Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 41240-41248 |
| Number of pages | 9 |
| Journal | Journal of Biological Chemistry |
| Volume | 279 |
| Issue number | 39 |
| DOIs | |
| State | Published - Sep 24 2004 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors. / Nair, K. Saidas; Hanson, Susan M.; Kennedy, Matthew J.; Hurley, James B.; Gurevich, Vsevolod V.; Slepak, Vladlen Z.
In: Journal of Biological Chemistry, Vol. 279, No. 39, 24.09.2004, p. 41240-41248.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors
AU - Nair, K. Saidas
AU - Hanson, Susan M.
AU - Kennedy, Matthew J.
AU - Hurley, James B.
AU - Gurevich, Vsevolod V.
AU - Slepak, Vladlen Z
PY - 2004/9/24
Y1 - 2004/9/24
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.M406768200
DO - 10.1074/jbc.M406768200
M3 - Article
VL - 279
SP - 41240
EP - 41248
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 39
ER -