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Functionalizing protein post-translational modifications using the phosphorylation integrated thermal shift assay

Award Number: R35GM165772
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: 07/08/2026
PERIOD OF PERFORMANCE END DATE: 02/28/2031

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Functionalizing protein post-translational modifications using the phosphorylation integrated thermal shift assay - PROJECT SUMMARY/ABSTRACT Protein post-translational modification is an essential biological process that regulates protein activity and function. Recent advances in instrumentation and sample preparation methods have enabled the detection and quantification of tens of thousands of phosphorylation events in a single experiment. While the resulting data has the potential to revolutionize our understanding of the biological functions of individual post-translational modification, the ability to identify these sites has far outpaced our understanding of how these modifications affect protein function and behavior. For example, only approximately 6% of phosphorylation sites in public databases have any functional annotation. As a result, lack of knowledge about the functional role of individual phosphorylation events has severely limited the utility of large-scale phosphoproteomics experiments. However, if we understood the functional role of individual phosphorylation sites, then our ability to predict function and phenotype from phosphoproteomics experiments would be greatly enhanced, with corresponding illumination of biological signaling and cellular function. To meet this need, we recently introduced the phosphorylation integrated thermal shift assay (PITSA) that identifies regulatory proteins and phosphorylation sites by measuring thermal shifts at proteome scale. This new PITSA methodology can identify both individual proteins and phosphorylation sites linked to cellular function. The resulting rich datasets provide a wealth of functional data that suggests previously unidentified hypotheses. Here, we propose to both utilize and expand this capability. We will adapt PITSA to include additional important post-translational modifications. We will enable the widespread adoption of PITSA by streamlining sample processing protocols, employing alternate data collection modalities, and developing data analysis tools. We will demonstrate the widespread utility of PITSA by analyzing additional model systems that include cancer and neurodevelopmental disorders. And finally, we will validate the functional role of important phosphorylation sites identified by PITSA using genetic, pharmacologic, and synthetic biology methods (including phospho-amino acid orthogonal translation systems). These efforts will expand our knowledge of the functional roles of protein phosphorylation and other post-translational modifications and enable increased adoption of this critical method in the larger scientific community.


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: 2026 ( Subtotal = $405,295 )
2026	2026	BRIGHAM YOUNG UNIVERSITY	A-153 ASB	PROVO	UT	84602	UTAH	USA	Biomedical Research and Research Training	000	1	7/8/2026	NEW	$405,295
														Subtotal = $405,295

Grand Total All Awards = $405,295

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Functionalizing protein post-translational modifications using the phosphorylation integrated thermal shift assay

Award Number: R35GM165772

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: 07/08/2026

PERIOD OF PERFORMANCE END DATE: 02/28/2031

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