Article

Villin-type headpiece domains show a wide range of F-actin-binding affinities

  1. D. Vardar1,
  2. A. H. Chishti2,
  3. B. S. Frank1,
  4. E. J. Luna3,
  5. A. A. Noegel4,
  6. S. W. Oh3,
  7. M. Schleicher5,
  8. C. J. McKnight1,*

Article first published online: 18 APR 2002

DOI: 10.1002/cm.10027

Issue

Cell Motility and the Cytoskeleton

Cell Motility and the Cytoskeleton

Volume 52, Issue 1, pages 9–21, May 2002

Additional Information

How to Cite

Vardar, D., Chishti, A. H., Frank, B. S., Luna, E. J., Noegel, A. A., Oh, S. W., Schleicher, M. and McKnight, C. J. (2002), Villin-type headpiece domains show a wide range of F-actin-binding affinities. Cell Motil. Cytoskeleton, 52: 9–21. doi: 10.1002/cm.10027

Author Information

  1. 1

    Department of Physiology and Biophysics, Boston University School of Medicine, Boston, Massachusetts

  2. 2

    Section of Hematology and Oncology Research, St. Elizabeth's Medical Center, Boston, Massachusetts

  3. 3

    Department of Cell Biology, University of Massachusetts Medical Center, Worcester, Massachusetts

  4. 4

    Institut für Biochemie I, Medizinische Einrichtungen der Universität zu Köln, Köln, Germany

  5. 5

    Adolf-Butenandt-Institut, Zellbiologie, München, Germany

*Department of Physiology and Biophysics, Boston University School of Medicine, 700 Albany St. Boston, MA 02118

Publication History

  1. Issue published online: 18 APR 2002
  2. Article first published online: 18 APR 2002
  3. Manuscript Accepted: 27 DEC 2001
  4. Manuscript Received: 30 OCT 2001

Funded by

  • Department of Biophysics at Boston University School of Medicine
  • NIH. Grant Numbers: GM62886, HL07291, HL-51445, GM33048
  • Deutsche Forschungsgemeinschaft

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Keywords:

  • villin headpiece;
  • dematin;
  • villidin;
  • supervillin;
  • actin-binding;
  • surface potential

Abstract

The villin-type “headpiece” domain is a modular motif found at the extreme C-terminus of larger “core” domains in over 25 cytoskeletal proteins in plants and animals. Although headpiece is classified as an F-actin-binding domain, it has been suggested that some expressed fusion-proteins containing headpiece may lack F-actin-binding in vivo. To determine the intrinsic F-actin affinity of headpiece domains, we quantified the F-actin affinity of seven headpiece domains and three N-terminal truncations, under identical in vitro conditions. The constructs are folded and adopt the native headpiece structure. However, they show a wide range of affinities that can be grouped into high, low, and nonspecific-binding categories. Computer models of the structure and charged surface potential of these headpiece domains suggest features important for high F-actin affinity. We conclude that not all headpiece domains are intrinsically F-actin-binding motifs, and suggest that the surface charge distribution may be an important element for F-actin recognition. Cell Motil. Cytoskeleton 52:9–21, 2002. © 2002 Wiley-Liss, Inc.

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