Functional conservation between mammalian MGRN1 and plant LOG2 ubiquitin ligases. Issue 21 (10th September 2013)

• Record Type: Journal Article
• Authors: Guerra, Damian D.; Pratelli, Réjane; Kraft, Edward; Callis, Judy; Pilot, Guillaume
• Is Part Of: FEBS letters. Volume 587:Issue 21(2013)
• Page Start: 3400
• Page End: 3405
• Publication Date: 2013-09-10
• Subjects: cGDU1 -- cytosolic domain of GDU1 -- DAR2 -- DOMAIN ASSOCIATED WITH RING 2 -- ESCRT -- endosomal sorting complex required for transport -- GDU -- GLUTAMINE DUMPER -- GST -- glutathione-S-transferase -- LOG2 -- LOSS OF GDU 2 -- MCR -- melancortin receptors -- MGRN1 -- mahogunin ring finger 1 -- RING -- really interesting new gene -- RNF -- ring finger -- VIMAG -- Val-Ile-Met-Ala-Gly -- Ubiquitin ligase -- Membrane trafficking -- Mahogunin -- GDU1 -- LOG2; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2013.08.045
• Languages: English
• ISSNs: 0014-5793

Abstract

Abstract : Plant LOSS OF GDU 2 (LOG2) and Mammalian Mahogunin Ring Finger 1 (MGRN1) proteins are RING‐type E3 ligases sharing similarity N‐terminal to the RING domain. Deletion of this region disrupts the interaction of LOG2 with the plant membrane protein GLUTAMINE DUMPER1 (GDU1). Phylogenetic analysis identified two clades of LOG2/MGRN1‐like proteins in vertebrates and plants. The ability of MGRN1 to functionally replace LOG2 was tested. MGRN1 ubiquitylates GDU1 in vitro and can partially substitute for LOG2 in the plant, partially restoring amino acid resistance to a GDU1‐myc over‐expression, log2 ‐ 2 background. Altogether, these results suggest a conserved function for the N‐terminal domain in evolution. Abstract : Arabidopsis E3 ligase LOG2 interacts with cGDU1 through DAR2, a conserved domain. There are two clades of DAR2‐containing proteins in both vertebrates and plants. Mammalian MGRN1, homologous to plant LOG2, binds to and ubiquitylates GDU1 in vitro . MGRN1 functionally complements log2 mutant plants indicating functional conservation. MGRN1 may have in vivo binding partners with GDU1‐like VIMAG motifs.