The Rev/Rex homolog HERV-K cORF multimerizes via a C-terminal domain

9Citations
Citations of this article
7Readers
Mendeley users who have this article in their library.

Abstract

Expression of human endogenous retrovirus K (HERV-K) is associated with germ-cell neoplasia. HERV-K encodes a protein of the Rev/Rex family, cORF, that supports cellular transformation and binds the promyelocytic leukemia zinc finger (PLZF) protein implicated in spermatogenesis. Rev/Rex function invariably depends on multimerization. Here we show that cORF likewise self-associates to form higher-order oligomers. Amino acids (aa) 47-87 in cORF are sufficient, aa 75-87 essential for self-association. Consistently, this domain is predicted to form a hydrophobic α-helix that may represent an oligomerization interface. The existence of a dimerization-competent cORF mutant lacking PLZF-binding activity (cORF47-87) suggests a way of dominant negative inhibition of the proposed tumor susceptibility factor cORF. © 2001 Federation of European Biochemical Societies.

Cite

CITATION STYLE

APA

Boese, A., Galli, U., Geyer, M., Sauter, M., & Mueller-Lantzsch, N. (2001). The Rev/Rex homolog HERV-K cORF multimerizes via a C-terminal domain. FEBS Letters, 493(2–3), 117–121. https://doi.org/10.1016/S0014-5793(01)02280-3

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free