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

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.
Mesh Terms:
Amino Acid Sequence, Animals, Binding Sites, Cattle, Cloning, Molecular, DNA-Binding Proteins, Humans, Kinetics, Leucine Zippers, Macromolecular Substances, Molecular Chaperones, Molecular Sequence Data, Nuclear Pore Complex Proteins, Nuclear Proteins, Peptide Hydrolases, Peptidylprolyl Isomerase, Proteasome Endopeptidase Complex, Recombinant Fusion Proteins, Retina, Sequence Alignment, Sequence Homology, Amino Acid
J. Biol. Chem.
Date: Sep. 18, 1998
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