How cells build and control a key enzyme that regulates protein phosphorylation
Protein Phosphatase 1 Holoenzyme Formation
['FUNDING_R01'] · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · NIH-11169775
This work looks at how two helper proteins assemble and control a central enzyme involved in phosphorylation, with relevance to cancers and future treatments for people affected by them.
Quick facts
| Phase | ['FUNDING_R01'] |
|---|---|
| Study type | Nih_funding |
| Sex | All |
| Sponsor | UNIVERSITY OF CONNECTICUT SCH OF MED/DNT (nih funded) |
| Locations | 1 site (FARMINGTON, UNITED STATES) |
| Trial ID | NIH-11169775 on ClinicalTrials.gov |
What this research studies
Researchers will study two regulator proteins (SDS22 and Inhibitor-3) that guide the formation and activity of Protein Phosphatase 1 (PP1), a major enzyme that removes phosphate tags from other proteins. The team will use biochemical experiments and cell models, including insights from yeast and mammalian cells, to map how these helpers bind and control PP1. They will track where and when PP1 is active inside cells and how misregulation could contribute to disease processes like cancer. Results aim to clarify the mechanisms by which phosphorylation balance is maintained and how its disruption leads to pathology.
Who could benefit from this research
Good fit: People with cancer—especially tumors thought to involve abnormal phosphorylation signaling—or patients willing to donate tumor samples for basic research may eventually be relevant to this work.
Not a fit: Patients looking for immediate treatment changes or those with conditions unrelated to phosphorylation or cancer are unlikely to receive direct benefit from this basic laboratory research.
Why it matters
Potential benefit: If successful, this research could reveal new molecular targets or strategies for therapies or diagnostics in cancers driven by phosphorylation dysregulation.
How similar studies have performed: Related biochemical and cell-biology studies have uncovered important cancer mechanisms and drug targets, but the specific roles and mechanisms of SDS22 and Inhibitor-3 remain largely untested and novel.
Where this research is happening
FARMINGTON, UNITED STATES
- UNIVERSITY OF CONNECTICUT SCH OF MED/DNT — FARMINGTON, UNITED STATES (ACTIVE)
Researchers
- Principal investigator: PETI, WOLFGANG — UNIVERSITY OF CONNECTICUT SCH OF MED/DNT
- Study coordinator: PETI, WOLFGANG
About this research
- This is an active NIH-funded research project — typically early-stage science, not a clinical trial accepting patient enrollment.
- Some NIH-funded labs run parallel clinical studies or seek volunteers for related work. To check, contact the principal investigator or institution listed above.
- For full project details, budget, and progress reports, visit the official NIH RePORTER page below.
Conditions: Cancers