Regulating filopodial dynamics through actin-depolymerizing factor/cofilin

Anat Sci Int. 2004 Dec;79(4):173-83. doi: 10.1111/j.1447-073x.2004.00087.x.

Abstract

The regulation of filopodial dynamics by neurotrophins and other guidance cues plays an integral role in growth cone pathfinding. Filopodia are F-actin-based structures that explore the local environment, generate forces and play a role in growth cone translocation. Here, we review recent research showing that the actin-depolymerizing factor (ADF)/cofilin family of proteins mediates changes in the length and number of growth cone filopodia in response to brain-derived neurotrophic factor (BDNF). Although inhibition of myosin contractility also causes filopodial elongation, the elongation in response to BDNF does not occur through a myosin-dependent pathway. Active ADF/cofilin increases the rate of cycling between the monomer and polymer pools and is critical for the BDNF-induced changes. Thus, we discuss potential mechanisms by which ADF/cofilin may affect filopodial initiation and length change via its effects on F-actin dynamics in light of past research on actin and myosin function in growth cones.

Publication types

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

MeSH terms

  • Actin Depolymerizing Factors
  • Animals
  • Cell Line, Tumor
  • Destrin
  • Growth Cones / metabolism*
  • Growth Cones / ultrastructure
  • Humans
  • Mice
  • Microfilament Proteins / metabolism*
  • Microfilament Proteins / ultrastructure
  • Nerve Tissue Proteins / metabolism*
  • Nerve Tissue Proteins / ultrastructure

Substances

  • Actin Depolymerizing Factors
  • DSTN protein, human
  • Destrin
  • Dstn protein, mouse
  • Microfilament Proteins
  • Nerve Tissue Proteins