Slo1 Caveolin-binding Motif, a Mechanism of Caveolin-1-Slo1 Interaction Regulating Slo1 Surface Expression.

Slo1 Caveolin-binding Motif, a Mechanism of Caveolin-1-Slo1 Interaction Regulating Slo1 Surface Expression. Research Abstract Details 

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Slo1 Caveolin-binding Motif, a Mechanism of Caveolin-1-Slo1 Interaction Regulating Slo1 Surface Expression. Abstract Text:

Abderrahmane Alioua,Rong Lu,Yogesh Kumar,Mansoureh Eghbali,Pallob Kundu,Ligia Toro,Enrico Stefani,

The large conductance, voltage- and Ca(2+)-activated potassium (MaxiK, BK) channel and caveolin-1 play important roles in regulating vascular contractility. Here, we hypothesized that the MaxiK alpha-subunit (Slo1) and caveolin-1 may interact with each other. Slo1 and caveolin-1 physiological association in native vascular tissue is strongly supported by (i) detergent-free purification of caveolin-1-rich domains demonstrating a pool of aortic Slo1 co-migrating with caveolin-1 to light density sucrose fractions, (ii) reverse co-immunoprecipitation, and (iii) double immunolabeling of freshly isolated myocytes revealing caveolin-1 and Slo1 proximity at the plasmalemma. In HEK293T cells, Slo1-caveolin-1 association was unaffected by the smooth muscle MaxiK beta1-subunit. Sequence analysis revealed two potential caveolin-binding motifs along the Slo1 C terminus, one equivalent, (1007)YNMLCFGIY(1015), and another mirror image, (537)YTEYLSSAF(545), to the consensus sequence, varphiXXXXvarphiXXvarphi. Deletion of (1007)YNMLCFGIY(1015) caused approximately 80% loss of Slo1-caveolin-1 association while preserving channel normal folding and overall Slo1 and caveolin-1 intracellular distribution patterns. (537)YTEYLSSAF(545) deletion had an insignificant dissociative effect. Interestingly, caveolin-1 coexpression reduced Slo1 surface and functional expression near 70% without affecting channel voltage sensitivity, and deletion of (1007)YNMLCFGIY(1015) motif obliterated channel surface expression. The results suggest (1007)YNMLCFGIY(1015) possible participation in Slo1 plasmalemmal targeting and demonstrate its role as a main mechanism for caveolin-1 association with Slo1 potentially serving a dual role: (i) maintaining channels in intracellular compartments downsizing their surface expression and/or (ii) serving as anchor of plasma membrane resident channels to caveolin-1-rich membranes. Because the caveolin-1 scaffolding domain is juxtamembrane, it is tempting to suggest that Slo1-caveolin-1 interaction facilitates the tethering of the Slo1 C-terminal end to the membrane.

Slo1 Caveolin-binding Motif, a Mechanism of Caveolin-1-Slo1 Interaction Regulating Slo1 Surface Expression. Publishing Authors By Initials

A Alioua,R Lu,Y Kumar,M Eghbali,P Kundu,L Toro,E Stefani,

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Slo1 Caveolin-binding Motif, a Mechanism of Caveolin-1-Slo1 Interaction Regulating Slo1 Surface Expression. Journal Published:

PUBLICATION TYPE: Journal Article

Journal: The Journal of biological chemistry

VOLUME: 283

Page Numbers: 4808-17

Journal Abbreviation: J. Biol. Chem.

ISSN: 0021-9258

DAY: 12

MONTH: 12

YEAR: 2007

Slo1 Caveolin-binding Motif, a Mechanism of Caveolin-1-Slo1 Interaction Regulating Slo1 Surface Expression. Information

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LANGUAGE: eng

NlmUniqueID: 2985121

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Grant and Affiliation Information for Slo1 Caveolin-binding Motif, a Mechanism of Caveolin-1-Slo1 Interaction Regulating Slo1 Surface Expression.

AFFILIATION: Departments of Anesthesiology, Molecular & Medical Pharmacology, and Physiology.

Country: United States

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MEDLINETA: J Biol Chem

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