title: Neurofilament phosphorylation: a new look at regulation and function.
abstract: Dynamic remodeling of cytoskeleton architecture is necessary for axonal growth and guidance, signal transduction and other fundamental aspects of neuron function. Protein phosphorylation plays a key part in these remodeling processes. Since neurofilaments are major cytoskeletal constituents and are among the most highly phosphorylated neuronal proteins, the control of their behavior serves as a possible model for understanding how phosphorylation regulates the many other phosphoproteins in the cytoskeleton. Recent studies show that neurofilament protein subunits are phosphorylated on both their amino-terminal head domains and carboxy-terminal tails by different protein kinases. This review considers the implications of this complex regulation for neurofilament function in normal neurons and in disease states characterized by neurofibrillary pathology.
authors.affiliation: Laboratory for Molecular Neuroscience, McLean Hospital, Belmont, MA.
authors.forename: R A
authors.initials: RA
authors.lastname: Nixon
authors.forename: R K
authors.initials: RK
authors.lastname: Sihag
mesh_terms: D000818:Animals; D001369:Axons / Q000502:physiology / Q000648:ultrastructure; D003599:Cytoskeleton / Q000502:physiology / Q000648:ultrastructure; D006706:Homeostasis; D007382:Intermediate Filaments / Q000502:physiology* / Q000648:ultrastructure; D008961:Models, Structural; D016900:Neurofilament Proteins / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism
chemical_list: D016900:Neurofilament Proteins; D011494:Protein Kinases