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Study of the phosphorylation, structure, and assembly of mammalian neurofilament subunits

Authors
Publisher
McGill University
Publication Date
Keywords
  • Chemistry
  • Biochemistry.
Disciplines
  • Chemistry

Abstract

The expression of all three NF subunits in cultured adrenal chromaffin cells was demonstrated by immunocytochemical staining, and by immunoprecipitation techniques. The NFs in chromaffin cells, which are largely restricted to the perikaryon, were found to be hypophosphorylated, as they comigrated with in vitro dephosphorylated bovine NF subunits on SDS-PAGE. Triton-soluble pools of NF-M, and NF-H were shown to be present in chromaffin cells. These were found to be distinct from the cytoskeleton-associated NF subunits based on differences in their relative amounts, and in the rate of $ sp{32}$P turnover. In addition, differences in the phosphopeptide maps of Triton-soluble and cytoskeletal NF-M suggested that certain phosphorylation sites may be important in regulating NF subunit assembly.

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