Search research articles

ABOUT JoVE

Overview Leadership Blog JoVE Help Center

AUTHORS

Publishing Process Editorial Board Scope & Policies Peer Review FAQ Submit

LIBRARIANS

Testimonials Subscriptions Access Resources Library Advisory Board FAQ

RESEARCH

JoVE Journal Methods Collections JoVE Encyclopedia of Experiments Archive

EDUCATION

JoVE Core JoVE Business JoVE Science Education JoVE Lab Manual Faculty Resource Center Faculty Site

Terms & Conditions of Use

Related Concept Videos

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...

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 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 sequences.

Covalently Linked Protein Regulators

Covalently Linked Protein Regulators

Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein.

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 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...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by

Same author

Selective N-Terminal Modification of Peptides and Proteins Using Fatty Acyl Phosphates.

Angewandte Chemie (International ed. in English)·2026

Same author

Direct analysis of biotransformations with mass spectrometry-DiBT-MS.

Nature protocols·2025

Same author

Stereoselective Chemoenzymatic Cascades for the Synthesis of Densely Functionalized Iminosugars.

Journal of the American Chemical Society·2025

Same author

Biocatalysis in Asia and the Pacific.

JACS Au·2024

Same author

Carboligation towards production of hydroxypentanones.

Journal of biotechnology·2024

Same author

Characterising glycosaminoglycans in human breastmilk and their potential role in infant health.

Microbial cell (Graz, Austria)·2024

Same journal

Cryo-EM sheds light on the mechanism of human telomerase inhibition by BIBR1532.

Nature chemical biology·2026

Same journal

Artificial metalloenzymes in complex biological environments.

Nature chemical biology·2026

Same journal

Allosteric disordering of eIF2B regulates the integrated stress response.

Nature chemical biology·2026

Same journal

A tail of two ligases.

Nature chemical biology·2026

Same journal

Non-canonical cytochrome P450 enzymes expand the diversity of bacterial hemoproteins.

Nature chemical biology·2026

Same journal

Image-guided activation of drugs with electromagnetic radiation.

Nature chemical biology·2026

See all related articles

Search research articles

Related Experiment Video

Updated: Jun 5, 2026

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

Post-translational modifications: S-linked sugars lost and found

Róbert Sardzík, Peter Both, Sabine L Flitsch

Nature Chemical Biology

|January 20, 2011

Summary

No abstract available in PubMed .

More Related Videos

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

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

Published on: April 27, 2010

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

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

Published on: October 4, 2017

Related Experiment Videos

Last Updated: Jun 5, 2026

Utilizing a Comprehensive Immunoprecipitation Enrichment System to Identify an Endogenous Post-translational Modification Profile for Target Proteins

Published on: January 8, 2018

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

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

Published on: April 27, 2010

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

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

Published on: October 4, 2017