Thursday, February 19, 2026 2/19/2026

J-Protein Regulation of Yeast Prion Propagation

Award Number: R15GM110606
ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
OPDIV: NIH
AWARD CLASS: DISCRETIONARY
AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)
PERIOD OF PERFORMANCE START DATE: 07/01/2014
PERIOD OF PERFORMANCE END DATE: 08/31/2028

Group Awards By:

View Award Description

J-Protein Regulation of Yeast Prion Propagation - A critical barrier to advancing the understanding of chaperone function in prion biology is that the fundamental chaperone interactions for most yeast prions remain unidentified. Existing knowledge is disjointed due to a lack of systematic evaluation that controls for variation in yeast strain background and prion structure. The continued existence of this barrier is an important problem because, until it is overcome, an understanding of how protein sequences give rise to amyloids with distinct patterns of chaperone interaction cannot be fully realized. The long- term goal is to utilize the highly tractable budding yeast, S. cerevisiae, to systematically decipher the complex relationships between amyloid-forming yeast prions and molecular chaperone proteins with a goal of better un- derstanding J-domain protein (JDP) function and prion behavior. The objective of this particular application is to utilize genetic systems and biochemical assays to determine the functional elements involved in specific prion- chaperone interactions. The central hypothesis is that differences in amyloid structure, arising primarily from amino acid composition, create distinct challenges for prion transmission which are overcome by specific JDP functions that buffer prions against loss during mitosis. The hypothesis has been formulated on the basis of data produced in the applicant’s laboratory. The rationale for the proposed research is that unambiguous determina- tions of JDP functional requirements are a necessary step toward understanding the mechanisms of chaperone function in amyloid biology. Using a distinct set of chimeric prions, our own collection of well-studied, naturally occurring prions, and the yeast cytosol as model systems, this hypothesis will be tested by pursuing two specific aims: 1) Identify elements of J-domain proteins that allow for amyloid conformer-specific propagation and prion elimination, and 2) Determine the impact of individual amino acid identities, and Q vs. N-richness, on prion- chaperone interactions. Proven yeast genetic manipulations, which have been established as feasible in the applicant’s laboratory, will be the primary methods used to accomplish these aims. The approach is innovative because it represents a substantive departure from the status quo by placing emphasis on the ability to draw distinctions and make comparisons among multiple JDPs and yeast prions as a way to broadly understand chaperone function. The contribution of the proposed research is expected to be the elucidation of the roles of distinct chaperones in prion propagation and prion elimination. This contribution is significant because it is the next step in a continuum of research which is expected to contribute to the understanding of the biochemical basis of amyloid-chaperone interactions. A molecular understanding of amyloid-chaperone interactions has the potential to inform the development of interventions for protein misfolding disorders, including the increasing prevalent neurodegenerative disorders Alzheimer’s and Parkinson’s.


Issue Date FY	Funding FY	Legal Entity Name	Legal Entity Address	Legal Entity City	Legal Entity State	Legal Entity Zip Code	Legal Entity COUNTY	Legal Entity COUNTRY	Assistance Listing	Award Code	Budget Year	Action Date	Action Type	Action Amount

Issue Date FY: 2025 ( Subtotal = $553,785 )
2025	2025	LAFAYETTE COLLEGE	730 SULLIVAN RD	EASTON	PA	18042	NORTHAMPTON	USA	Biomedical Research and Research Training	000	4	8/8/2025	COMPETING CONTINUATION	$553,785
														Subtotal = $553,785

Issue Date FY: 2024 ( Subtotal = $0 )
2024	2021	LAFAYETTE COLLEGE	730 SULLIVAN RD	EASTON	PA	18042	NORTHAMPTON	USA	Biomedical Research and Research Training	000	3	8/7/2024	COMPETING CONTINUATION	$0
														Subtotal = $0

Issue Date FY: 2022 ( Subtotal = $0 )
2022	2021	LAFAYETTE COLLEGE	730 SULLIVAN RD	EASTON	PA	18042	NORTHAMPTON	USA	Biomedical Research and Research Training	001	3	3/2/2022	COMPETING CONTINUATION	$4,374
2022	2017	LAFAYETTE COLLEGE	730 SULLIVAN RD	EASTON	PA	18042	NORTHAMPTON	USA	Biomedical Research and Research Training	000	2	3/2/2022	COMPETING CONTINUATION	-$4,374
														Subtotal = $0

Issue Date FY: 2021 ( Subtotal = $442,683 )
2021	2021	LAFAYETTE COLLEGE	730 SULLIVAN RD	EASTON	PA	18042	NORTHAMPTON	USA	Biomedical Research and Research Training	000	3	8/11/2021	COMPETING CONTINUATION	$442,683
														Subtotal = $442,683

Issue Date FY: 2018 ( Subtotal = $0 )
2018	2014	LAFAYETTE COLLEGE	730 HIGH ST	EASTON	PA	18042	NORTHAMPTON	USA	Biomedical Research and Research Training	000	1	6/5/2018	NEW	$0
														Subtotal = $0

Issue Date FY: 2017 ( Subtotal = $394,870 )
2017	2017	LAFAYETTE COLLEGE	730 HIGH ST	EASTON	PA	18042	NORTHAMPTON	USA	Biomedical Research and Research Training	001	2	8/28/2017	COMPETING CONTINUATION	$394,870
2017	2014	LAFAYETTE COLLEGE	730 HIGH ST	EASTON	PA	18042	NORTHAMPTON	USA	Biomedical Research and Research Training	000	1	8/28/2017	NEW	$0
														Subtotal = $394,870

Issue Date FY: 2014 ( Subtotal = $268,220 )
2014	2014	LAFAYETTE COLLEGE	219 MARKLE HALL	EASTON	PA	18042	NORTHAMPTON	USA	Biomedical Research and Research Training	000	1	5/23/2014	NEW	$268,220
														Subtotal = $268,220

Grand Total All Awards = $1,659,558

Top

All Categories

About

Search

Reports

Data Submission

Award Information

J-Protein Regulation of Yeast Prion Propagation

Award Number: R15GM110606

ORGANIZATION: NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES

OPDIV: NIH

AWARD CLASS: DISCRETIONARY

AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)

PERIOD OF PERFORMANCE START DATE: 07/01/2014

PERIOD OF PERFORMANCE END DATE: 08/31/2028

Federal Websites

Department of Health & Human Services

HHS Operating Divisions

HHS Staff Divisions

Download A Document Viewer