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SUMMARY:Molecular characterization of the Flagellar Pocket Collar cytoskel
 etal of the protozoan parasite Trypanosoma brucei - Prof Derrick Robinson\
 , CNRS\, University of Bordeaux\, France
DTSTART:20170614T150000Z
DTEND:20170614T160000Z
UID:TALK66917@talks.cam.ac.uk
CONTACT:Mark Carrington
DESCRIPTION:Trypanosoma brucei\, Trypanosoma cruzi and Leishmania species 
 are protozoan parasites that cause Human African Trypanosomiasis\, Chagas 
 disease and Leishmaniasis\, respectively. A common feature among these kin
 etoplast-containing parasites is the modification of cell shape during the
 ir life cycle. This involves important changes in the cytoskeleton and dup
 lication and re-positioning of the single copy organelles. The cytoskeleto
 n of these parasites is primarily based on a closely-knit helical microtub
 ule array. Actin filaments have not been observed and no intermediate fila
 ment genes have been identified. \n\nDue to this microtubule-based cytoske
 leton T. brucei has a polarized cell biology\, which has positive and nega
 tive morphological aspects to it. Positive aspects are that it is very sta
 ble and probably easily and rapidly modified for differentiation but on th
 e other hand there is little room for endo and exocytosis. The array is on
 ly perforated at one point by a unique structure in the posterior of the c
 ell called the flagellar pocket (FP) from which the flagellum emerges. Not
  surprisingly\, the FP is also the exclusive region for endo- and exocytic
  activity.  The FP has a unique ring-shaped cytoskeleton at its origin cal
 led the flagellar pocket collar (FPC)\, which is also attached to the flag
 ellum at the site where the flagellum exits the cell. The only known prote
 in present at\, and within\, the FPC is the essential protein TbBILBO1- a 
 ring forming and precious protein. \n\nUsing a yeast-two-hybrid (Y2H) scre
 en with TbBILBO1 as bait\, we obtained new data that allowed the laborator
 y to assemble a list of putative TbBILBO1 interacting protein partners and
  these are currently being characterized to identify function\, form and l
 ocation.  In this presentation I will discuss some of the properties and c
 urrent thinking of the role(s) and organization of the FPC\, its main comp
 onent protein TbBILBO1 and some of its binding partners.
LOCATION:Greaves Room\, Department of Pathology
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