The high and middle molecular weight neurofilament subunits regulate the association of neurofilaments with kinesin: Inhibition by phosphorylation of the high molecular weight subunit

• Published in: Brain research. Molecular brain research. Vol. 141; no. 2; pp. 151 - 155
• Main Authors: Jung, Cheolwha, Lee, Sangmook, Ortiz, Daniela, Zhu, Qinzhang, Julien, Jean-Pierre, Shea, Thomas B.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 30.11.2005; Elsevier
• Subjects: Animals; Axonal transport; Axonal Transport - physiology; Biological and medical sciences; Cytoskeleton; Fundamental and applied biological sciences. Psychology; Intermediate Filaments - metabolism; Intermediate Filaments - ultrastructure; Kinesin; Kinesin - metabolism; Mice; Mice, Knockout; Molecular Motor Proteins - physiology; Molecular Weight; Motor protein; Neural Conduction - physiology; Neurofilament; Neurofilament Proteins - chemistry; Neurofilament Proteins - deficiency; Neurofilament Proteins - genetics; Neurofilament Proteins - metabolism; Neurofilament Proteins - physiology; Optic Nerve - chemistry; Optic Nerve - ultrastructure; Phosphorylation; Protein Binding; Protein Interaction Mapping; Protein Processing, Post-Translational; Retinal Ganglion Cells - chemistry; Retinal Ganglion Cells - ultrastructure; Vertebrates: nervous system and sense organs; Neurofilament; Phosphorylation; Cytoskeleton transport; Motor protein; Cellular and molecular biology; Cytoskeleton; Axonal transport; Kinesin; Biological transport; Subunit; Protein
• ISSN: 0169-328X; 1872-6941
• DOI: 10.1016/j.molbrainres.2005.08.009

Kinesin participates in axonal transport of neurofilaments (NFs), but the mode by which they attach to kinesin is unclear. We compared the association of NFs with kinesin in mice expressing or lacking NF-H or NF-M. In normal and M−/− mice, the leading edge of metabolically labeled NF subunits was selectively co-precipitated with kinesin. By contrast, the entire wave of radiolabeled subunits co-precipitated with kinesin in H−/− mice. Similar bulk levels of NFs co-precipitated with kinesin from normal and H−/− mice, but reduced levels co-precipitated from M−/− mice. These data suggest that both NF-H and NF-M regulate the association of NFs with kinesin. They further indicate that phosphorylation of NF-H dissociates NFs from kinesin and provides a mechanism by which NF-H phosphorylation can contribute to the slowing of NF axonal transport.