# Molecular function of Myosin-l

> **NIH NIH R37** · UNIVERSITY OF PENNSYLVANIA · 2020 · $496,074

## Abstract

   
DESCRIPTION (provided by applicant): Our goal is to determine the molecular mechanisms of the myosin-I family of molecular motors. Myosin-Is comprise the largest unconventional myosin family found in humans (eight genes), and its large size and expression profile distinguish it as one of the most diverse. Myosin-Is physically link cell membranes to the underlying actin cytoskeleton where they play essential roles in powering membrane dynamics, membrane trafficking, and mechanical signal- transduction. Myosin-I's show remarkable diversity in their cellular function, which is mediated by their diverse biophysical properties, which includes dynamic tension sensing, membrane- attachment, and unique regulatory modes. Our goal is to provide the biochemical and biophysical foundation for understanding the molecular physiology of this important class of motors. We will use a combination of innovative biophysical techniques to define (1) the structural origin of myosin-I force sensing, (2) the role f myosin-I adaptor proteins in controlling myosin-I activity, and (3) control of myosin-I function by
actin regulatory proteins.

## Key facts

- **NIH application ID:** 9827988
- **Project number:** 5R37GM057247-22
- **Recipient organization:** UNIVERSITY OF PENNSYLVANIA
- **Principal Investigator:** E. Michael Ostap
- **Activity code:** R37 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2020
- **Award amount:** $496,074
- **Award type:** 5
- **Project period:** 1998-08-01 → 2020-11-30

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/9827988

## Citation

> US National Institutes of Health, RePORTER application 9827988, Molecular function of Myosin-l (5R37GM057247-22). Retrieved via AI Analytics 2026-05-25 from https://api.ai-analytics.org/grant/nih/9827988. Licensed CC0.

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