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Related Concept Videos

Gene Duplication and Divergence02:37

Gene Duplication and Divergence

The seminal work of Ohno in 1970 popularized the idea of gene duplication and divergence. DNA sequence comparison studies reveal that a large portion of the genes in bacteria, archaebacteria, and eukaryotes was  generated by gene duplication and divergence, indicating its critical role in evolution.
The duplicated copies of the gene are called Paralogs. Paralogs with similar sequences and functions form a gene family. Across several species, a large number of gene families are characterized.
Phosphorylation01:02

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...
Phosphorylation01:02

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...
Gene Families01:57

Gene Families

Gene families consist of groups of genes proposed to have originated from a common ancestor. Typically these arise through events in which a gene or genes are mistakenly duplicated during cell division. Unlike their parent genes (which are subject to selection pressure to maintain function), these gene copies do not need to preserve their sequences and may evolve at a relatively faster rate.
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...

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Related Experiment Video

Updated: May 31, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Phosphorylation network rewiring by gene duplication.

Luca Freschi1, Mathieu Courcelles, Pierre Thibault

  • 1Département de Biologie, Université Laval, Québec, Canada.

Molecular Systems Biology
|July 8, 2011
PubMed
Summary
This summary is machine-generated.

Gene duplication drives rapid evolution of protein phosphorylation, with most sites changing over 100 million years. Proteins often rewire kinase interactions, suggesting subfunctionalization in post-translational regulation.

More Related Videos

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Related Experiment Videos

Last Updated: May 31, 2026

Oligopeptide Competition Assay for Phosphorylation Site Determination
09:16

Oligopeptide Competition Assay for Phosphorylation Site Determination

Published on: May 18, 2017

Identification of Kinase-substrate Pairs Using High Throughput Screening
11:13

Identification of Kinase-substrate Pairs Using High Throughput Screening

Published on: August 29, 2015

Area of Science:

  • Evolutionary biology
  • Molecular biology
  • Systems biology

Background:

  • Understanding the evolution of complex regulatory networks requires studying gene duplication dynamics.
  • Post-translational modifications, like phosphorylation, play crucial roles in protein regulation and evolution.

Purpose of the Study:

  • To investigate the evolutionary changes in phosphorylation profiles of paralogous proteins.
  • To assess the impact of 100 million years of divergence on phosphorylation sites and kinase-substrate relationships.

Main Methods:

  • Comparative analysis of phosphorylation profiles between paralogous proteins in Saccharomyces cerevisiae and an ancestral species.
  • Quantification of phosphorylation site gain/loss and kinase-substrate network rewiring.

Main Results:

  • A majority of phosphorylation sites were gained or lost in one paralog over 100 million years, with a bias towards loss.
  • Paralogous proteins maintained similar phosphosite numbers, suggesting compensatory evolution.
  • Up to 50% of kinase-substrate relationships were rewired, indicating significant regulatory evolution.

Conclusions:

  • Post-gene duplication, proteins tend to subfunctionalize at the post-translational regulation level.
  • Significant turnover of kinases phosphorylating preserved phosphosites occurs over evolutionary time.