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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.

Proteomics

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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...

Proteins: From Genes to Degradation

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick. Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...

Proteins: From Genes to Degradation

Proteins: From Genes to Degradation

Within a biological system, the DNA encodes the RNA, and the nucleotide sequence in the RNA further defines the amino acid sequence in the protein. This is referred to as “The Central Dogma of Molecular Biology” - a term coined by Francis Crick. Central dogma is a firm principle in biology that defines the flow of genetic information within any life form. The two fundamental steps in central dogma are - transcription and translation.
Transcription is the synthesis of RNA molecules by RNA...

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Related Experiment Video

Updated: May 27, 2026

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

Published on: February 27, 2020

VDAC proteomics: post-translation modifications.

Janos Kerner¹, Kwangwon Lee, Bernard Tandler

¹Center for Mitochondrial Diseases, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.

Biochimica Et Biophysica Acta

|November 29, 2011

Summary

This summary is machine-generated.

Voltage-dependent anion channels (VDACs) are crucial mitochondrial gatekeepers. This review explores how posttranslational modifications, particularly phosphorylation, impact VDAC function and protein interactions, influencing cellular processes.

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Simultaneous Affinity Enrichment of Two Post-Translational Modifications for Quantification and Site Localization

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A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

A Fast and Quantitative Method for Post-translational Modification and Variant Enabled Mapping of Peptides to Genomes

Published on: May 22, 2018

Area of Science:

Mitochondrial biology
Cellular metabolism
Protein regulation

Background:

Voltage-dependent anion channels (VDACs) are key proteins in the mitochondrial outer membrane, regulating transport and cellular functions.
VDACs exist in three isoforms (VDAC1-3) and are involved in metabolite exchange, energy transfer, and apoptosis.
VDAC functions are modulated by interactions with other proteins and by posttranslational modifications.

Purpose of the Study:

To review recent findings on posttranslational modifications of VDACs.
To discuss the physiological consequences of these modifications on VDAC function and interactions.

Main Methods:

Literature review of recent research on VDAC posttranslational modifications.
Analysis of studies investigating the functional outcomes of VDAC modifications.

Main Results:

Posttranslational modifications, primarily phosphorylation, significantly affect VDAC activity and protein binding.
These modifications influence VDAC's role in mitochondrial metabolism and cell death pathways.
Specific modifications lead to distinct physiological outcomes, highlighting VDAC's regulatory complexity.

Conclusions:

Posttranslational modification is a critical regulatory mechanism for VDAC function.
Understanding VDAC modifications provides insights into mitochondrial regulation and potential therapeutic targets.
Further research into VDAC modification dynamics is essential for comprehending mitochondrial health and disease.