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Characterization of Dominant and Recessive Assembly-Defective Mutations in Mouse Neurofilament NF-M

Philip C. Wong and Don W. Cleveland
The Journal of Cell Biology
Vol. 111, No. 5, Part 1 (Nov., 1990), pp. 1987-2003
Stable URL: http://www.jstor.org/stable/1614261
Page Count: 17
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Characterization of Dominant and Recessive Assembly-Defective Mutations in Mouse Neurofilament NF-M
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Abstract

We have generated a set of amino- and carboxy-terminal deletions of the neurofilament NF-M gene and determined the molecular consequences of forced expression of these mutant constructs in mouse fibroblasts. To follow the expression of mutant NF-M subunits in transfected cells, a 12 amino acid epitope (from the human c-myc protein) was expressed at the carboxy terminus of each mutant. We show that NF-M molecules missing up to 90 or 70% of the nonhelical carboxy-terminal tail or amino-terminal head domains, respectively, incorporate readily into an intermediate filament network comprised either of vimentin or NF-L, whereas deletions into either the amino- or carboxy-terminal α-helical rod region generate assembly-incompetent polypeptides. Carboxy-terminal deletions into the rod domain invariably yield dominant mutants which rapidly disrupt the array of filaments comprised of NF-L or vimentin. Accumulation of these mutant NF-M subunits disrupts vimentin filament arrays even when present at ∼1% the level of the wild-type subunits. In contrast, the amino-terminal deletions into the rod produce pseudo-recessive mutants that perturb the wild-type NF-L or vimentin arrays only modestly. The inability of such amino-terminal mutants to disrupt wild-type subunits defines a region near the amino-terminal α-helical rod domain (residues 75-126) that is required for the earliest steps in filament assembly.

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