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Molecular characterization of the sumo-1 modification of rangap1 and its role in nuclear envelope association

Academic Article
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Overview

authors

  • Mahajan, R.
  • Gerace, Larry
  • Melchior, F.

publication date

  • January 1998

journal

  • Journal of Cell Biology  Journal

abstract

  • The mammalian guanosine triphosphate (GTP)ase-activating protein RanGAP1 is the first example of a protein covalently linked to the ubiquitin-related protein SUMO-1. Here we used peptide mapping, mass spectroscopy analysis, and mutagenesis to identify the nature of the link between RanGAP1 and SUMO-1. SUMO-1 is linked to RanGAP1 via glycine 97, indicating that the last 4 amino acids of this 101- amino acid protein are proteolytically removed before its attachment to RanGAP1. Recombinant SUMO-1 lacking the last four amino acids is efficiently used for modification of RanGAP1 in vitro and of multiple unknown proteins in vivo. In contrast to most ubiquitinated proteins, only a single lysine residue (K526) in RanGAP1 can serve as the acceptor site for modification by SUMO-1. Modification of RanGAP1 with SUMO-1 leads to association of RanGAP1 with the nuclear envelope (NE), where it was previously shown to be required for nuclear protein import. Sufficient information for modification and targeting resides in a 25-kD domain of RanGAP1. RanGAP1-SUMO-1 remains stably associated with the NE during many cycles of in vitro import. This indicates that removal of RanGAP1 from the NE is not a required element of nuclear protein import and suggests that the reversible modification of RanGAP1 may have a regulatory role.

subject areas

  • Amino Acid Sequence
  • Animals
  • COS Cells
  • Carrier Proteins
  • Cloning, Molecular
  • GTPase-Activating Proteins
  • Glycine
  • Lysine
  • Molecular Sequence Data
  • Mutagenesis
  • Nuclear Envelope
  • SUMO-1 Protein
  • Saccharomyces cerevisiae
  • Ubiquitins
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Identity

International Standard Serial Number (ISSN)

  • 0021-9525

Digital Object Identifier (DOI)

  • 10.1083/jcb.140.2.259

PubMed ID

  • 9442102
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Additional Document Info

start page

  • 259

end page

  • 270

volume

  • 140

issue

  • 2

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