Mechanisms of Monomeric and Dimeric Glycogenin Autoglucosylation

Issoglio, Federico M.; Carrizo, M.E.; Romero, Jorge M.; Curtino, Juan A.

doi:10.1074/jbc.m111.287813

Cited by 14 publications

(12 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Other non-standard sequons have been observed for recombinant immunoglobulin G2 antibodies expressed in Chinese hamster ovary cells 23 or mouse laminin 22 , but these structures have not been confirmed more widely in animal systems. || Variation in ppGALNT specificities was determined empirically 154 . ¶ Prediction software available from the YinOYang WWW server 155 . # The specificity for the initiation of proteoglycan core synthesis is defined empirically 156 . ** Proposed consensus 157 with variable support from mass spectrometry analysis 123 . ‡‡ Collagen domains are modified at Lys residues to form hydroxylysine (Hyl) and galactosylated, then they are extended with an α1,2-Glc residue prior to triple helix formation 144 . §§ Autoglucosylation and extension of the initial glycogen polymer on the glycogenin backbone occurs on the Tyr194 hydroxyl group 143 . |||| Mannose liked to the C2 of the indole ring of the tryptophan residue based on the corresponding consensus sequence 111 . ¶¶ Prediction of consensus sequence has been defined based on hidden Markov model and prediction software 158 . ADAMTS, a disintegrin and metalloproteinase with thrombospondin motifs; EOGT, EGF domain-specific O -linked GlcNAc transferase; GLT25D1/2, glycosyltransferase 25 family member 1/2; GYG, glycogenin; NCAM1, neural cell adhesion molecule 1; OGT, O -linked GlcNAc transferase; OST, oligosaccharyltransferase; POFUT, protein O -fucosyltransferase; POGLUT, protein O -glucosyltransferase; POMT, protein O mannosyltransferase; ppGALNTs, polypeptide GalNAc transferases; TSR, thrombospondin type 1 repeat; XYLT, xylosyltransferase.…”

Section: Figurementioning

confidence: 99%

“… §§ Autoglucosylation and extension of the initial glycogen polymer on the glycogenin backbone occurs on the Tyr194 hydroxyl group 143 . …”

Section: Figurementioning

confidence: 99%

“…O -linked GlcNAc is found on the extracellular domains of some proteins and on numerous cytosolic and nuclear proteins, but different enzymes mediate extracellular and nucleocytoplasmic O -GlcNAcylation 6 . O -linked glycan structures attached to other amino acids include Gal on hydroxylysine of collagen domains that is extended by the addition of an α1,2-Glc residue and the addition of a Glc on Tyr of glycogenin that is extended and branched with additional Glc residues to form glycogen 143,144 . In addition to proteins, sphingolipids can be modified by glycosylation.…”

mentioning

confidence: 99%

See 2 more Smart Citations

Vertebrate protein glycosylation: diversity, synthesis and function

Moremen

Tiemeyer

Nairn

2012

Nat Rev Mol Cell Biol

1,460

1,292

View full text Add to dashboard Cite

Protein glycosylation is a ubiquitous post-translational modification found in all domains of life. Despite their significant complexity in animal systems, glycan structures have crucial biological and physiological roles, from contributions in protein folding and quality control to involvement in a large number of biological recognition events. As a result, they impart an additional level of ‘information content’ to underlying polypeptide structures. Improvements in analytical methodologies for dissecting glycan structural diversity, along with recent developments in biochemical and genetic approaches for studying glycan biosynthesis and catabolism, have provided a greater understanding of the biological contributions of these complex structures in vertebrates.

show abstract

Section: Figurementioning

confidence: 99%

“… §§ Autoglucosylation and extension of the initial glycogen polymer on the glycogenin backbone occurs on the Tyr194 hydroxyl group 143 . …”

Section: Figurementioning

confidence: 99%

mentioning

confidence: 99%

See 1 more Smart Citation

Vertebrate protein glycosylation: diversity, synthesis and function

Moremen

Tiemeyer

Nairn

2012

Nat Rev Mol Cell Biol

1,460

1,292

View full text Add to dashboard Cite

show abstract

“…In the lumen of the ER and Golgi, secretory and transmembrane proteins can be modified with oligosaccharides (glycans) attaching to the side chains of a specific amino acid. Depending on where the sugar chains are attached to a protein, lumenal glycosylation can be further divided into four groups: 1) N-glycosylation, attached to the amide group of asparagine (Asn); 2) O-glycosylation, linked to the hydroxyl group of Serine (Ser), Threonine (Thr), hydroxylysine [14] or Tyrosine (Tyr) [15]; 3) C-mannosylation, a mannose is attached to the C2 atom of tryptophan (Trp) through an C-C bond [16]; and 4) Glypiation, in which a glycan acts as a linker to bridge a protein to a glycosylphophatidylinositol (GPI) anchor in the membrane [17]. …”

