Kcv (K+ Chlorella virus) is a miniature virus-encoded K+ channel. Its predicted membrane-pore-membrane structure lacks a cytoplasmic C-terminus and it has a short 12 amino acid (aa) cytoplasmic N-terminus. Kcv forms a functional channel when expressed in human HEK 293 cells. Deletion of the 14 N-terminal aa results in no apparent differences in the subcellular location and expression level of the Kcv protein. However, the truncated protein does not induce a measurable current in transfected HEK 293 cells or Xenopus oocytes. We conclude that the N-terminus controls functional properties of the Kcv channel, but does not influence protein expression.

The short N-terminus is required for functioanl expression of the virus encoded miniature K+ channel Kcv / A. Moroni, C. Viscomi, V. Sangiorgio, C. Pagliuca, T. Meckel, F. Horvath, S. Gazzarrini, P. Valbuzzi, J.L. Van Etten, D. DiFrancesco, G. Thiel. - In: FEBS LETTERS. - ISSN 0014-5793. - 530:1-3(2002), pp. 65-69. [10.1016/S0014-5793(02)03397-5]

The short N-terminus is required for functioanl expression of the virus encoded miniature K+ channel Kcv

A. Moroni
Primo
;
S. Gazzarrini;D. Difrancesco
Penultimo
;
2002

Abstract

Kcv (K+ Chlorella virus) is a miniature virus-encoded K+ channel. Its predicted membrane-pore-membrane structure lacks a cytoplasmic C-terminus and it has a short 12 amino acid (aa) cytoplasmic N-terminus. Kcv forms a functional channel when expressed in human HEK 293 cells. Deletion of the 14 N-terminal aa results in no apparent differences in the subcellular location and expression level of the Kcv protein. However, the truncated protein does not induce a measurable current in transfected HEK 293 cells or Xenopus oocytes. We conclude that the N-terminus controls functional properties of the Kcv channel, but does not influence protein expression.
Chlorella virus PBCV-1; HEK 293 cell; K+ channel; Kcv
Settore BIO/04 - Fisiologia Vegetale
Settore BIO/09 - Fisiologia
2002
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2434/29363
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