Dynamic interplay between O-linked N-acetylglucosaminylation and glycogen synthase kinase-3-dependent phosphorylation.
AuthorsWang Z, Pandey A, Hart GW
JournalMol Cell Proteomics
PubMed ID17507370
'O-GlcNAcylation on serine and threonine side chains of nuclear and cytoplasmic proteins is dynamically regulated in response to various environmental and biological stimuli. O-GlcNAcylation is remarkably similar to O-phosphorylation and appears to have a dynamic interplay with O-phosphate in cellular regulation. A systematic glycoproteomics analysis of the affects of inhibiting ... More
Novel in vivo-degradable cellulose-chitin copolymer from metabolically engineered Gluconacetobacter xylinus.
AuthorsYadav V, Paniliatis BJ, Shi H, Lee K, Cebe P, Kaplan DL,
JournalAppl Environ Microbiol
PubMed ID20656868
'Despite excellent biocompatibility and mechanical properties, the poor in vitro and in vivo degradability of cellulose has limited its biomedical and biomass conversion applications. To address this issue, we report a metabolic engineering-based approach to the rational redesign of cellular metabolites to introduce N-acetylglucosamine (GlcNAc) residues into cellulosic biopolymers during ... More
Direct in-gel fluorescence detection and cellular imaging of O-GlcNAc-modified proteins.
'We report an advanced chemoenzymatic labeling strategy for direct fluorescence detection of O-GlcNAc proteins in gels that facilitates proteomic studies and greatly extend the reach of existing technologies. These new tools also enable the expression and dynamics of O-GlcNAc modifications to be monitored by imaging in cells and tissues. ... More
The chemical neurobiology of carbohydrates.
AuthorsMurrey HE, Hsieh-Wilson LC,
JournalChem Rev
PubMed ID18452339
The problems associated with oligosaccharide analysis have hindered efforts to understand the biology of oligosaccharides yet have given chemists a unique opportunity to develop new methods to overcome these challenges. The development of chemical tools for the analysis of glycan structure and function is essential to advance our understanding of ... More
O-linked N-acetylglucosamine modification on CCAAT enhancer-binding protein beta: role during adipocyte differentiation.
AuthorsLi X, Molina H, Huang H, Zhang YY, Liu M, Qian SW, Slawson C, Dias WB, Pandey A, Hart GW, Lane MD, Tang QQ,
JournalJ Biol Chem
PubMed ID19478079
CCAAT enhancer-binding protein (C/EBP)beta is a basic leucine zipper transcription factor family member, and can be phosphorylated, acetylated, and sumoylated. C/EBPbeta undergoes sequential phosphorylation during 3T3-L1 adipocyte differentiation. Phosphorylation on Thr(188) by MAPK or cyclin A/cdk2 primes the phosphorylations on Ser(184)/Thr(179) by GSK3beta, and these phosphorylations are required for the ... More
Identification of structural and functional O-linked N-acetylglucosamine-bearing proteins in Xenopus laevis oocyte.
O-Linked N-acetylglucosaminylation (O-GlcNAcylation) (or O-linked N-acetylglucosamine (O-GlcNAc)) is an abundant and reversible glycosylation type found within the cytosolic and the nuclear compartments. We have described previously the sudden O-GlcNAcylation increase occurring during the Xenopus laevis oocyte G(2)/M transition, and we have demonstrated that the inhibition of O-GlcNAc-transferase (OGT) blocked this ... More
Regulation of calcium/calmodulin-dependent kinase IV by O-GlcNAc modification.
AuthorsDias WB, Cheung WD, Wang Z, Hart GW,
JournalJ Biol Chem
PubMed ID19506079
Similar to phosphorylation, GlcNAcylation (the addition of O-GlcNAc to Ser(Thr) residues on polypeptides) is an abundant, dynamic, and inducible post-translational modification. GlcNAcylated proteins are crucial in regulating virtually all cellular processes, including signaling, cell cycle, and transcription. Here we show that calcium/calmodulin-dependent kinase IV (CaMKIV) is highly GlcNAcylated in vivo. ... More