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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.

Allosteric Proteins-ATCase

Allosteric Proteins-ATCase

Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis pathway,...

Anaphase Promoting Complex

Anaphase Promoting Complex

The stepwise destruction of specific proteins is necessary for the progression and completion of the cell cycle. Such proteins are ubiquitinated by ubiquitin ligases and then subsequently destroyed by the proteasome. The SCF (Skp1/Cullin/F-box) and the anaphase-promoting complex (APC) are two important ubiquitin ligases involved in cell cycle progression. While SCF is active throughout the cell cycle, APC gets activated during metaphase to anaphase transition. Cdc20 or Cdh1 binds to APC and...

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...

Regulation of Nuclear Protein Sorting

Regulation of Nuclear Protein Sorting

Nuclear protein sorting regulates nucleus composition and gene expression, crucial for determining the fate of a eukaryotic cell. Hence, the entry and exit of molecules across the nuclear envelope is a tightly controlled process. Nuclear protein sorting can be inhibited by one of the following ways: 1) masking cargo signal sequences, 2) modifying the nuclear receptor's affinity for cargo, 3) controlling the nuclear pore size, 4) retaining the cargo during its transit to the cytosol or the...

Phase II Reactions: Acetylation Reactions

Phase II Reactions: Acetylation Reactions

Acetylation, a phase II biotransformation reaction, introduces an acetyl group to drugs or their metabolites. Acetyltransferase enzymes facilitate this reaction, which resembles α-amino acid conjugation due to the addition of a functional group to the drug molecule.
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Related Experiment Video

Updated: May 20, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

Published on: December 9, 2017

Acetylation-dependent regulation of Skp2 function.

Hiroyuki Inuzuka¹, Daming Gao, Lydia W S Finley

¹Department of Pathology, Beth Israel Deaconess Medical Center, Harvard Medical School, Boston, MA 02215, USA.

|July 10, 2012

Summary

Aberrant Skp2 acetylation, regulated by p300 and SIRT3, increases Skp2 stability and promotes cancer cell migration and proliferation. This acetylation mechanism governs Skp2

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Last Updated: May 20, 2026

A Facile Protocol to Generate Site-Specifically Acetylated Proteins in Escherichia Coli

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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

Area of Science:

Molecular Oncology
Epigenetics
Cancer Biology

Background:

Aberrant Skp2 signaling is a key driver in tumorigenesis.
Cytoplasmic Skp2 correlates with aggressive breast and prostate cancers, but mechanisms are unclear.

Purpose of the Study:

To elucidate the acetylation-dependent regulation of Skp2.
To investigate the role of cytoplasmic Skp2 in cancer progression.

Main Methods:

Investigated Skp2 acetylation by p300 and deacetylation by SIRT3.
Analyzed Skp2 stability and proteolysis via the Cdh1 pathway.
Utilized acetylation-mimetic mutants to assess cellular proliferation and tumorigenesis.
Examined Skp2 localization, E-cadherin ubiquitination, and cellular migration.

Main Results:

Skp2 is acetylated by p300 at K68 and K71, antagonized by SIRT3.
SIRT3 inactivation increases Skp2 acetylation, enhancing stability by inhibiting Cdh1-mediated degradation.
Acetylation-mimetic Skp2 mutants show increased proliferation and tumorigenesis.
Skp2 acetylation in the nuclear localization signal (NLS) promotes cytoplasmic retention.
Cytoplasmic Skp2 enhances migration by promoting E-cadherin ubiquitination and degradation.

Conclusions:

Identified a novel acetylation-dependent regulatory mechanism for Skp2 oncogenic function.
Demonstrated that cytoplasmic Skp2 controls cellular migration through E-cadherin regulation.
Provides mechanistic insight into Skp2's role in aggressive cancers.