Rhodopsin’s carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1

Autoren

AW Tai
JZ Chuang
C Bode
U Wolfrum
CH Sung

Autoren-URL

https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000081162800009&DestLinkType=FullRecord&DestApp=WOS_CPL

DOI

10.1016/S0092-8674(00)80800-4

eISSN

1097-4172

Externe Identifier

Clarivate Analytics Document Solution ID: 211LP
PubMed Identifier: 10399916

ISSN

0092-8674

Ausgabe der Veröffentlichung

7

Zeitschrift

CELL

Paginierung

877 - 887

Datum der Veröffentlichung

1999

Status

Published

Titel

Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1

Sub types

Article

Ausgabe der Zeitschrift

97

Datenquelle: Web of Science (Lite)

Autoren

Andrew W Tai
Jen-Zen Chuang
Christian Bode
Uwe Wolfrum
Ching-Hwa Sung

DOI

10.1016/s0092-8674(00)80800-4

ISSN

0092-8674

Ausgabe der Veröffentlichung

7

Zeitschrift

Cell

Sprache

en

Paginierung

877 - 887

Datum der Veröffentlichung

1999

Status

Published

Herausgeber

Elsevier BV

Herausgeber URL

http://dx.doi.org/10.1016/s0092-8674(00)80800-4

Datum der Datenerfassung

2024

Titel

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

Ausgabe der Zeitschrift

97

Datenquelle: Crossref

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.

Addresses

Department of Cell Biology and Anatomy, Margaret M. Dyson Vision Research Institute, Weill Medical College of Cornell University, New York, New York 10021, USA.

Autoren

AW Tai
JZ Chuang
C Bode
U Wolfrum
CH Sung

DOI

10.1016/s0092-8674(00)80800-4

eISSN

1097-4172

Externe Identifier

PubMed Identifier: 10399916

Funding acknowledgements

NEI NIH HHS: EY11307
NEI NIH HHS: R01 EY011307

Open access

false

ISSN

0092-8674

Ausgabe der Veröffentlichung

7

Zeitschrift

Cell

Schlüsselwörter

Cytoplasm
Microtubules
Animals
Cattle
Mice
Microtubule Proteins
Rhodopsin
Microtubule-Associated Proteins
Receptors, Cell Surface
Nuclear Proteins
Recombinant Fusion Proteins
Mutagenesis
Binding Sites
Amino Acid Sequence
Biological Transport
Molecular Sequence Data
Photoreceptor Cells, Vertebrate
Dyneins
t-Complex Genome Region

Sprache

eng

Medium

Print

Paginierung

877 - 887

Datum der Veröffentlichung

1999

Status

Published

Publisher licence

CC BY-NC-ND

Datum der Datenerfassung

1999

Titel

Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1.

Sub types

Research Support, U.S. Gov't, P.H.S.
Research Support, Non-U.S. Gov't
Journal Article

Ausgabe der Zeitschrift

97

Datenquelle: Europe PubMed Central

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.

Autoren

AW Tai
JZ Chuang
C Bode
U Wolfrum
CH Sung

Autoren-URL

https://www.ncbi.nlm.nih.gov/pubmed/10399916

DOI

10.1016/s0092-8674(00)80800-4

Funding acknowledgements

NEI NIH HHS: R01 EY011307
NEI NIH HHS: EY11307

ISSN

0092-8674

Ausgabe der Veröffentlichung

7

Zeitschrift

Cell

Schlüsselwörter

Amino Acid Sequence
Animals
Binding Sites
Biological Transport
Cattle
Cytoplasm
Dyneins
Mice
Microtubule Proteins
Microtubule-Associated Proteins
Microtubules
Molecular Sequence Data
Mutagenesis
Nuclear Proteins
Photoreceptor Cells, Vertebrate
Receptors, Cell Surface
Recombinant Fusion Proteins
Rhodopsin
t-Complex Genome Region

Sprache

eng

Country

United States

Paginierung

877 - 887

PII

S0092-8674(00)80800-4

Datum der Veröffentlichung

1999

Status

Published

Datum, an dem der Datensatz öffentlich gemacht wurde

1999

Titel

Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1.

Sub types

Journal Article
Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

Ausgabe der Zeitschrift

97

Datenquelle: PubMed

Rhodopsin’s carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1

Werkzeuge