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Mechanism Behind Nuclear-Specific Nicotinamide Adenine Dinucleotide (NAD+) Synthase, Nicotinamide Mononucleotide Adenylyl Transferase-1 (NMNAT1) in Retinal Photoreceptor Biogenesis and Health

Award Number: R01EY037294
ORGANIZATION: NATIONAL EYE INSTITUTE
OPDIV: NIH
AWARD CLASS: DISCRETIONARY
AWARD ACTIVITY TYPE: SCIENTIFIC/HEALTH RESEARCH (INCLUDES SURVEYS)
PERIOD OF PERFORMANCE START DATE: 09/01/2026
PERIOD OF PERFORMANCE END DATE: 05/31/2030

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Mechanism Behind Nuclear-Specific Nicotinamide Adenine Dinucleotide (NAD+) Synthase, Nicotinamide Mononucleotide Adenylyl Transferase-1 (NMNAT1) in Retinal Photoreceptor Biogenesis and Health - Project Summary The long-term goal of this proposal is to elucidate the precise role of nicotinamide mononucleotide adenylyltransferase-1 (NMNAT1) in the development and maintenance of retinal photoreceptor neurons. Mutations in NMNAT1 cause Leber congenital amaurosis (LCA), a severe early-onset blinding disorder. Although all three NMNAT isoforms (NMNAT1–3) contribute to subcellular NAD⁺ biosynthesis, essential for metabolism, cell survival, and genomic stability, NMNAT1 plays a uniquely critical role in retinal health. This project seeks to understand why NMNAT1 is indispensable for photoreceptor survival and why its loss leads to photoreceptor degeneration, even when SARM1, a key pro-degenerative NADase, is inhibited. We hypothesize that NMNAT1 regulates critical NAD⁺/NMN pools and possesses essential SARM1-independent, non-enzymatic functions required during early retinal development. Our first aim will determine whether elevated NMN is intrinsically toxic to photoreceptors, independent of SARM1, a mechanism that remains poorly understood and represents a major gap in the field. Next, we will investigate NMNAT1's non-enzymatic functions and its compartment-specific roles in maintaining NAD⁺ homeostasis. Together, these studies will guide the development of targeted gene therapies for LCA. The expected impact is to establish a new paradigm for NMNAT1 function in subcellular NAD⁺ regulation and its potential chaperone-like roles, revealing novel therapeutic strategies for restoring vision in NMNAT1- associated retinal diseases.


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 = $550,584 )
2026	2026	WEST VIRGINIA UNIVERSITY RESEARCH CORPORATION	886 CHESTNUT RIDGE ROAD	MORGANTOWN	WV	26505	MONONGALIA	USA	Vision Research	000	1	9/2/2026	NEW	$550,584
														Subtotal = $550,584

Grand Total All Awards = $550,584

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Mechanism Behind Nuclear-Specific Nicotinamide Adenine Dinucleotide (NAD+) Synthase, Nicotinamide Mononucleotide Adenylyl Transferase-1 (NMNAT1) in Retinal Photoreceptor Biogenesis and Health

Award Number: R01EY037294

ORGANIZATION: NATIONAL EYE INSTITUTE

OPDIV: NIH

AWARD CLASS: DISCRETIONARY

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

PERIOD OF PERFORMANCE START DATE: 09/01/2026

PERIOD OF PERFORMANCE END DATE: 05/31/2030

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