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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.
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Protein Complexes with Interchangeable Parts01:57

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.
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Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the daughter...
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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...
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.
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The polycomb protein Pc2 is a SUMO E3.

Michael H Kagey1, Tiffany A Melhuish, David Wotton

  • 1Department of Biochemistry and Molecular Genetics, Center for Cell Signaling, University of Virginia, Charlottesville, VA 22908, USA.

Cell
|April 8, 2003
PubMed
Summary
This summary is machine-generated.

Polycomb protein Pc2 enhances sumoylation of CtBP, a transcriptional corepressor. This suggests Pc2 acts as a SUMO E3 ligase, positioning PcG bodies as key sumoylation centers.

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Area of Science:

  • Molecular Biology
  • Epigenetics
  • Protein Biochemistry

Background:

  • Polycomb group (PcG) proteins regulate gene expression through large complexes called PcG bodies.
  • The human PcG protein, Pc2, interacts with the transcriptional corepressor CtBP within PcG bodies.

Purpose of the Study:

  • To investigate the role of Pc2 in the modification of CtBP.
  • To determine if Pc2 influences CtBP sumoylation and to elucidate the mechanism.

Main Methods:

  • In vitro sumoylation assays using purified proteins.
  • In vivo studies examining protein localization and interactions within PcG bodies.
  • Biochemical analysis of CtBP modification.

Main Results:

  • CtBP undergoes sumoylation at a single lysine residue.
  • CtBP sumoylation requires SUMO E1, E2 (Ubc9), and SUMO-1.
  • Pc2 significantly enhances CtBP sumoylation in vitro and in vivo.
  • Pc2 facilitates sumoylation by recruiting CtBP and Ubc9 to PcG bodies.

Conclusions:

  • Pc2 functions as a SUMO E3 ligase for CtBP.
  • PcG bodies serve as centers for sumoylation reactions.
  • This mechanism highlights a novel regulatory role for PcG proteins in gene expression.