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The tetraspanin protein peripherin-2 forms a complex with melanoregulin, a putative membrane fusion regulator

  1. Author:
    Boesze-Battaglia, K.
    Song, H. M.
    Sokolov, M.
    Lillo, C.
    Pankoski-Walker, L.
    Gretzula, C.
    Gallagher, B.
    Rachel, R. A.
    Jenkins, N. A.
    Copeland, N. G.
    Morris, F.
    Jacob, J.
    Yeagle, P.
    Williams, D. S.
    Damek-Poprawa, M.

  2. Author Address

    Univ Penn, Sch Dent Med, Dept Biochem, Philadelphia, PA 19104 USA. Univ Penn, Sch Dent Med, Dept Pathol, Philadelphia, PA 19104 USA. W Virginia Univ, Ctr Hlth Sci, Dept Mol Pharmacol & Biochem, Morgantown, WV 26506 USA. W Virginia Univ, Inst Eye, Dept Ophthalmol, Morgantown, WV 26506 USA. Univ Calif San Diego, Sch Med, Dept Pharmacol, La Jolla, CA 92093 USA. NCI, Mouse Canc Genet Program, Frederick, MD 21702 USA. Univ Connecticut, Dept Mol & Cell Biol, Storrs, CT 06269 USA.;Boesze-Battaglia, K, Univ Penn, Sch Dent Med, Dept Biochem, 240 S 40th St, Philadelphia, PA 19104 USA.;battagli@biochem.dental.upenn.edu
    1. Year: 2007
    2. Date: Feb
  2. Journal: Biochemistry
    1. 46
    2. 5
    3. Pages: 1256-1272
  4. Type of Article: Article
  5. ISSN: 0006-2960
  1. Abstract:

    Peripherin-2, the product of the rds gene, is a tetraspanin protein. In this study, we show that peripherin-2 forms a complex with melanoregulin (MREG), the product of the Mreg locus. Genetic studies suggest that MREG is involved in organelle biogenesis. In this study, we explore the role of this protein in processes associated with the formation of disk membranes, specialized organelles of photoreceptor rod cells. MREG antibodies were generated and found to be immunoreactive with a 28 kDa protein in retinal extracts, bovine OS, ARPE-19 cells, and rat RPE. MREG colocalized with peripherin-2 in WT (CB6F1/J) and in rds+/- retinas. Western blots of serial tangential sections confirmed the close association of these two proteins within the IS and basal outer segment of rods. Immunoprecipitation (IP) of OS extracts showed formation of a complex between MREG and peripherin-2-ROM-1 hetero-oligomers. This interaction was confirmed with pulldown analyses in which the GST-PerCter protein selectively pulled down (His-)MREG and (His-)MREG selectively pulled down PerCter. Biacore analysis using peptide inhibitors and per-2 truncation mutant studies allowed us to map the MREG binding site on per-2 to the last five residues of the C-terminus (Gln(341)-Gly(346)), and kinetic data predicted a K-D of 80 nM for PerCter-MREG binding. Finally, the effect of MREG on photoreceptor specific membrane fusion was assayed using a disk-plasma membrane cell free assay. Preincubation of target membranes with MREG resulted in a dose-dependent inhibition of fusion with an IC50 in the submicromolar range. Collectively, these results suggest that this newly identified protein regulates peripherin-2 function.

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  2. DOI: 10.1021/bi061466i
  3. View record in Web of Science®
  4. WOS: 000243839500014

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