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Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors.

Nair KS, Hanson SM, Kennedy MJ, Hurley JB, Gurevich VV, Slepak VZ
J Biol Chem. 2004 279 (39): 41240-8

PMID: 15272005 · DOI:10.1074/jbc.M406768200

Proper function of visual arrestin is indispensable for rapid signal shut-off in rod photoreceptors. Dramatic light-dependent changes in its subcellular localization are believed to play an important role in light adaptation of photoreceptor cells. Here we show that visual arrestin binds microtubules. The truncated splice variant of visual arrestin, p44, demonstrates dramatically higher affinity for microtubules than the full-length protein (p48). Enhanced microtubule binding of p44 underlies its earlier reported preferential localization to detergent-resistant membranes, where it is anchored via membrane-associated microtubules in a rhodopsin-independent fashion. Experiments with purified proteins demonstrate that arrestin interaction with microtubules is direct and does not require any additional protein partners. Most importantly, arrestin interactions with microtubules and light-activated phosphorylated rhodopsin are mutually exclusive, suggesting that microtubule interaction may play a role in keeping p44 arrestin away from rhodopsin in dark-adapted photoreceptors.

Copyright 2004 American Society for Biochemistry and Molecular Biology, Inc.

MeSH Terms (25)

Alternative Splicing Animals Arrestin Arrestins Cattle Cell Membrane Centrifugation, Density Gradient Chromatography, Affinity Chromatography, Liquid Cytoskeleton Detergents Escherichia coli Light Mass Spectrometry Membrane Microdomains Microtubules Molecular Sequence Data Phosphorylation Photoreceptor Cells Protein Binding Recombinant Proteins Retina Rod Cell Outer Segment Sucrose Time Factors

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