Caveolin interaction governs Kv1.3 lipid raft targeting

Perez-Verdaguer, Mireia, Capera, Jesusa, Martinez-Marmol, Ramon, Camps, Marta, Comes, Nuria, Tamkun, Michael M. and Felipe, Antonio (2016) Caveolin interaction governs Kv1.3 lipid raft targeting. Scientific Reports, 6 . doi:10.1038/srep22453

Author Perez-Verdaguer, Mireia
Capera, Jesusa
Martinez-Marmol, Ramon
Camps, Marta
Comes, Nuria
Tamkun, Michael M.
Felipe, Antonio
Title Caveolin interaction governs Kv1.3 lipid raft targeting
Journal name Scientific Reports   Check publisher's open access policy
ISSN 2045-2322
Publication date 2016-03-02
Year available 2016
Sub-type Article (original research)
DOI 10.1038/srep22453
Open Access Status DOI
Volume 6
Total pages 12
Place of publication London, United Kingdom
Publisher Nature Publishing Group
Language eng
Subject 1000 General
Abstract The spatial localization of ion channels at the cell surface is crucial for their functional role. Many channels localize in lipid raft microdomains, which are enriched in cholesterol and sphingolipids. Caveolae, specific lipid rafts which concentrate caveolins, harbor signaling molecules and their targets becoming signaling platforms crucial in cell physiology. However, the molecular mechanisms involved in such spatial localization are under debate. Kv1.3 localizes in lipid rafts and participates in the immunological response. We sought to elucidate the mechanisms of Kv1.3 surface targeting, which govern leukocyte physiology. Kv1 channels share a putative caveolin-binding domain located at the intracellular N-terminal of the channel. This motif, lying close to the S1 transmembrane segment, is situated near the T1 tetramerization domain and the determinants involved in the Kvβ subunit association. The highly hydrophobic domain (FQRQVWLLF) interacts with caveolin 1 targeting Kv1.3 to caveolar rafts. However, subtle variations of this cluster, putative ancillary associations and different structural conformations can impair the caveolin recognition, thereby altering channel's spatial localization. Our results identify a caveolin-binding domain in Kv1 channels and highlight the mechanisms that govern the regulation of channel surface localization during cellular processes.
Keyword Caveolins
Lipid rafts
Lipid raft targeting
Lipid raft microdomains
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status UQ

Document type: Journal Article
Sub-type: Article (original research)
Collections: HERDC Pre-Audit
Queensland Brain Institute Publications
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