Steric regulation of tandem calponin homology domain actin-binding affinity-Reference-Cited by-同舟云学术

Steric regulation of tandem calponin homology domain actin-binding affinity

Published:2019-12-15 Issue:26 Volume:30 Page:3112-3122
ISSN:1059-1524
Container-title:Molecular Biology of the Cell
language:en
Short-container-title:MBoC

Author:

Harris Andrew R.¹,Belardi Brian¹,Jreij Pamela¹,Wei Kathy¹,Shams Hengameh²,Bausch Andreas³,Fletcher Daniel A.¹⁴⁵

Affiliation:

1. Department of Bioengineering, University of California, Berkeley, Berkeley, CA 94720

2. Department of Mechanical Engineering, University of California, Berkeley, Berkeley, CA 94720

3. Lehrstuhl für Biophysik (E27), Technische Universität München, Garching 85748, Germany

4. Biological Systems and Engineering Division, Lawrence Berkeley National Laboratory, Berkeley, CA 94720

5. Chan Zuckerberg Biohub, San Francisco, CA 94158

Abstract

We show that the affinity of CH1–CH2 domains for F-actin can be both increased and decreased by diverse modifications that change the effective “openness” of CH1 and CH2, which sterically regulates binding to F-actin. We also show that subcellular localization depends on the N-terminal flanking region of CH1 but not on the overall affinity for F-actin.

Publisher

American Society for Cell Biology (ASCB)

Subject

Cell Biology,Molecular Biology

Reference46 articles.

1. Structural basis for high-affinity actin binding revealed by a β-III-spectrin SCA5 missense mutation

2. Interdomain Linker Determines Primarily the Structural Stability of Dystrophin and Utrophin Tandem Calponin-Homology Domains Rather than Their Actin-Binding Affinity

3. Structural comparisons of calponin homology domains: implications for actin binding

4. Comparative analysis of tools for live cell imaging of actin network architecture

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