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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...
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G protein-coupled receptor (GPCR) signaling plays a crucial role in cell functioning. GPCR desensitization is an equally essential process. It allows cells to respond to changing environments and regain sensitivity to new stimuli while preventing unnecessary stimulation when no longer needed. Prolonged exposure to stimuli leads to GPCR desensitization. It involves blocking the receptors from binding and activating additional G proteins. This inhibits activation of downstream effectors, thereby...
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Structural proteomics defines a sequential priming mechanism for the progesterone receptor.

Matthew D Mann1,2, Min Wang3, Josephine C Ferreon4

  • 1Skaggs Graduate School of Chemical and Biological Sciences, Scripps Research, La Jolla, CA, USA.

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Progesterone receptor (PR) interactions with co-regulators (CoRs) are key in breast cancer. This study reveals specific binding mechanisms and unique interaction surfaces, challenging current models of nuclear receptor function.

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Area of Science:

  • Molecular biology
  • Structural biology
  • Cancer research

Background:

  • Progesterone receptor (PR) has two isoforms, PR-A and PR-B, crucial for cellular signaling.
  • Disrupted PR signaling is linked to breast cancer via interactions with co-regulatory proteins (CoRs).
  • The precise molecular details of how PR isoforms interact with CoRs are not well understood.

Purpose of the Study:

  • To investigate the sequential binding mechanism of PR isoforms and CoRs (SRC3 and p300) on target DNA.
  • To elucidate the structural basis of PR-CoR interactions at a peptide level.
  • To understand how antagonist binding affects PR-CoR interactions.

Main Methods:

  • Structural mass spectrometry was employed to analyze purified full-length PR and intact CoRs.
  • Complexes were studied on target DNA to mimic physiological conditions.
  • Peptide-level analysis provided insights into protein-protein interactions.

Main Results:

  • Selective binding of CoR NR-boxes by PR was observed.
  • Unique interaction surfaces between PR and CoRs were identified during complex assembly.
  • Antagonist-bound PR maintained persistent CoR interactions, contrary to established models.

Conclusions:

  • This study provides a structural framework for understanding sequential CoR binding to PR.
  • The findings offer a peptide-level perspective on the progesterone receptor transcriptional complex organization.
  • Observed persistent CoR interactions with antagonist-bound PR challenge classical models of nuclear receptor regulation.