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Rhodopsin’s Carboxy-Terminal Cytoplasmic Tail Acts as a Membrane Receptor for Cytoplasmic Dynein by Binding to the Dynein Light Chain Tctex-1

Open access
Tai, Andrew W, Chuang, Jen-Zen, Bode, Christian, Wolfrum, Uwe, Sung, Ching-Hwa·1999·Cell

Abstract

The interaction of cytoplasmic dynein with its cargoes is thought to be indirectly mediated by dynactin, a complex that binds to the dynein intermediate chain. However, the roles of other dynein subunits in cargo binding have been unknown. Here we demonstrate that dynein translocates rhodopsin-bearing vesicles along microtubules. This interaction occurs directly between the C-terminal cytoplasmic tail of rhodopsin and Tctex-1, a dynein light chain. C-terminal rhodopsin mutations responsible for retinitis pigmentosa inhibit this interaction. Our results point to an alternative docking mechanism for cytoplasmic dynein, provide novel insights into the role of motor proteins in the polarized transport of post-Golgi vesicles, and shed light on the molecular basis of retinitis pigmentosa.

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Metadata

Authors
Tai, A. W., Chuang, J.-Z., Bode, C., Wolfrum, U., & Sung, C.-H.
Venue
Cell
Publisher
Elsevier BV
Published
1999-06
Volume
97
Issue
7
Pages
877-887
ISSN
0092-8674 (ISSN-L)
OpenAlex
W2118200380
Cited by
478
References
0
FWCI
13.02
Type
journal article
Language
en
Open access
hybrid

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CoChat. (2026). Citation check: Rhodopsin’s Carboxy-Terminal Cytoplasmic Tail Acts as a Membrane Receptor for Cytoplasmic Dynein by Binding to the Dynein Light Chain Tctex-1. https://app.cochat.ai/papers/10.1016/s0092-8674(00)80800-4
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Tai, A. W., Chuang, J.-Z., Bode, C., Wolfrum, U., & Sung, C.-H. (1999). Rhodopsin’s Carboxy-Terminal Cytoplasmic Tail Acts as a Membrane Receptor for Cytoplasmic Dynein by Binding to the Dynein Light Chain Tctex-1. Cell. https://doi.org/10.1016/s0092-8674(00)80800-4

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