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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.

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.

Post-translational Translocation of Proteins to the RER

Post-translational Translocation of Proteins to the RER

A sizable fraction of proteins destined for ER are first synthesized in the cell cytosol and then transported across the ER membrane–a process called post-translational translocation. Similar to cotranslationally translocated proteins, these proteins also use the Sec translocon complex to enter the ER lumen.
Targeting proteins to the ER
Hsp40 and Hsp70 chaperone molecules bind the translated proteins in the cytosol to prevent their folding. The chaperone binding helps to keep the signal...

Phosphorylation

Phosphorylation

The addition or removal of phosphate groups from proteins is the most common chemical modification that regulates cellular processes. These modifications can affect the structure, activity, stability, and localization of proteins within cells as well as their interactions with other proteins.
During phosphorylation, protein kinases transfer the terminal phosphate group of ATP to specific amino acid side chains of substrate proteins. Serine, threonine, and tyrosine are the most commonly...

Conservative Site-specific Recombination and Phase Variation

Conservative Site-specific Recombination and Phase Variation

Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
The recognition sites for Cre recombinase called LoxP...

Pre-mRNA Processing: Modification of pre-mRNA Ends

Pre-mRNA Processing: Modification of pre-mRNA Ends

In eukaryotic cells, transcripts made by RNA polymerase are modified and processed before exiting the nucleus. Unprocessed RNA is called precursor mRNA or pre-mRNA to distinguish it from mature mRNA.
Once about 20-40 ribonucleotides have been joined together by RNA polymerase, a group of enzymes adds a cap to the 5' end of the growing transcript. In this process, a 5' phosphate is replaced by modified guanosine that has a methyl group attached (7-methyl guanosine). This 5' cap helps the cell...

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Related Experiment Video

Updated: Jun 10, 2026

Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins

Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins

Published on: April 27, 2019

Post-translational modification by SUMO.

Zara Hannoun¹, Sebastian Greenhough, Ellis Jaffray

¹Medical Research Council-Centre for Regenerative Medicine, University of Edinburgh, Chancellor's Building, 49 Little France Crescent, Edinburgh EH164SB, UK.

|August 3, 2010

Summary

This summary is machine-generated.

This review explores protein SUMOylation, a key post-translational modification (PTM), and its critical functions in stem and somatic cell biology. Understanding SUMOylation advances cell biology models and drug discovery.

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Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins

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In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

In Vivo Detection and Analysis of Rb Protein SUMOylation in Human Cells

Published on: November 2, 2017

Area of Science:

Biochemistry
Cell Biology
Molecular Biology

Background:

Post-translational modifications (PTMs) are crucial for regulating protein stability and function.
Reversible phosphorylation and SUMOylation are significant PTMs involved in diverse cellular processes.
SUMOylation impacts cell cycle, gene transcription, differentiation, and localization.

Purpose of the Study:

To review the role of protein SUMOylation in stem cell biology.
To review the role of protein SUMOylation in somatic cell biology.
To highlight the importance of SUMOylation in advancing cell biology models for drug discovery.

Main Methods:

Literature review of existing studies on protein SUMOylation.
Analysis of SUMOylation's involvement in stem cell differentiation and function.
Examination of SUMOylation's role in somatic cell processes.

Main Results:

SUMOylation is a vital PTM affecting numerous proteins across cellular functions.
Specific roles of SUMOylation in stem cell pluripotency and differentiation are elucidated.
SUMOylation's influence on somatic cell activities like transcription and localization is detailed.

Conclusions:

Protein SUMOylation is integral to stem and somatic cell biology.
Further understanding of SUMOylation can enhance cell biology models.
Investigating SUMOylation pathways can accelerate the drug discovery process.