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Giardia lamblia EB1 is a functional homolog of yeast Bim1p that binds to microtubules

Authors
 Juri Kim  ;  Seobo Sim  ;  Junwon Kim  ;  Kiwon Song  ;  Tai-Soon Yong  ;  Soon-Jung Park 
Citation
 PARASITOLOGY INTERNATIONAL, Vol.57(4) : 465-471, 2008 
Journal Title
 PARASITOLOGY INTERNATIONAL 
ISSN
 1383-5769 
Issue Date
2008
MeSH
Animals ; Cell Cycle Proteins*/chemistry ; Cell Cycle Proteins*/genetics ; Cell Cycle Proteins*/metabolism ; Genetic Complementation Test* ; Giardia lamblia/genetics ; Giardia lamblia/growth & development ; Giardia lamblia/metabolism* ; Humans ; Microtubule Proteins*/chemistry ; Microtubule Proteins*/genetics ; Microtubule Proteins*/metabolism ; Microtubule-Associated Proteins*/chemistry ; Microtubule-Associated Proteins*/genetics ; Microtubule-Associated Proteins*/metabolism ; Microtubules/metabolism* ; Mutation ; Protozoan Proteins/chemistry ; Protozoan Proteins/genetics ; Protozoan Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/growth & development ; Saccharomyces cerevisiae/metabolism* ; Saccharomyces cerevisiae Proteins*/chemistry ; Saccharomyces cerevisiae Proteins*/genetics ; Saccharomyces cerevisiae Proteins*/metabolism
Keywords
Microtubule ; EB1 ; Bim1p ; Microtubule-associated protein ; Giardia lamblia
Abstract
Giardia lamblia, with two nuclei and a distinct polarized morphology, is an interesting organism for investigating how distribution of its microtubule (MT) is controlled during its cell cycle. In this study, we identified the end-binding protein 1 (EB1) of G. lamblia, a well-known microtubule-associated protein that organizes MTs in eukaryotes. Immunofluorescence assays using recombinant EB1 (rEB1)-specific antibodies demonstrated EB1 localization in nuclear membrane as well as in some cytoskeletal structures such as axomenes and median bodies of trophozoites of G. lamblia. Complementation experiments using the BIM1 knock-out mutant of yeast, the yeast homolog of mammalian EB1, showed that giardial EB1 was able to carry out a homologous function in controlling MT dynamics. In addition, rEB1 of G. lamblia co-precipitated with MTs by an in vitro binding assay, thereby demonstrating that G. lamblia EB1 is a MT-associated protein. These results, taken together, suggest that G. lamblia EB1 is a functional homolog of eukaryotic EB1 and is likely to be a determinant for MT distribution.
Full Text
http://www.sciencedirect.com/science/article/pii/S1383576908000780
DOI
10.1016/j.parint.2008.05.008
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Environmental Medical Biology (환경의생물학교실) > 1. Journal Papers
Yonsei Authors
Kim, Ju Ri(김주리) ORCID logo https://orcid.org/0000-0001-8270-7584
Park, Soon Jung(박순정) ORCID logo https://orcid.org/0000-0002-0423-1944
Yong, Tai Soon(용태순) ORCID logo https://orcid.org/0000-0002-3445-0769
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/108577
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