Please use this identifier to cite or link to this item: https://doi.org/10.1242/jcs.11362
Title: An intracellular membrane junction consisting of flagellum adhesion glycoproteins links flagellum biogenesis to cell morphogenesis in Trypanosoma brucei
Authors: Sun, S.Y.
Wang, C.
Yuan, Y.A. 
He, C.Y. 
Keywords: Cell morphogenesis
Flagellum
Flagellum adhesion proteins
Flagellum attachment zone (FAZ)
Trypanosoma brucei
Issue Date: Jan-2013
Citation: Sun, S.Y.,Wang, C.,Yuan, Y.A.,He, C.Y. (2013-01). An intracellular membrane junction consisting of flagellum adhesion glycoproteins links flagellum biogenesis to cell morphogenesis in Trypanosoma brucei. Journal of Cell Science 126 (2) : 520-531. ScholarBank@NUS Repository. https://doi.org/10.1242/jcs.11362
Abstract: African trypanosomes have a single, membrane-bounded flagellum that is attached to the cell cortex by membrane adhesion proteins and an intracellular flagellum attachment zone (FAZ) complex. The coordinated assembly of flagellum and FAZ, during the cell cycle and the life cycle development, plays a pivotal role in organelle positioning, cell division and cell morphogenesis. To understand how the flagellum and FAZ assembly are coordinated, we examined the domain organization of the flagellum adhesion protein 1 (FLA1), a glycosylated, transmembrane protein essential for flagellum attachment and cell division. By immunoprecipitation of a FLA1-truncation mutant that mislocalized to the flagellum, a novel FLA1-binding protein (FLA1BP) was identified in procyclic Trypanosoma brucei. The interaction between FLA1 on the cell membrane and FLA1BP on the flagellum membrane acts like a molecular zipper, joining flagellum membrane to cell membrane and linking flagellum biogenesis to FAZ elongation. By coordinating flagellum and FAZ assembly during the cell cycle, morphology information is transmitted from the flagellum to the cell body. © 2013. Published by The Company of Biologists Ltd.
Source Title: Journal of Cell Science
URI: http://scholarbank.nus.edu.sg/handle/10635/100072
ISSN: 00219533
DOI: 10.1242/jcs.11362
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