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Structural proteomics defines a sequential priming mechanism for the progesterone receptor.

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

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This study reveals how progesterone receptor (PR) isoforms interact with co-regulators (CoRs) like SRC3 and p300. Findings show selective binding and persistent interactions, even with antagonists, offering new insights into breast cancer mechanisms.

Keywords:
Progesterone receptorcrosslinkinghydrogen-deuterium exchangemass spectrometrynuclear receptorsprotein-protein interactionstranscriptional co-regulatory proteins

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • The progesterone receptor (PR) is a nuclear receptor with two isoforms, PR-A and PR-B, crucial for cellular function.
  • Disruption of PR signaling is linked to breast cancer development via interactions with co-regulatory proteins (CoRs).
  • Detailed molecular mechanisms 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, p300) on target DNA.
  • To elucidate the structural basis of isoform-specific PR-CoR interactions.
  • To understand the role of PR conformation (active vs. inactive) in CoR binding.

Main Methods:

  • Utilized structural mass spectrometry to analyze purified full-length PR and intact CoRs (SRC3, p300).
  • Examined protein complexes assembled on target DNA.
  • Investigated interactions in both antagonist-bound and presumably active conformations.

Main Results:

  • Revealed selective binding of CoR NR-boxes by PR.
  • Identified unique interaction surfaces between PR and CoRs during complex assembly.
  • Observed persistent CoR interactions with antagonist-bound PR, challenging traditional models.

Conclusions:

  • Provided a peptide-level structural perspective on the PR transcriptional complex organization.
  • Inferred mechanisms governing PR-CoR interactions in both active and inactive states.
  • Highlighted the complexity of nuclear receptor regulation beyond classical activation/repression models.