Molecular Mechanisms of Myosin-3

Information

  • Research Project
  • 10280676
  • ApplicationId
    10280676
  • Core Project Number
    R01GM143414
  • Full Project Number
    1R01GM143414-01
  • Serial Number
    143414
  • FOA Number
    PA-20-185
  • Sub Project Id
  • Project Start Date
    9/10/2021 - 3 years ago
  • Project End Date
    8/31/2026 - a year from now
  • Program Officer Name
    AINSZTEIN, ALEXANDRA M
  • Budget Start Date
    9/10/2021 - 3 years ago
  • Budget End Date
    8/31/2022 - 2 years ago
  • Fiscal Year
    2021
  • Support Year
    01
  • Suffix
  • Award Notice Date
    9/14/2021 - 3 years ago
Organizations

Molecular Mechanisms of Myosin-3

PROJECT SUMMARY/ABSTRACT Our goal is to determine the molecular mechanisms of myosin-3 motors, unique kinase-myosin hybrids in the myosin superfamily, that are involved in fundamental cellular processes including cargo transport and the organization of the actin cytoskeleton in sensory cells. Despite their critical role in human biology, the molecular mechanisms of myosin-3 motors are not well understood. We propose that different modes of regulation together with different kinase substrates and binding partners determine the molecular mechanisms of myosin-3 motors. An integrated and innovative biochemical, biophysical, cell biological and high-resolution structural approach will be used to (i) determine the enzymatic profile and regulation, (ii) the unique structure (iii) and pathways that control myosin-3 function and regulation in vitro and in cells. Collectively, these studies will reveal novel mechanistic insights into the regulation of myosin-3 motors and have broad implications in the understanding of how different myosins are tuned to organize actin networks in cells.

IC Name
NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES
  • Activity
    R01
  • Administering IC
    GM
  • Application Type
    1
  • Direct Cost Amount
    215479
  • Indirect Cost Amount
    108506
  • Total Cost
    323985
  • Sub Project Total Cost
  • ARRA Funded
    False
  • CFDA Code
    859
  • Ed Inst. Type
    SCHOOLS OF MEDICINE
  • Funding ICs
    NIGMS:323985\
  • Funding Mechanism
    Non-SBIR/STTR RPGs
  • Study Section
    MSFC
  • Study Section Name
    Macromolecular Structure and Function C Study Section
  • Organization Name
    OHIO STATE UNIVERSITY
  • Organization Department
    PHYSIOLOGY
  • Organization DUNS
    832127323
  • Organization City
    COLUMBUS
  • Organization State
    OH
  • Organization Country
    UNITED STATES
  • Organization Zip Code
    432101016
  • Organization District
    UNITED STATES