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FEBS Lett. 2013 Nov 1;587(21):3400-5. doi: 10.1016/j.febslet.2013.08.045. Epub 2013 Sep 10.

Functional conservation between mammalian MGRN1 and plant LOG2 ubiquitin ligases.

Author information

1
Department of Molecular and Cellular Biology, UC Davis, Davis, CA 95616, United States; UC Davis Biochemistry, Molecular, Cellular, Developmental Biology Graduate Group, United States.

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.

KEYWORDS:

DAR2; DOMAIN ASSOCIATED WITH RING 2; ESCRT; GDU; GDU1; GLUTAMINE DUMPER; GST; LOG2; LOSS OF GDU 2; MCR; MGRN1; Mahogunin; Membrane trafficking; RING; RNF; Ubiquitin ligase; VIMAG; Val-Ile-Met-Ala-Gly; cGDU1; cytosolic domain of GDU1; endosomal sorting complex required for transport; glutathione-S-transferase; mahogunin ring finger 1; melancortin receptors; really interesting new gene; ring finger

PMID:
24036454
PMCID:
PMC4157525
DOI:
10.1016/j.febslet.2013.08.045
[Indexed for MEDLINE]
Free PMC Article

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