Time-resolved studies of actin organization by multivalent ions and actin-binding proteins

ORAL

Abstract

Actin is one of the principal components in the eukaryotic cytoskeleton, the architecture of which is highly regulated for a wide range of biological functions. In the presence of multivalent salts or actin-binding proteins, it is known that F-actin can organize into bundles or networks. In this work, we use time-resolved confocal microscopy to study the dynamics of actin bundle growth induced by multivalent ions and by espin, a prototypical actin binding protein that is known to induce bundles. For divalent ion induced bundles, we observe a rapid lateral saturation followed by longitudinal growth of bundles, in sharp contrast to the bundling mechanism of espin, which favors finite length bundles.

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Authors

  • Ghee Hwee Lai

    • Dept. of Physics, Dept. of Materials Science \& Engineering, F. Seitz Materials Research Laboratory, University of Illinois, Urbana-Champaign
    • University of Illinois at Urbana-Champaign

  • Kirstin Purdy

    • University of Illinois at Urbana-Champaign

  • James R. Bartles

    • Northwestern University

  • Gerard C. L. Wong

    • University of Illinois, Department of Materials Science and Engineering, Department of Physics
    • Department of Materials Science and Engineering, Dept. of Physics, Dept. of Bioengineering, University of Illinois at Urbana-Champaign
    • Dept. of Physics, Dept. of Materials Science \& Engineering, F. Seitz Materials Research Laboratory, University of Illinois, Urbana-Champaign
    • University of Illinois at Urbana-Champaign