Actin depolymerizing factor is a component of slow axonal transport

J Neurochem. 1992 Jun;58(6):2081-7. doi: 10.1111/j.1471-4159.1992.tb10949.x.


We examined the low molecular weight proteins transported with actin in the chicken sciatic nerve after injection of [35S]methionine into the lumbar spinal cord. A prominent component of slow axonal transport with apparent molecular mass 19 kDa comigrated on two-dimensional gels with chicken actin depolymerizing factor (ADF), previously shown to be a major actin-binding protein in brain. There was comparatively little radioactivity associated with the actin monomer sequestering proteins, profilin or cofilin, and examination of the rapid component of axonal transport failed to reveal appreciable quantities of actin, ADF, profilin, or cofilin. These results show that both actin and ADF are carried by slow axonal transport and raise the possibility that actin travels within the axon in an unpolymerized form in a complex with ADF.

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.

MeSH terms

  • Actin Depolymerizing Factors
  • Actins / analysis
  • Actins / metabolism
  • Animals
  • Axonal Transport / physiology*
  • Axons / chemistry
  • Axons / metabolism
  • Axons / physiology
  • Chickens
  • Contractile Proteins*
  • Destrin
  • Electrophoresis, Polyacrylamide Gel
  • Immunoblotting
  • Methionine / metabolism
  • Microfilament Proteins / analysis
  • Microfilament Proteins / metabolism
  • Microfilament Proteins / physiology*
  • Nerve Tissue Proteins / analysis
  • Nerve Tissue Proteins / metabolism
  • Profilins
  • Sciatic Nerve / chemistry
  • Sciatic Nerve / metabolism
  • Sulfur Radioisotopes


  • Actin Depolymerizing Factors
  • Actins
  • Contractile Proteins
  • Destrin
  • Microfilament Proteins
  • Nerve Tissue Proteins
  • Profilins
  • Sulfur Radioisotopes
  • Methionine