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An amphipathic helix enables septins to sense micrometer-scale membrane curvature.

Publication ,  Journal Article
Cannon, KS; Woods, BL; Crutchley, JM; Gladfelter, AS
Published in: J Cell Biol
April 1, 2019

Cell shape is well described by membrane curvature. Septins are filament-forming, GTP-binding proteins that assemble on positive, micrometer-scale curvatures. Here, we examine the molecular basis of curvature sensing by septins. We show that differences in affinity and the number of binding sites drive curvature-specific adsorption of septins. Moreover, we find septin assembly onto curved membranes is cooperative and show that geometry influences higher-order arrangement of septin filaments. Although septins must form polymers to stay associated with membranes, septin filaments do not have to span micrometers in length to sense curvature, as we find that single-septin complexes have curvature-dependent association rates. We trace this ability to an amphipathic helix (AH) located on the C-terminus of Cdc12. The AH domain is necessary and sufficient for curvature sensing both in vitro and in vivo. These data show that curvature sensing by septins operates at much smaller length scales than the micrometer curvatures being detected.

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Published In

J Cell Biol

DOI

EISSN

1540-8140

Publication Date

April 1, 2019

Volume

218

Issue

4

Start / End Page

1128 / 1137

Location

United States

Related Subject Headings

  • Structure-Activity Relationship
  • Signal Transduction
  • Septins
  • Protein Domains
  • Protein Conformation, alpha-Helical
  • Protein Binding
  • Kinetics
  • Fungal Proteins
  • Eremothecium
  • Developmental Biology
 

Citation

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Cannon, K. S., Woods, B. L., Crutchley, J. M., & Gladfelter, A. S. (2019). An amphipathic helix enables septins to sense micrometer-scale membrane curvature. J Cell Biol, 218(4), 1128–1137. https://doi.org/10.1083/jcb.201807211
Cannon, Kevin S., Benjamin L. Woods, John M. Crutchley, and Amy S. Gladfelter. “An amphipathic helix enables septins to sense micrometer-scale membrane curvature.J Cell Biol 218, no. 4 (April 1, 2019): 1128–37. https://doi.org/10.1083/jcb.201807211.
Cannon KS, Woods BL, Crutchley JM, Gladfelter AS. An amphipathic helix enables septins to sense micrometer-scale membrane curvature. J Cell Biol. 2019 Apr 1;218(4):1128–37.
Cannon, Kevin S., et al. “An amphipathic helix enables septins to sense micrometer-scale membrane curvature.J Cell Biol, vol. 218, no. 4, Apr. 2019, pp. 1128–37. Pubmed, doi:10.1083/jcb.201807211.
Cannon KS, Woods BL, Crutchley JM, Gladfelter AS. An amphipathic helix enables septins to sense micrometer-scale membrane curvature. J Cell Biol. 2019 Apr 1;218(4):1128–1137.

Published In

J Cell Biol

DOI

EISSN

1540-8140

Publication Date

April 1, 2019

Volume

218

Issue

4

Start / End Page

1128 / 1137

Location

United States

Related Subject Headings

  • Structure-Activity Relationship
  • Signal Transduction
  • Septins
  • Protein Domains
  • Protein Conformation, alpha-Helical
  • Protein Binding
  • Kinetics
  • Fungal Proteins
  • Eremothecium
  • Developmental Biology