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Decoding the functions of nuclear speckle in protein quality control

Award Number: R35GM157978
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: 06/01/2025
PERIOD OF PERFORMANCE END DATE: 04/30/2030

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Decoding the functions of nuclear speckle in protein quality control - Maintaining proper protein folding, trafficking, and turnover—collectively known as proteostasis—is crucial for cellular health. Disruptions in proteostasis, such as the accumulation of misfolded proteins, are implicated in various pathological conditions, including aging and neurodegeneration. To maintain proteome integrity, organisms employ a spectrum of protein quality control mechanisms, encompassing the ubiquitin-proteasome system (UPS), the ER-Golgi protein secretory pathways, ribosome quality control, and the autophagy-lysosomal pathway (ALP). While significant strides have been made in understanding these mechanisms individually, elucidating how they are coordinated across diverse cellular compartments both spatially and temporally remains a formidable challenge. Unraveling the mechanisms governing this spatiotemporal coordination is paramount. Identifying a central regulatory hub overseeing all protein quality control processes will not only deepen our understanding of proteostasis regulation but also unveil potential therapeutic targets. Targeting such a hub could simultaneously engage multiple quality control mechanisms, offering a more effective approach to addressing proteinopathies and aging-related diseases. We recently unveiled an unexpected role for nuclear speckles— membrane-less organelles traditionally viewed as facilitating mRNA processing and gene regulation, in proteostasis control. Contrary to their previous characterization as simple housekeeping condensates, nuclear speckles emerge as pivotal sensors of proteostatic stress, orchestrating rapid stress responses by temporally coordinating the global transcriptional activation of proteostasis genes. Over the next five years, our research aims to develop innovative tools to dissect how nuclear speckles detect proteostatic stress and regulate temporal proteostasis dynamics. Ultimately, we aspire to leverage this knowledge to devise novel therapeutic strategies for proteinopathies and aging-related diseases, with the goal of alleviating their burdens on human health.


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 = $437,250 )
2026	2026	UNIVERSITY OF PITTSBURGH - OF THE COMMONWEALTH SYSTEM OF HIGHER EDUCATION	4200 FIFTH AVENUE	PITTSBURGH	PA	15260	ALLEGHENY	USA	Biomedical Research and Research Training	000	2	5/12/2026	NON-COMPETING CONTINUATION	$437,250
														Subtotal = $437,250

Issue Date FY: 2025 ( Subtotal = $452,250 )
2025	2025	UNIVERSITY OF PITTSBURGH - OF THE COMMONWEALTH SYSTEM OF HIGHER EDUCATION	4200 FIFTH AVENUE	PITTSBURGH	PA	15260	ALLEGHENY	USA	Biomedical Research and Research Training	000	1	5/22/2025	NEW	$452,250
														Subtotal = $452,250

Grand Total All Awards = $889,500

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Decoding the functions of nuclear speckle in protein quality control

Award Number: R35GM157978

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: 06/01/2025

PERIOD OF PERFORMANCE END DATE: 04/30/2030

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