# REGULATION OF PROGESTERONE RECEPTORS BY PHOSPHORYLATION

> **NIH NIH R01** · BAYLOR COLLEGE OF MEDICINE · 1993 · $158,375

## Abstract

The long term goal of this project is to determine the role of
phosphorylation in the regulation of chicken progesterone receptor (PR)
function.  PR is a member of a superfamily of ligand activated
transcription factors including the other steroid receptors, Vitamin D,
retinoic acid, and thyroid receptors as well as other proteins whose
ligand if any has not yet been identified.  Recent studies have shown
that phosphorylation is a key mechanism for regulating the activity of
transcription factors.  We have identified 5 phosphorylation sites in the
receptor which can be divided into three classes--l.  Sites which are
partially phosphorylated, but whose phosphorylation increases in response
to progesterone administration. 2.  Sites phosphorylated only in response
to progesterone administration. 3. Sites which are constitutively
phosphorylated.  The specific aims for the next grant period are first,
to determine the role of individual phosphorylations in PR function by
analysis of receptor site mutants.  Glycine, which will mimic the
dephosphorylated state, and aspartic acid which may mimic the
phosphorylated state, will be substituted for serine.  The effect of
these mutations on transcription, DNA binding and interactions with other
proteins will be examined to determine the role of each phosphorylation
site.  Second, additional constitutive phosphorylation sites will be
identified using the methods used for the hormone dependent sites and the
role of the sites studied as described above.  Finally, most analyses of
steroid hormone receptor function have been performed using receptor from
tissue which has not been treated with hormone.  Numerous studies have
shown that hormone administration results in increased steroid receptor
phosphorylation and it is presumably this form which is active in vivo.
Therefore, we will purify receptor from progesterone treated animals, and
the activities of this modified receptor will be compared to receptor
from untreated animals.  These studies will provide a good understanding
of the role of phosphorylation in PR function.  Since PR belongs to a
superfamily of transcription factors, the information obtained will
provide a basis for understanding and testing the role of phosphorylation
of the related regulatory proteins.

## Key facts

- **NIH application ID:** 2198435
- **Project number:** 5R01HD022061-06
- **Recipient organization:** BAYLOR COLLEGE OF MEDICINE
- **SAM.gov UEI:** FXKMA43NTV21
- **Principal Investigator:** Nancy L. Weigel
- **Activity code:** R01 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 1993
- **Award amount:** $158,375
- **Award type:** 5
- **Project period:** 1986-07-01 → 1995-06-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/2198435

## Citation

> US National Institutes of Health, RePORTER application 2198435, REGULATION OF PROGESTERONE RECEPTORS BY PHOSPHORYLATION (5R01HD022061-06). Retrieved via MORVS 2026-10-25 from https://api.morvs.ai/grant/nih/2198435. Licensed CC0.

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