DYNLL/LC8: A Light Chain Subunit of the Dynein Motor Complex and Beyond

FEBS J. 2011 Sep;278(17):2980-96. doi: 10.1111/j.1742-4658.2011.08254.x. Epub 2011 Aug 8.

Abstract

The LC8 family members of dynein light chains (DYNLL1 and DYNLL2 in vertebrates) are highly conserved ubiquitous eukaryotic homodimer proteins that interact, besides dynein and myosin 5a motor proteins, with a large (and still incomplete) number of proteins involved in diverse biological functions. Despite an earlier suggestion that LC8 light chains function as cargo adapters of the above molecular motors, they are now recognized as regulatory hub proteins that interact with short linear motifs located in intrinsically disordered protein segments. The most prominent LC8 function is to promote dimerization of their binding partners that are often scaffold proteins of various complexes, including the intermediate chains of the dynein motor complex. Structural and functional aspects of this intriguing hub protein will be highlighted in this minireview.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Biological Transport
  • Cytoplasmic Dyneins / chemistry
  • Cytoplasmic Dyneins / physiology*
  • Cytoskeleton / metabolism*
  • Dyneins / metabolism
  • Humans
  • Protein Interaction Domains and Motifs
  • Protein Subunits / chemistry
  • Protein Subunits / physiology*

Substances

  • Protein Subunits
  • Cytoplasmic Dyneins
  • DYNLL2 protein, human
  • Dyneins