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Related Concept Videos

The Proteasome Structure01:17

The Proteasome Structure

The ubiquitin-proteasome pathway is a well-known mechanism utilized by eukaryotic cells to remove cytoplasmic proteins that are misfolded, damaged, or no longer needed. In this pathway, the protein that needs to be eliminated undergoes a process called ubiquitination, where a chain of ubiquitin molecules is attached to the 48th lysine residue of the target protein. This ubiquitin modification helps the proteasome distinguish between a target protein and a healthy protein.
The proteasome is an...
The Proteasome01:13

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important among these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. This involves participation of a series of enzymes including— E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3 (ubiquitin...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
In this pathway, the target proteins are first tagged with small proteins called ubiquitin. A series of enzymes carry out the ubiquitination of the target proteins - E1 (ubiquitin-activating enzyme), E2 (ubiquitin-conjugating enzyme), and E3...
The Proteasome02:18

The Proteasome

Eukaryotic cells can degrade proteins through several pathways. One of the most important amongst these is the ubiquitin-proteasome pathway. It helps the cell eliminate the misfolded, damaged, or unwarranted cytoplasmic proteins in a highly specific manner.
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
The Spindle Assembly Checkpoint02:19

The Spindle Assembly Checkpoint

The spindle assembly checkpoint is a molecular surveillance mechanism ensuring the fidelity of chromosome segregation during anaphase. The checkpoint monitors the completion of all the prerequisite steps before chromosome segregation to determine whether the segregation process should proceed or be delayed.
Many proteins function together to control the spindle assembly checkpoint. Mutations affecting these proteins may allow cells to proceed into anaphase prematurely, resulting in the...

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Assaying Proteasomal Degradation in a Cell-free System in Plants
07:43

Assaying Proteasomal Degradation in a Cell-free System in Plants

Published on: March 26, 2014

Staying the distance: avoiding the proteasomal trap.

Michael Downes1, Ronald M Evans

  • 1Howard Hughes Medical Institute, Gene Expression Laboratory, Salk Institute for Biological Studies, 10010 Torrey Pines Road, La Jolla, CA 92037, USA.

Cancer Cell
|March 11, 2008
PubMed
Summary
This summary is machine-generated.

Estrogen signaling relies on SRC-3, a coactivator. Atypical PKC prevents SRC-3 degradation, enhancing estrogenic gene activity and potentially impacting breast cancer.

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Area of Science:

  • Molecular Biology
  • Endocrinology
  • Cancer Research

Background:

  • Nuclear receptor coactivators play crucial roles in hormone signaling pathways.
  • Specificity in hormone signaling is often attributed to the receptor and ligand, but coactivators like SRC-3 are increasingly recognized for their distinct functions.
  • SRC-3 (Steroid Receptor Coactivator-3) is notably linked to cell growth regulation.

Purpose of the Study:

  • To investigate the role of SRC-3 in estrogen signaling.
  • To elucidate the mechanism by which SRC-3 activity is regulated.
  • To explore the implications of SRC-3 regulation in hormone-sensitive cancers.

Main Methods:

  • The study utilized molecular biology techniques to examine protein interactions and modifications.
  • Assays were performed to assess the impact of atypical PKC on SRC-3 stability.
  • Gene activity was measured to determine the effect of SRC-3 modulation on estrogenic responses.

Main Results:

  • Estrogen-induced posttranslational modification of SRC-3 by atypical PKC was demonstrated.
  • This modification protects SRC-3 from proteasomal degradation, leading to its stabilization.
  • Stabilized SRC-3 enhances estrogenic gene activity.

Conclusions:

  • Atypical PKC-mediated regulation of SRC-3 is a key mechanism controlling estrogenic gene activity.
  • This pathway may represent an important target for therapeutic intervention in hormone-sensitive tumors.
  • The findings highlight the critical role of SRC-3 in estrogen-driven processes, particularly in breast cancer.