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

Overview

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.

publication date

  • June 25, 1999

Research

keywords

  • Dyneins
  • Microtubule Proteins
  • Microtubule-Associated Proteins
  • Nuclear Proteins
  • Receptors, Cell Surface
  • Rhodopsin

Identity

Scopus Document Identifier

  • 0033603239

Digital Object Identifier (DOI)

  • 10.1016/s0092-8674(00)80800-4

PubMed ID

  • 10399916

Additional Document Info

volume

  • 97

issue

  • 7