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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 Complexes with Interchangeable Parts

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...

The Proteasome

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...

Intralumenal Vesicles and Multivesicular Bodies

Intralumenal Vesicles and Multivesicular Bodies

Intraluminal vesicles (ILVs) are small vesicles 50-80 nm in diameter formed during the maturation of early endosomes. A specialized endosome containing numerous ILVs is called a multivesicular body (MVB). ILVs contain internalized molecules such as antigens, nucleic acids, proteins, and metabolites. Some of these molecules are released from the MVBs inside exosomes and are transported to other cells. Other MVBs contain molecules that are retained in the ILVs and are later degraded within the...

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.

The Proteasome

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...

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Related Experiment Video

Updated: May 16, 2026

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Ubiquitin Chain Analysis by Parallel Reaction Monitoring

Published on: June 17, 2020

Ubiquitin branches out.

Erica S Johnson¹

¹Department of Biochemistry and Molecular Pharmacology, Thomas Jefferson University, Philadelphia, PA 19107, USA. Erica.Johnson@mail.tju.edu

Nature Cell Biology

|December 4, 2002

Summary

This summary is machine-generated.

Ubiquitin (Ub) and related proteins have expanded roles beyond protein breakdown. Research presented at the ASCB meeting highlighted these diverse, non-traditional functions in cell biology.

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Ubiquitin Chain Analysis by Parallel Reaction Monitoring

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Area of Science:

Cell Biology
Molecular Biology
Biochemistry

Background:

Ubiquitin (Ub) traditionally known for proteasomal degradation.
Emerging roles in non-proteolytic cellular processes.
Proliferation of Ubiquitin-like (UBL) proteins with covalent attachment functions.

Framework:

Focus on non-traditional functions of Ub and UBL proteins.
Exploration of diverse regulatory mechanisms.
Understanding covalent modification pathways.

Implementation:

Summarizing key findings from the ASCB meeting.
Highlighting novel research areas.
Showcasing the breadth of Ub and UBL protein involvement.

Implications:

Broadens understanding of Ubiquitin's cellular roles.
Reveals new regulatory networks.
Opens avenues for therapeutic targets.