A 240 kDa protein represents the complete β subunit of the cyclic nucleotide-gated channel from rod photoreceptor

Heinz Gerd Körschen, Michelle Illing, Reinhard Seifer, Federico Sesti, Andrew Williams, Sebastian Gotzes, Caroline Colville, Frank Muller, Andrea Dosé, Matthias Godde, Laurie Molday, U. Benjamin Kaupp, Robert S. Molday

Research output: Contribution to journalArticlepeer-review

198 Scopus citations

Abstract

The cyclic nucleotide-gated channel from rod photoreceptors is composed of two distinct subunits (α and β). The properties of the a subunit, which can form functional channels by itself, are modified by coexpression with a homologous polypeptide, designated the β subunit. However, the α subunit from rod photoreceptor membranes copurifies with a 240 kDa protein that is significantly larger than this putative β subunit. We now demonstrate by peptide sequencing and by cloning and functional expression of cDNA that the 240 kDa protein represents the complete β subunit with an unusual bipartite structure. The N-terminal part is essentially identical to a glutamic acid-rich protein (GARP), whereas the C-terminal part is highly homologous to the previously cloned human "β subunit." Expression of the complete β subunit in HEK 293 cells results in a polypeptide with the same apparent molecular weight as the 240 kDa protein of the native rod channel. Coexpression of the α subunit with the fulllength β subunit yields hetero-oligomeric channels with properties characteristic of the native channel.

Original languageEnglish (US)
Pages (from-to)627-636
Number of pages10
JournalNeuron
Volume15
Issue number3
DOIs
StatePublished - Sep 1995
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)

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