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Oligosaccharide Assembly

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
Multiple sugar molecules that may or may...

Protein Glycosylation

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...

Proteoglycans

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...

Protein Modifications in the RER

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal...

Protein Folding Quality Check in the RER

Protein Folding Quality Check in the RER

ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...

Amyloid Fibrils

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Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
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Updated: Sep 1, 2025

Analysis of SCAP N-glycosylation and Trafficking in Human Cells

Analysis of SCAP N-glycosylation and Trafficking in Human Cells

Published on: November 8, 2016

CREB-associated glycosylation and function in human disease.

Ning Zhang¹, Liu Shi¹, Yuli Wang²

¹Division of Gastroenterology, The Affiliated Ganzhou Hospital of Nanchang University, China.

Advances in Clinical and Experimental Medicine : Official Organ Wroclaw Medical University

|August 11, 2022

Summary

Glycosylation modification of cyclic adenosine monophosphate (cAMP) response element-binding protein (CREB) is emerging as a key regulator of gene expression and disease. This review explores current insights into CREB glycosylation

Keywords:

CREB function glycosylation modification

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Last Updated: Sep 1, 2025

Analysis of SCAP N-glycosylation and Trafficking in Human Cells

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Published on: November 8, 2016

Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins

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Pulse-chase Analysis of N-linked Sugar Chains from Glycoproteins in Mammalian Cells

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Published on: April 27, 2010

Area of Science:

Proteomics and Post-Translational Modifications
Molecular Biology and Gene Regulation
Cellular Signaling and Disease Pathogenesis

Background:

Proteomics is gaining prominence over mRNA sequencing for understanding biological functions.
Post-translational modifications (PTMs) like glycosylation significantly impact protein function and disease, despite not altering basic physicochemical properties.
Cyclic adenosine monophosphate (cAMP) response element-binding protein (CREB) is a critical transcription regulator implicated in neurodegenerative diseases, cancer, and neurogenesis.

Purpose of the Study:

To comprehensively review current research on CREB glycosylation.
To elucidate the role of CREB glycosylation in regulating gene expression.
To evaluate the impact of CREB glycosylation on disease development.

Main Methods:

Literature review of existing studies on CREB.
Analysis of research focusing on protein glycosylation.
Synthesis of findings on CREB glycosylation and its functional consequences.

Main Results:

While CREB phosphorylation has been extensively studied, CREB glycosylation is an emerging area of research.
Glycosylation of CREB influences targeted gene expression.
CREB glycosylation plays a role in the initiation and development of various diseases.

Conclusions:

CREB glycosylation is a critical regulatory mechanism for gene function.
Further investigation into CREB glycosylation is essential for understanding its role in health and disease.
Targeting CREB glycosylation may offer new therapeutic strategies for related diseases.