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Actin Depolymerizing Factor Is a Component of Slow Axonal Transport
Author(s) -
Bray John J.,
Fernyhough Paul,
Bamburg James R.,
Bray Dennis
Publication year - 1992
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1992.tb10949.x
Subject(s) - cofilin , actin , profilin , axoplasmic transport , microbiology and biotechnology , chemistry , biology , actin remodeling of neurons , biophysics , microfilament , anatomy , biochemistry , cytoskeleton , actin cytoskeleton , cell
We examined the low molecular weight proteins transported with actin in the chicken sciatic nerve after injection of [ 35 S]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.