Phosphorylation protects neurofilaments against proteolysis

J Neuroimmunol. 1987 Mar;14(2):149-60. doi: 10.1016/0165-5728(87)90049-x.


During incubation with phosphatase, the 200 kDa neurofilament protein in cytoskeletal preparations is degraded extensively. Degradation, which is divalent cation-independent, does not occur when inhibitors of phosphatase are added. The 160 kDa chymotryptic fragment of neurofilaments or affinity-purified 200 kDa protein are not degraded by phosphatase. The results suggest that phosphorylated neurofilaments are protected against proteolysis, and dephosphorylated neurofilaments are degraded by a calcium-independent, endogenous proteinase which is associated with assembled neurofilaments or with other cytoskeletal components, and not with the phosphatase used.

Publication types

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

MeSH terms

  • Chromatography, Affinity
  • Chymotrypsin / metabolism
  • Collodion
  • Cytoskeleton / metabolism
  • Drug Stability
  • Electrophoresis, Polyacrylamide Gel
  • Intermediate Filament Proteins / metabolism*
  • Neurofilament Proteins
  • Paper
  • Phosphoric Monoester Hydrolases / metabolism
  • Phosphorylation


  • Intermediate Filament Proteins
  • Neurofilament Proteins
  • Collodion
  • Phosphoric Monoester Hydrolases
  • Chymotrypsin