Myosin-I's motor and actin assembly activation activities are modular and separable in budding yeast

Jennifer M Hill1, Ross Ta Pedersen1, David G Drubin1

  • 1Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, United States.

PubMed

Insights

Myosin-I proteins, Myo3 and Myo5, are crucial for budding yeast endocytosis. Their motor and nucleation-promoting factor activities must link to membrane binding for effective actin assembly and force generation.

Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Clathrin-mediated endocytosis (CME) is a vital cellular process.
  • Myosin-Is, including Myo3 and Myo5 in budding yeast, play roles in CME.
  • These proteins possess motor activity, membrane binding, and Arp2/3 activation capabilities.

Purpose of the Study:

  • To investigate the functional requirements of Myo5's motor and nucleation-promoting factor (NPF) activities during CME.
  • To determine if these activities must be integrated or can function independently.

Main Methods:

  • Utilizing budding yeast as a model organism.
  • Investigating the roles of Myo5's motor and NPF activities.
  • Assessing the necessity of membrane binding for these functions.

Main Results:

  • Myo5's force-generating motor activity requires coupling to membrane binding for CME.
  • Myo5's NPF activity also necessitates membrane binding for successful CME.
  • These motor and NPF activities are modular and separable, functioning independently.

Conclusions:

  • Myosin-I's essential functions in actin network assembly and force generation during budding yeast CME are achieved through independently acting motor and NPF activities.
  • Membrane binding is a critical prerequisite for both Myo5's motor and NPF functions in CME.

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