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Related Experiment Videos

Myosin is involved in postmitotic cell spreading

L P Cramer1, T J Mitchison

  • 1Department of Cellular and Molecular Pharmacology, University of California, San Francisco 94143-0450, USA.

The Journal of Cell Biology
|October 1, 1995
PubMed
Summary

Myosin plays a role in kidney cell spreading after division. Inhibiting myosin II reversibly stops cell spreading, suggesting its involvement in this crucial cellular process.

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Area of Science:

  • Cell Biology
  • Cytoskeleton Dynamics
  • Molecular Motor Function

Background:

  • Cell spreading is a fundamental process following cell division.
  • The role of myosin, particularly nonmuscle myosin II, in cell motility and adhesion is well-established.
  • Understanding the specific contribution of myosin to postmitotic cell spreading in epithelial cells remains incompletely defined.

Purpose of the Study:

  • To investigate the involvement of myosin in the postmitotic spreading of Potoroo tridactylis kidney (PtK2) cells.
  • To elucidate the spatial organization and polarity of actin filaments during cell spreading.
  • To determine the specific roles of different myosin isoforms in this process.

Main Methods:

  • Inhibitor studies using butanedione monoxime (BDM) to target myosin activity.
  • Time-lapse video microscopy to observe cell spreading dynamics.
  • Immunofluorescence and electron microscopy to analyze actin and myosin localization and organization.

Main Results:

  • Butanedione monoxime (BDM) reversibly inhibited PtK2 cell spreading, indicating myosin's role.
  • BDM affected nonmuscle myosin II and myosin V ATPase activity but not Listeria motility.
  • Actin filaments in spreading edges showed specific orientation, with myosin II localized to these edges but excluded from lamellipodia.

Conclusions:

  • Myosin, likely myosin II, is implicated in the process of postmitotic cell spreading in PtK2 cells.
  • Specific organization and polarity of actin filaments are crucial for directed cell spreading.
  • Myosin II's association with actin at cell edges, but not in retraction fibers or lamellipodia, suggests a regulatory role in spreading dynamics.

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