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Structure-function studies on Ion channels

Award Number: R35GM153212
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: 04/01/2024
PERIOD OF PERFORMANCE END DATE: 03/31/2029

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Structure-function studies on Ion channels - Project Summary: Our research program investigates the functional mechanisms that operate in voltage gated K+ (Kv) channels. Kv channels are essential for the generation and conduction of electrical signals by neurons, muscles and endocrine cells. Underlying the physiological roles of Kv channels is their ability to regulate the flux of K+ across cellular membranes. The flux of K+ through a Kv channel is controlled by the processes of voltage activation, which turns on the flux, and inactivation, which turns off the flux of K+ through the channel. There have been extensive investigations on Kv channels but major questions remain on the activation and inactivation mechanisms. In our research program, we use a multidisciplinary approach that combines structural and functional studies with protein modifications using unnatural amino acid (UAA) mutagenesis. UAA mutagenesis is a very powerful method for protein modification compared to traditional mutagenesis because it allows a large variety of side chain modifications and permits the modification of the protein backbone. In the grant period, we will investigate C-type inactivation in the Shaker, Kv1.2 and the cardiac Kv channel HERG. C-type inactivation refers to a conformational change at the selectivity filter, the ion binding region of the channel, that turns off the flux of ions through the channel. We will also investigate the role of the protein main chain interactions in voltage gating. Our studies on voltage gating will be carried out in the hyperpolarization activated and cyclic nucleotide gated ion (HCN) channel. The research proposed is significant because it will provide key mechanistic insights into the working of Kv channels. The research will also provide strategies for investigating the role of the protein backbone and ion binding sites, strategies that will be generally applicable to other ion channels.


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 = $429,000 )
2025	2025	OREGON HEALTH & SCIENCE UNIVERSITY	3181 SW SAM JACKSON PARK RD	PORTLAND	OR	97239	MULTNOMAH	USA	Biomedical Research and Research Training	001	2	4/4/2025	NON-COMPETING CONTINUATION	$429,000
2025	2024	OREGON HEALTH & SCIENCE UNIVERSITY	3181 SW SAM JACKSON PARK RD	PORTLAND	OR	97239	MULTNOMAH	USA	Biomedical Research and Research Training	000	1	11/21/2024	NEW	$0
														Subtotal = $429,000

Issue Date FY: 2024 ( Subtotal = $407,496 )
2024	2024	OREGON HEALTH & SCIENCE UNIVERSITY	3181 SW SAM JACKSON PARK RD	PORTLAND	OR	97239	MULTNOMAH	USA	Biomedical Research and Research Training	000	1	3/7/2024	NEW	$407,496
														Subtotal = $407,496

Grand Total All Awards = $836,496

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Structure-function studies on Ion channels

Award Number: R35GM153212

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: 04/01/2024

PERIOD OF PERFORMANCE END DATE: 03/31/2029

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