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The cyclophilin-like domain mediates the association of Ran-binding protein 2 with subunits of the 19 S regulatory complex of the proteasome.

Publication ,  Journal Article
Ferreira, PA; Yunfei, C; Schick, D; Roepman, R
Published in: J Biol Chem
September 18, 1998

The combination of the Ran-binding domain 4 and cyclophilin domains of Ran-binding protein 2 selectively associate with a subset of G protein-coupled receptors, red/green opsins, upon cis-trans prolyl isomerase-dependent and direct modification of opsin followed by association of the modified opsin isoform to Ran-binding domain 4. This effect enhances in vivo the production of functional receptor and generates an opsin isoform with no propensity to self-aggregate in vitro. We now show that another domain of Ran-binding protein 2, cyclophilin-like domain, specifically associates with the 112-kDa subunit, P112, and other subunits of the 19 S regulatory complex of the 26 S proteasome in the neuroretina. This association possibly mediates Ran-binding protein 2 limited proteolysis into a smaller and stable isoform. Also, the interaction of Ran-binding protein 2 with P112 regulatory subunit of the 26 S proteasome involves still another protein, a putative kinesin-like protein. Our results indicate that Ran-binding protein 2 is a key component of a macro-assembly complex selectively linking protein biogenesis with the proteasome pathway and, thus, with potential implications for the presentation of misfolded and ubiquitin-like modified proteins to this proteolytic machinery.

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Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

September 18, 1998

Volume

273

Issue

38

Start / End Page

24676 / 24682

Location

United States

Related Subject Headings

  • Sequence Homology, Amino Acid
  • Sequence Alignment
  • Retina
  • Recombinant Fusion Proteins
  • Proteasome Endopeptidase Complex
  • Peptidylprolyl Isomerase
  • Peptide Hydrolases
  • Nuclear Proteins
  • Nuclear Pore Complex Proteins
  • Molecular Sequence Data
 

Citation

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Ferreira, P. A., Yunfei, C., Schick, D., & Roepman, R. (1998). The cyclophilin-like domain mediates the association of Ran-binding protein 2 with subunits of the 19 S regulatory complex of the proteasome. J Biol Chem, 273(38), 24676–24682. https://doi.org/10.1074/jbc.273.38.24676
Ferreira, P. A., C. Yunfei, D. Schick, and R. Roepman. “The cyclophilin-like domain mediates the association of Ran-binding protein 2 with subunits of the 19 S regulatory complex of the proteasome.J Biol Chem 273, no. 38 (September 18, 1998): 24676–82. https://doi.org/10.1074/jbc.273.38.24676.
Ferreira, P. A., et al. “The cyclophilin-like domain mediates the association of Ran-binding protein 2 with subunits of the 19 S regulatory complex of the proteasome.J Biol Chem, vol. 273, no. 38, Sept. 1998, pp. 24676–82. Pubmed, doi:10.1074/jbc.273.38.24676.

Published In

J Biol Chem

DOI

ISSN

0021-9258

Publication Date

September 18, 1998

Volume

273

Issue

38

Start / End Page

24676 / 24682

Location

United States

Related Subject Headings

  • Sequence Homology, Amino Acid
  • Sequence Alignment
  • Retina
  • Recombinant Fusion Proteins
  • Proteasome Endopeptidase Complex
  • Peptidylprolyl Isomerase
  • Peptide Hydrolases
  • Nuclear Proteins
  • Nuclear Pore Complex Proteins
  • Molecular Sequence Data