Identification and characterization of a nuclear pore complex protein.

Abstract

We describe studies using a monoclonal antibody that recognizes a 62 kd protein (p62) of rat liver nuclei. This protein remains associated with the nuclear pore complex-lamina fraction resulting from treatment of nuclei with DNAase, RNAase, and nonionic detergent. Immunofluorescence revealed a strikingly punctate pattern of nuclear rim staining. By immunoferritin microscopy, p62 was specifically localized to the pore complex. Thus, pore complexes can be resolved by fluorescence light microscopy. Pulse chase analysis of labeled tissue culture cells showed that p62 is synthesized as a soluble cytoplasmic precursor of 61 kd, which is incorporated into the nuclear fraction with an unusually long t1/2 of about 6 hr. Incorporation is followed by modification that may involve addition of N-acetylglucosamine residues.