Cells},
  volume    = {4},
  journal   = {Cells},
  number    = {4},
  doi       = {10.3390/cells4040726},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-149467},
  pages     = {726-747},
  year      = {2015},
  abstract  = {Trypanosoma brucei is a uniflagellated protist and the causative agent of African trypanosomiasis, a neglected tropical disease. The single flagellum of T. brucei is essential to a number of cellular processes such as motility, and has been a longstanding focus of scientific enquiry. A number of cytoskeletal structures are associated with the flagellum in T. brucei, and one such structure—a multiprotein complex containing the repeat motif protein TbMORN1—is the focus of this review. The TbMORN1-containing complex, which was discovered less than ten years ago, is essential for the viability of the mammalian-infective form of T. brucei. The complex has an unusual asymmetric morphology, and is coiled around the flagellum to form a hook shape. Proteomic analysis using the proximity-dependent biotin identification (BioID) technique has elucidated a number of its components. Recent work has uncovered a role for TbMORN1 in facilitating protein entry into the cell, thus providing a link between the cytoskeleton and the endomembrane system. This review summarises the extant data on the complex, highlights the outstanding questions for future enquiry, and provides speculation as to its possible role in a size-exclusion mechanism for regulating protein entry. The review additionally clarifies the nomenclature associated with this topic, and proposes the adoption of the term "hook complex" to replace the former name "bilobe" to describe the complex.},
  language  = {en}
}
@article{CicovaDejungSkalickyetal.2016,
  author    = {Cicova, Zdenka and Dejung, Mario and Skalicky, Tomas and Eisenhuth, Nicole and Hanselmann, Steffen and Morriswood, Brooke and Figueiredo, Luisa M. and Butter, Falk and Janzen, Christian J.},
  title     = {Two flagellar BAR domain proteins in Trypanosoma brucei with stage-specific regulation},
  series = {Scientific Reports},
  volume    = {6},
  journal   = {Scientific Reports},
  doi       = {10.1038/srep35826},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-181021},
  year      = {2016},
  abstract  = {Trypanosomes are masters of adaptation to different host environments during their complex life cycle. Large-scale proteomic approaches provide information on changes at the cellular level, and in a systematic way. However, detailed work on single components is necessary to understand the adaptation mechanisms on a molecular level. Here, we have performed a detailed characterization of a bloodstream form (BSF) stage-specific putative flagellar host adaptation factor Tb927.11.2400, identified previously in a SILAC-based comparative proteome study. Tb927.11.2400 shares 38\% amino acid identity with TbFlabarin (Tb927.11.2410), a procyclic form (PCF) stage-specific flagellar BAR domain protein. We named Tb927.11.2400 TbFlabarin-like (TbFlabarinL), and demonstrate that it originates from a gene duplication event, which occurred in the African trypanosomes. TbFlabarinL is not essential for the growth of the parasites under cell culture conditions and it is dispensable for developmental differentiation from BSF to the PCF in vitro. We generated TbFlabarinL-specific antibodies, and showed that it localizes in the flagellum. Co-immunoprecipitation experiments together with a biochemical cell fractionation suggest a dual association of TbFlabarinL with the flagellar membrane and the components of the paraflagellar rod.},
  language  = {en}
}