The bi-lobe-associated LRRP1 regulates Ran activity in Trypanosoma brucei.

Abstract:

:Cilia and flagella are conserved eukaryotic organelles important for motility and sensory. The RanGTPase, best known for nucleocytoplasmic transport functions, may also play a role in protein trafficking into the specialized flagellar/ciliary compartments, although the regulatory mechanisms controlling Ran activity at the flagellum remain unclear. The unicellular parasite Trypanosoma brucei contains a single flagellum necessary for cell movement, division and morphogenesis. Correct flagellum functions require flagellar attachment to the cell body, which is mediated by a specialized flagellum attachment zone (FAZ) complex that is assembled together with the flagellum during the cell cycle. We have previously identified the leucine-rich-repeat protein 1 LRRP1 on a bi-lobe structure at the proximal base of flagellum and FAZ. LRRP1 is essential for bi-lobe and FAZ biogenesis, consequently affecting flagellum-driven cell motility and division. Here, we show that LRRP1 forms a complex with Ran and a Ran-binding protein, and regulates Ran-GTP hydrolysis in T. brucei. In addition to mitotic inhibition, depletion of Ran inhibits FAZ assembly in T. brucei, supporting the presence of a conserved mechanism that involves Ran in the regulation of flagellum functions in an early divergent eukaryote.

journal_name

J Cell Sci

journal_title

Journal of cell science

authors

Brasseur A,Bayat S,Chua XL,Zhang Y,Zhou Q,Low BC,He CY

doi

10.1242/jcs.148015

subject

Has Abstract

pub_date

2014-11-15 00:00:00

pages

4846-56

issue

Pt 22

eissn

0021-9533

issn

1477-9137

pii

jcs.148015

journal_volume

127

pub_type

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