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J. Biol. Chem., Vol. 278, Issue 6, 4305-4313, February 7, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/6/4305    most recent M209422200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kosolapov, A. Articles by Deutsch, C. Search for Related Content PubMed PubMed Citation Articles by Kosolapov, A. Articles by Deutsch, C. Social Bookmarking                      What's this?

Folding of the Voltage-gated K⁺ Channel T1 Recognition Domain^*

Andrey Kosolapov and Carol Deutsch

From the Department of Physiology, University of Pennsylvania, Philadelphia, Pennsylvania 19104-6085

Voltage-gated K⁺ channels (Kv) are tetramers whose assembly is coordinated in part by a conserved T1 recognition domain. Although T1 achieves its quaternary structure in the ER, nothing is known about its acquisition of tertiary structure. We developed a new folding assay that relies on intramolecular cross-linking of pairs of cysteines engineered at the folded T1 monomer interface. Using this assay, we show directly that the T1 domain is largely folded while the Kv protein is still attached to membrane-bound ribosomes. The ER membrane facilitates both folding and oligomerization of Kv proteins. We show that folding and oligomerization assays can be used to study coupling between these two biogenic events and diagnose defects in assembly of Kv channels.

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