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h-Goliath, paralog of GRAIL, is a new E3 ligase protein, expressed in human leukocytes

Guais, Adeline, Siegrist, Sylvie, Solhonne, Brigitte, Jouault, Hélène, Guellaën, Georges, Bulle, Frédérique·2006·Gene
DOI 10.1016/j.gene.2006.01.028
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Abstract

In Drosophila, the RING finger protein d-Goliath was originally identified as a transcription factor involved in the embryo mesoderm formation [Bouchard, M.L., Cote, S., 1993. The Drosophila melanogaster developmental gene g1 encodes a variant zinc-finger-motif protein. Gene 125, 205-209]. In mouse, the m-Goliath mRNA level was shown to be increased in growth factor withdrawal-induced apoptosis of myeloid cells [Baker, S.J., Reddy, E.P., 2000. Cloning of murine G1RP, a novel gene related to Drosophila melanogaster g1. Gene 248, 33-40]. Due to its putative function of transcription factor in apoptosis, we cloned the human cDNA for h-Goliath and characterized the expression of the protein in blood and bone marrow cells. The human protein of 419 aa (44 kDa) contains a protease-associated domain, a transmembrane domain and a RING-H2 motif. This structure classifies h-Goliath as a new member of a human family of ubiquitin ligases with GRAIL (gene related to anergy in lymphocytes) as founder. This E3 ligase controls the development of T cell clonal anergy by ubiquitination [Anandasabapathy, N., Ford, G.S., Bloom, D., Holness, C., Paragas, V., Seroogy, C., Skrenta, H., Hollenhorst, M., Fathman, C.G., Soares, L., 2003. GRAIL: an E3 ubiquitin ligase that inhibits cytokine gene transcription is expressed in anergic CD4+ T cells. Immunity 18, 535-547]. In vitro ubiquitination studies support the E3 ubiquitin ligase activity of h-Goliath. In human, the protein is expressed under 3 isofor…

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Metadata

Authors
Guais, A., Siegrist, S., Solhonne, B., Jouault, H., Guellaën, G., & Bulle, F.
Venue
Gene
Publisher
Elsevier BV
Published
2006-06
Volume
374
Pages
112-120
ISSN
0378-1119
DOI
10.1016/j.gene.2006.01.028
Cited by
19
References
2
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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