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Related Concept Videos

Covalently Linked Protein Regulators02:04

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.
Catenins01:23

Catenins

Catenins are characterized by multiple binding domains and dynamic structures that allow them to function as linker proteins in cell junction complexes. All catenins, except α-catenin, contain a characteristic protein sequence called the armadillo repeat and are therefore also called armadillo proteins.
Catenins in Cell Junctions
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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...
Protein Modifications in the RER01:26

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.
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...
Allosteric Proteins-ATCase01:19

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,...

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Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes
09:40

Co-immunoprecipitation Assay for Studying Functional Interactions Between Receptors and Enzymes

Published on: September 28, 2018

PTEN acetylation modulates its interaction with PDZ domain.

Tsuneo Ikenoue1, Ken Inoki, Bin Zhao

  • 1Life Sciences Institute, University of Michigan, Ann Arbor, USA.

Cancer Research
|September 2, 2008
PubMed
Summary

PTEN acetylation on Lys(402) by CBP and deacetylation by SIRT1 impacts its interaction with PDZ proteins. This finding suggests acetylation regulates PTEN tumor suppressor activity.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • The PTEN tumor suppressor gene is crucial for preventing cancer and its function requires tight regulation.
  • PTEN activity is known to be modulated by phosphorylation and membrane association.
  • The C-terminal region of PTEN contains a PDZ domain-binding motif involved in protein interactions.

Purpose of the Study:

  • To investigate the role of post-translational modifications, specifically acetylation, in regulating PTEN function.
  • To identify the enzymes responsible for PTEN acetylation and deacetylation.
  • To determine how PTEN acetylation affects its interaction with PDZ domain-containing proteins.

Main Methods:

  • Western blotting to detect PTEN acetylation.
  • Co-immunoprecipitation assays to assess PTEN interactions with PDZ proteins.
  • In vitro assays using recombinant CBP and SIRT1 to study PTEN acetylation/deacetylation.

Main Results:

  • PTEN is acetylated on Lysine 402 (Lys402), located within its C-terminal PDZ domain-binding motif.
  • CBP (CREB-binding protein) was identified as the primary acetyltransferase for PTEN.
  • SIRT1 (Sirtuin 1) was identified as the main deacetylase responsible for removing acetyl groups from PTEN.
  • Acetylation of Lys402 significantly alters PTEN's interaction with PDZ domain-containing proteins.

Conclusions:

  • PTEN acetylation, particularly at Lys402, represents a novel regulatory mechanism for its tumor suppressor activity.
  • The interplay between CBP-mediated acetylation and SIRT1-mediated deacetylation fine-tunes PTEN's cellular functions.
  • Targeting PTEN acetylation could offer new therapeutic strategies for cancers with PTEN inactivation.