http://www.cnr.it/ontology/cnr/individuo/prodotto/ID9771

The Role of the C-Terminus for Functional Heteromerization of the Plant Channel KDC1 (Articolo in rivista)

Type

Prodotto della ricerca (Classe)
Articolo in rivista (Classe)

Label

The Role of the C-Terminus for Functional Heteromerization of the Plant Channel KDC1 (Articolo in rivista) (literal)

Anno

2009-01-01T00:00:00+01:00 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi

10.1016/j.bpj.2009.02.055 (literal)

Alternative label

Naso A; Dreyer I; Pedemonte L; Testa I; Gomez-Porras JL; Usai C; Mueller-Rueber B; Diaspro A; Gambale F; Picco C (2009)
The Role of the C-Terminus for Functional Heteromerization of the Plant Channel KDC1
in Biophysical journal (Print)
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Naso A; Dreyer I; Pedemonte L; Testa I; Gomez-Porras JL; Usai C; Mueller-Rueber B; Diaspro A; Gambale F; Picco C (literal)

Pagina inizio

4063 (literal)

Pagina fine

4074 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#url

http://www.sciencedirect.com/science/article/pii/S0006349509006717 (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume

96 (literal)

Rivista

Biophysical journal (Rivista)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroFascicolo

10 (literal)

Note

ISI Web of Science (WOS) (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

Univ Potsdam, Inst Biochem & Biol, Mol Biol Abt, Heisenberg Grp BPMPB, D-14476 Potsdam, Germany CNR, Ist Biofis, I-16149 Genoa, Italy Univ Genoa, LAMBS MicroScoBio, I-16146 Genoa, Italy Univ Genoa, IFOM Res Ctr, Dept Phys, I-16146 Genoa, Italy (literal)

Titolo

The Role of the C-Terminus for Functional Heteromerization of the Plant Channel KDC1 (literal)

Abstract

Voltage-gated potassium channels are formed by the assembly of four identical (homotetramer) or different (heterotetramer) subunits. Tetramerization of plant potassium channels involves the C-terminus of the protein. We investigated the role of the C-terminus of KDC1, a Shaker-like inward-rectifying K(+) channel that does not form functional homomeric channels, but participates in the formation of heteromeric complexes with other potassium alpha-subunits when expressed in Xenopus oocytes. The interaction of KDC1 with KAT1 was investigated using the yeast two-hybrid system, fluorescence and electrophysiological studies. We found that the KDC1-EGFP fusion protein is not targeted to the plasma membrane of Xenopus oocytes unless it is coexpressed with KAT1. Deletion mutants revealed that the KDC1 C-terminus is involved in heteromerization. Two domains of the C-terminus, the region downstream the putative cyclic nucleotide binding domain and the distal part of the C-terminus called K(HA) domain, contributed to a different extent to channel assembly. Whereas the first interacting region of the C-terminus was necessary for channel heteromerization, the removal of the distal KHA domain decreased but did not abolish the formation of heteromeric complexes. Similar results were obtained when coexpressing KDC1 with the KAT1-homolog KDC2 from carrots, thus indicating the physiological significance of the KAT1/KDC1 characterization. Electrophysiological experiments showed furthermore that the heteromerization capacity of KDC1 was negatively influenced by the presence of the enhanced green fluorescence protein fusion. (literal)

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