Interactions between CAP70 and actinfilin are important for integrity of actin cytoskeleton structures in neurons

Neuropharmacology. 2005 Dec;49(7):1026-41. doi: 10.1016/j.neuropharm.2005.05.022. Epub 2005 Jul 28.

Abstract

The integrity of dynamic actin structures is coupled to a variety of neurological processes. Actin-binding proteins play a critical role in regulating actin structure dynamics. A link between actin-binding proteins and receptor interacting scaffolding proteins may provide a conduit for transmitting signaling events to the cytoskeleton. Actinfilin is a brain-enriched actin-binding protein, though its functions are currently unknown. We report here that actinfilin interacts with the multi-PDZ domain protein CAP70. Recombinant expression of an actin-binding domain of actinfilin progressively causes marked changes of cellular morphology. The effect on cell morphology may be reduced by co-expression with CAP70. Mutation of actinfilin lacking the ability to interact with CAP70 abolished the effect by CAP70. The evidence suggests a role of actinfilin and possible regulation by scaffolding proteins.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / chemistry
  • Actins / metabolism
  • Actins / physiology*
  • Animals
  • Brain / drug effects
  • Brain / ultrastructure
  • Carrier Proteins / chemistry
  • Carrier Proteins / physiology*
  • Cells, Cultured
  • Cytoskeletal Proteins
  • Cytoskeleton / chemistry
  • Cytoskeleton / physiology*
  • HeLa Cells
  • Humans
  • Immunoblotting
  • Immunohistochemistry
  • Immunoprecipitation
  • In Situ Hybridization
  • Neurons / chemistry*
  • Rats
  • Rats, Sprague-Dawley
  • Saccharomyces cerevisiae
  • Subcellular Fractions / drug effects
  • Subcellular Fractions / ultrastructure
  • Transfection

Substances

  • Actins
  • Carrier Proteins
  • Cytoskeletal Proteins
  • Pdzk1 protein, rat