Section: Introductionmentioning

confidence: 99%

Glycosylation Quality Control by the Golgi Structure

Zhang

Wang

2016

Journal of Molecular Biology

116

View full text Add to dashboard Cite

Glycosylation is a ubiquitous modification that occurs on proteins and lipids in all living cells. Consistent with their high complexity, glycans play crucial biological roles in protein quality control and recognition events. Asparagine-linked protein N-glycosylation, the most complex glycosylation, initiates in the endoplasmic reticulum (ER) and matures in the Golgi apparatus. This process not only requires an accurate distribution of processing machineries, such as glycosyltransferases, glycosidases and nucleotide sugar transporters, but also needs an efficient and well-organized factory that is responsible for the fidelity and quality control of sugar chain processing. In addition, accurate glycosylation must occur in coordination with protein trafficking and sorting. These activities are carried out by the Golgi apparatus, a membrane organelle in the center of the secretory pathway. To accomplish these tasks, the Golgi has developed into a unique stacked structure of closely aligned flattened cisternae in which Golgi enzymes reside; in mammalian cells, dozens of Golgi stacks are often laterally linked into a ribbon-like structure. Here, we review our current knowledge of how the Golgi structure is formed and why its formation is required for accurate glycosylation, with the focus of how the Golgi stacking factors GRASP55 and GRASP65 generate the Golgi structure and how the conserved oligomeric Golgi (COG) complex maintains Golgi enzymes in different Golgi subcompartments by retrograde protein trafficking.

show abstract

“…GN and GS are capable of forming dimers and tetramers (12,19), although GN can function as a monomer at low enzyme concentrations (22). Given the potential for multimer formation, the differences in affinities and Hill coefficients for full-length CeGN versus CeGN 34 binding to CeGS could in part be due to an avidity affect.…”

Section: Oligomerization Of Cegn and Cegsmentioning

confidence: 99%

Structural basis for the recruitment of glycogen synthase by glycogenin

Zeqiraj

Tang

Hunter

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

Glycogen is a primary form of energy storage in eukaryotes that is essential for glucose homeostasis. The glycogen polymer is synthesized from glucose through the cooperative action of glycogen synthase (GS), glycogenin (GN), and glycogen branching enzyme and forms particles that range in size from 10 to 290 nm. GS is regulated by allosteric activation upon glucose-6-phosphate binding and inactivation by phosphorylation on its N-and C-terminal regulatory tails. GS alone is incapable of starting synthesis of a glycogen particle de novo, but instead it extends preexisting chains initiated by glycogenin. The molecular determinants by which GS recognizes self-glucosylated GN, the first step in glycogenesis, are unknown. We describe the crystal structure of Caenorhabditis elegans GS in complex with a minimal GS targeting sequence in GN and show that a 34-residue region of GN binds to a conserved surface on GS that is distinct from previously characterized allosteric and binding surfaces on the enzyme. The interaction identified in the GS-GN costructure is required for GS-GN interaction and for glycogen synthesis in a cell-free system and in intact cells. The interaction of full-length GS-GN proteins is enhanced by an avidity effect imparted by a dimeric state of GN and a tetrameric state of GS. Finally, the structure of the N-and C-terminal regulatory tails of GS provide a basis for understanding phosphoregulation of glycogen synthesis. These results uncover a central molecular mechanism that governs glycogen metabolism.glucose metabolism | energy metabolism | glycogenesis | starch

show abstract

Mechanisms of Monomeric and Dimeric Glycogenin Autoglucosylation

Cited by 14 publications

References 22 publications

Vertebrate protein glycosylation: diversity, synthesis and function

Vertebrate protein glycosylation: diversity, synthesis and function

Glycosylation Quality Control by the Golgi Structure

Structural basis for the recruitment of glycogen synthase by glycogenin

Contact Info

Product

Resources

About