Document Detail


An orphan kinesin in trypanosomes cooperates with a kinetoplastid-specific kinesin to maintain cell morphology by regulating subpellicular microtubules.
MedLine Citation:
PMID:  22623724     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Microtubules are a vital part of the cytoskeleton of eukaryotic cells and are involved in various cellular processes. The cytoskeleton of Trypanosoma brucei is characterized by an array of subpellicular microtubules and is essential for maintenance of cell shape and polarity, but little is known about the regulation of the assembly and organization of the subpellicular microtubule corset. Here, we report that the orphan kinesin TbKIN-D regulates the organization of subpellicular microtubules and is required for maintaining cell morphology. TbKIN-D possesses in vitro ATPase activity, associates with cytoskeletal microtubules and is distributed throughout the cytoskeleton at all cell cycle stages. RNAi of TbKIN-D disrupts the organization of the subpellicular microtubule corset and distorts cell morphology, resulting in round cells with an elongated posterior filled with newly assembled microtubules. Depletion of TbKIN-D also abolishes the segregation of organelles and cytoskeletal structures, suggesting that cellular morphogenesis is essential for proper organelle segregation. Moreover, TbKIN-D deficiency impairs the attachment of the new flagellum without compromising the formation of the flagellum attachment zone. Finally, we identified TbKIN-C, a kinetoplastid-specific kinesin known to regulate subpellicular microtubules and cell morphogenesis in T. brucei, as a partner of TbKIN-D. Further, we demonstrate that interaction between TbKIN-C and TbKIN-D requires the coiled-coil motifs in the C-termini of both proteins. Altogether, our results suggest that TbKIN-D cooperates with TbKIN-C to maintain cell morphology by regulating the organization of the subpellicular microtubule corset.
Authors:
Huiqing Hu; Liu Hu; Zhonglian Yu; Amanda E Chasse; Feixia Chu; Ziyin Li
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-05-23
Journal Detail:
Title:  Journal of cell science     Volume:  125     ISSN:  1477-9137     ISO Abbreviation:  J. Cell. Sci.     Publication Date:  2012 Sep 
Date Detail:
Created Date:  2012-10-29     Completed Date:  2013-05-07     Revised Date:  2013-09-03    
Medline Journal Info:
Nlm Unique ID:  0052457     Medline TA:  J Cell Sci     Country:  England    
Other Details:
Languages:  eng     Pagination:  4126-36     Citation Subset:  IM    
Affiliation:
Department of Microbiology and Molecular Genetics, University of Texas Medical School, Houston, TX 77030, USA.
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / metabolism
Amino Acid Sequence
Cell Death
Cell Proliferation
Cell Shape*
Chromatography, Affinity
Flagella / metabolism,  ultrastructure
Kinesin / chemistry,  metabolism*
Microtubules / metabolism*,  ultrastructure
Mitochondria / metabolism,  ultrastructure
Molecular Sequence Data
Negative Staining
Organ Specificity
Protein Binding
Protozoan Proteins / chemistry,  metabolism*
RNA Interference
Trypanosoma brucei brucei / cytology*,  growth & development,  metabolism*,  ultrastructure
Tubulin / metabolism
Tyrosine / metabolism
Grant Support
ID/Acronym/Agency:
AI090070/AI/NIAID NIH HHS; R56 AI090070/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Protozoan Proteins; 0/Tubulin; 55520-40-6/Tyrosine; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/Kinesin
Comments/Corrections

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