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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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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...
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Protein Folding Quality Check in the RER01:29

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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...
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Oligosaccharide Assembly01:24

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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.
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During most eukaryotic translation processes, the small 40S ribosome subunit scans an mRNA from its 5' end until it encounters the first start AUG codon. The large 60S ribosomal subunit then joins the smaller one to initiate protein synthesis. The location of the translation initiation is largely determined by the nucleotides near the start codon as there may be multiple translation initiation sites present on the mRNA.  Marilyn Kozak discovered that the sequence RCCAUGG (where R...
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Covalently Linked Protein Regulators02:04

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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.
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Updated: Sep 28, 2025

LERLIC-MS/MS for In-depth Characterization and Quantification of Glutamine and Asparagine Deamidation in Shotgun Proteomics
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Polyglutamylation: biology and analysis.

Cristian I Ruse1, Hang Gyeong Chin2, Sriharsa Pradhan3

  • 1Moderna Therapeutics, 200 Technology Square, Cambridge, MA, 02139, USA. Cristian.Ruse@modernatx.com.

Amino Acids
|March 31, 2022
PubMed
Summary
This summary is machine-generated.

Polyglutamylation, a posttranslational modification, involves adding glutamate chains to proteins like tubulin. Proteomics methods now enable large-scale detection of these modified peptides, revealing key sites in tubulin and other proteins.

Keywords:
Mass spectrometryNanoESIPolyglutamylationProtein chemistryProteomicsTubulin

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Proteomics

Background:

  • Polyglutamylation is a posttranslational modification (PTM) involving glutamate addition to proteins by polyglutamylases.
  • This modification is well-documented in microtubules, affecting α- and β-tubulin subunits.
  • Recent research has elucidated catalytic mechanisms of glutamylation enzymes, particularly tubulin tyrosine ligase-like (TTLL) family.

Purpose of the Study:

  • To review advancements in using proteomics for large-scale polyglutamylated peptide detection.
  • To summarize the biology and analytical approaches for studying polyglutamylation.
  • To highlight newly identified polyglutamylation sites and enzymes.

Main Methods:

  • Utilizing nano-electrospray ionization (ESI) proteomic approaches for quantifiable site identification.
  • Employing nano-liquid chromatography and tandem mass spectrometry (MS/MS) for characterization.
  • Mapping variable length polyglutamylation using protein chemistry and proteomics.

Main Results:

  • Identified quantifiable polyglutamylated sites in specific substrates.
  • Characterized conjugated glutamylated peptides via MS/MS.
  • Revealed major polyglutamylation sites at E445 in α-tubulin, E435 in β-tubulin, and E860 in SdeA.

Conclusions:

  • Proteomics has significantly advanced the large-scale detection and analysis of polyglutamylated peptides.
  • Polyglutamylation extends beyond tubulin, with enzymes like SidJ identified.
  • Understanding polyglutamylation patterns is crucial for functional microtubule dynamics and cellular processes.