The Aspergillus nidulans Kinesin-3 Tail Is Necessary And Sufficient To Recognize Modified Microtubules

Ref ID: 18286

Author:

Constanze Seidel, Nadine Zekert and Reinhard Fischer,

Author address:

KIT, Dept. of Microbiology, Karlsruhe, Germany, constanze.seidel@kit.edu

Full conference title:

Asperfest 9

Abstract:

Posttranslational microtubule modifications are numerous; however, the biochemical and cell biological roles of those modifications
remain mostly an enigma. The Aspergillus nidulans kinesin-3 UncA uses preferably modified MTs as tracks for vesicle transportation.
Here, we show that a positively charged region in the tail of UncA (amino acids 1316 to 1402) is necessary for the recognition of
modified MTs. Chimeric proteins composed of the kinesin-1 motor domain and the UncA tail displayed the same specificity as UncA,
suggesting that the UncA tail is sufficient to establish specificity. Interaction between the UncA tail and alpha-tubulin was shown
using a yeast two-hybrid assay and in A. nidulans by bimolecular fluorescence complementation (BiFC). Our data show that
specificity determination depends on the tail rather than the motor domain, as has been demonstrated for kinesin 1 in neuronal cells. In
a non-targeted Y2H approach interaction partners of this region were identified, because they are most likely involved in the
recognition of MT subpopulations. Several candidates were confirmed using BiFC. Two are associated with vesicles; one is a
predicted siderophore uptake transmembrane transporter and the other one was previously shown to be involved in ER to Golgi
vesicle-mediated transport. The deletion of another fished interactor with similarity to Phosphatidylinositol 3- & 4-kinase family
showed strongly reduced growth.

Abstract Number: 34)

Conference Year: 2012

Link to conference website: NULL

New link: NULL

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