Abstract
Nuclear protein import can be separated into two distinct steps: binding to the nuclear pore complex followed by translocation to the nuclear interior. A previously identified nuclear location sequence (NLS) receptor and a 97-kD protein purified from bovine erythrocytes reconstitute the binding step in a permeabilized cell assay. Binding to the envelope is specific for a functional SV-40 large T antigen NLS and is not ATP or temperature dependent. Modification of p97 with N-ethylmaleimide (NEM) decreases binding to the pore, but interestingly, NEM treatment of the NLS receptor does not. Nuclear envelope binding is inhibited by wheat germ agglutinin suggesting a possible mechanism for the inhibition of transport by the lectin.
Dates
Type | When |
---|---|
Created | 21 years, 3 months ago (May 14, 2004, 8:22 p.m.) |
Deposited | 2 years, 1 month ago (July 22, 2023, 12:42 a.m.) |
Indexed | 1 month, 3 weeks ago (July 2, 2025, 2:45 p.m.) |
Issued | 31 years, 3 months ago (May 1, 1994) |
Published | 31 years, 3 months ago (May 1, 1994) |
Published Online | 31 years, 3 months ago (May 1, 1994) |
Published Print | 31 years, 3 months ago (May 1, 1994) |
@article{Adam_1994, title={Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope.}, volume={125}, ISSN={1540-8140}, url={http://dx.doi.org/10.1083/jcb.125.3.547}, DOI={10.1083/jcb.125.3.547}, number={3}, journal={The Journal of cell biology}, publisher={Rockefeller University Press}, author={Adam, E J and Adam, S A}, year={1994}, month=may, pages={547–555} }