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Gronning-Wang, L. M.

Publications and source records attributed to Gronning-Wang, L. M..

2 recordsLinked to original sources

Open the LID: LXRα regulates ChREBPα transactivity in a target gene-specific manner through an agonist-modulated LBD-LID interaction

The cholesterol-sensing nuclear receptor liver X receptor (LXR) and the glucose-sensing transcription factor carbohydrate responsive element-binding protein (ChREBP) are central players in regulating glucose and lipid metabolism in liver. We have previously shown that LXR regulates ChREBP transcription and activity; however, the underlying mechanisms are unclear. In the current study, we demonstrate that LXR and ChREBP interact physically, and show a high co-occupancy at regulatory regions in the mouse genome. LXR co-activates ChREBP, and regulates ChREBP-specific target genes in vitro and in vivo. This co-activation is dependent on functional recognition elements for ChREBP, but not for LXR, indicating that ChREBP recruits LXR to chromatin in trans. The two factors interact via their key activation domains; ChREBPs low glucose inhibitory domain (LID) and the ligand-binding domain (LBD) of LXR. While unliganded LXR co-activates ChREBP, ligand-bound LXR surprisingly represses ChREBP activity on ChREBP-specific target genes. Mechanistically, this is due to a destabilized LXR:ChREBP interaction, leading to reduced ChREBP-binding to chromatin and restricted activation of glycolytic and lipogenic target genes. This ligand-driven molecular switch highlights an unappreciated role of LXR that was overlooked due to LXR lipogenesis-promoting function.

molecular biology↗

OGT (O-GlcNAc Transferase) selectively modifies multiple residues unique to lamin A

The LMNA gene encodes lamins A and C with key roles in nuclear structure, signaling, chromatin organization, and genome integrity. Mutations in LMNA cause >12 diseases, termed laminopathies. Lamins A and C are identical for their first 566 residues. However, they form distinct filaments in vivo with apparently distinct roles. We report that lamin A is O-GlcNAc modified in human hepatoma (Huh7) cells and in mouse liver. In vitro assays with purified OGT enzyme showed robust O-GlcNAcylation of recombinant mature lamin A tails (residues 385-646), with no detectable modification of lamin B1, lamin C, or progerin ({Delta}50) tails. Using mass spectrometry, we identified 11 O-GlcNAc sites in a sweet spot unique to lamin A, with up to seven sugars per peptide. Most sites were unpredicted by current algorithms. Double-mutant (S612A/T643A) lamin A tails were still robustly O-GlcNAc-modified at seven sites. By contrast, O-GlcNAcylation was undetectable on tails bearing deletion {Delta}50, which causes Hutchinson-Gilford progeria syndrome, and greatly reduced by deletion {Delta}35, suggesting this region is required for substrate recognition or modification by OGT in vitro. These results suggest OGT, an essential protein and master regulator, regulates partners or function(s) unique to lamin A that are lost in progeria.

biochemistry↗