RGD Reference Report - Changes in activation gating of IsK potassium currents brought about by mutations in the transmembrane sequence. - Rat Genome Database

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Changes in activation gating of IsK potassium currents brought about by mutations in the transmembrane sequence.

Authors: Wilson, GG  Sivaprasadarao, A  Findlay, JB  Wray, D 
Citation: Wilson GG, etal., FEBS Lett. 1994 Oct 24;353(3):251-4.
RGD ID: 7243866
Pubmed: PMID:7957868   (View Abstract at PubMed)

Expression of the rat kidney IsK protein in Xenopus oocytes produces slowly-activating potassium channel currents. We have investigated the relationship between structure and function of the single putative membrane-spanning domain using site-directed mutagenesis. Six mutants were constructed in which consecutive individual amino acids (53 to 58) of the transmembrane region were substituted by cysteine. Expression of four of these mutants in Xenopus oocytes resulted in currents which were similar to wild-type. However, for one mutant (position 55) activation curves were shifted in a hyperpolarising direction and for another mutant (position 58) activation curve were shifted in a depolarising direction. This suggests that the hydrophobic phenylalanine residues at positions 55 and 58 may play a critical role in IsK activation gating. This spacing of functional amino acids at every third residue may indicate an alpha-helical conformation for the membrane-spanning domain of IsK. Furthermore, these results also indicate that one face of the helix may represent a region of subunit association.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Kcne1Ratpositive regulation of potassium ion transmembrane transport  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Kcne1  (potassium voltage-gated channel subfamily E regulatory subunit 1)


Additional Information