Literature DB >> 8706877

Do voltage-gated Kv1.1 and inward rectifier Kir2.1 potassium channels form heteromultimers?

J Tytgat1, G Buyse, J Eggermont, G Droogmans, B Nilius, P Daenens.   

Abstract

Possible heteromultimer formation between Kv- and Kir-type K+ channels was investigated, in connection with the known functional diversity of K+ channels in vivo. Voltage-clamp experiments were performed on Xenopus oocytes, either injected with concatenated Kir2.1-Kv1.1 mRNA, or co-injected with Kv1.1 and Kir2.1 mRNA. K+ currents could be approximated by the algebraic sum of the 2 K+ current types alone. The tandem construct did not show functional expression, although it could be detected by Western blotting. We conclude that Kv1.1 and Kir2.1 alpha-subunit proteins fail to assemble and do not contribute functional diversity to K+ channels.

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Year:  1996        PMID: 8706877     DOI: 10.1016/0014-5793(96)00674-6

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

1.  Kir2.4 and Kir2.1 K(+) channel subunits co-assemble: a potential new contributor to inward rectifier current heterogeneity.

Authors:  Gernot Schram; Peter Melnyk; Marc Pourrier; Zhiguo Wang; Stanley Nattel
Journal:  J Physiol       Date:  2002-10-15       Impact factor: 5.182

2.  Assembly of ROMK1 (Kir 1.1a) inward rectifier K+ channel subunits involves multiple interaction sites.

Authors:  J C Koster; K A Bentle; C G Nichols; K Ho
Journal:  Biophys J       Date:  1998-04       Impact factor: 4.033

3.  BmTx3, a scorpion toxin with two putative functional faces separately active on A-type K+ and HERG currents.

Authors:  Isabelle Huys; Chen-Qi Xu; Cheng-Zhong Wang; Hélène Vacher; Marie-France Martin-Eauclaire; Cheng-Wu Chi; Jan Tytgat
Journal:  Biochem J       Date:  2004-03-15       Impact factor: 3.857

  3 in total

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