Cytoplasmic dynein regulation by subunit heterogeneity and its role in apical transport. Academic Article uri icon

Overview

abstract

  • Despite the existence of multiple subunit isoforms for the microtubule motor cytoplasmic dynein, it has not yet been directly shown that dynein complexes with different compositions exhibit different properties. The 14-kD dynein light chain Tctex-1, but not its homologue RP3, binds directly to rhodopsin's cytoplasmic COOH-terminal tail, which encodes an apical targeting determinant in polarized epithelial Madin-Darby canine kidney (MDCK) cells. We demonstrate that Tctex-1 and RP3 compete for binding to dynein intermediate chain and that overexpressed RP3 displaces endogenous Tctex-1 from dynein complexes in MDCK cells. Furthermore, replacement of Tctex-1 by RP3 selectively disrupts the translocation of rhodopsin to the MDCK apical surface. These results directly show that cytoplasmic dynein function can be regulated by its subunit composition and that cytoplasmic dynein is essential for at least one mode of apical transport in polarized epithelia.

publication date

  • June 25, 2001

Research

keywords

  • Cytoplasm
  • Dyneins
  • Eye Proteins
  • Microtubule-Associated Proteins
  • Nuclear Proteins
  • Protein Subunits

Identity

PubMed Central ID

  • PMC2150720

Scopus Document Identifier

  • 0035954436

Digital Object Identifier (DOI)

  • 10.1083/jcb.153.7.1499

PubMed ID

  • 11425878

Additional Document Info

volume

  • 153

issue

  • 7