Abstract:
:Vacuolar tandem-pore channels could not be analysed in Xenopus oocytes so far, due to misguided translocation. Owing to the conservation of their pore regions, we were able to prepare functional pore-chimeras between the plasma membrane localised TPK4 and vacuolar TPKs. Thereby, we found evidence that TPK2, TPK3 and TPK5, just like TPK4, form potassium-selective channels with instantaneous current kinetics. Homology modelling and mutational analyses identified a pore-located aspartate residue (Asp110), which is involved in potassium permeation as well as in inward rectification of TPK4. Furthermore, dominant-negative mutations in the selectivity filter of either pore one or two (Asp86,Asp200) rendered TPK4 non-functional. This observation supports the notion that the functional TPK4 channel complex is formed by two subunits.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Marcel D,Müller T,Hedrich R,Geiger Ddoi
10.1016/j.febslet.2010.04.038subject
Has Abstractpub_date
2010-06-03 00:00:00pages
2433-9issue
11eissn
0014-5793issn
1873-3468pii
S0014-5793(10)00322-4journal_volume
584pub_type
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