Identification of cytosolic factors required for nuclear location sequence-mediated binding to the nuclear envelope

Ermoné J.H. Adam*, Stephen A. Adam

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

253 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)547-555
Number of pages9
JournalJournal of Cell Biology
Volume125
Issue number3
DOIs
StatePublished - May 1994

ASJC Scopus subject areas

  • Cell Biology

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