Christopher L. Schwebach

ORCID: 0000-0002-5595-8641
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About
Contact & Profiles
Research Areas
  • Cellular Mechanics and Interactions
  • Connective tissue disorders research
  • Protease and Inhibitor Mechanisms
  • Cell Adhesion Molecules Research
  • Bone health and treatments
  • Protist diversity and phylogeny
  • Skin and Cellular Biology Research
  • Bone Metabolism and Diseases
  • Ubiquitin and proteasome pathways
  • Microtubule and mitosis dynamics

The Ohio State University
2017-2022

Abstract Mutations in actin-bundling protein plastin 3 (PLS3) emerged as a cause of congenital osteoporosis, but neither the role PLS3 bone development nor mechanisms underlying PLS3-dependent osteoporosis are understood. Of over 20 identified osteoporosis-linked mutations, we investigated all five that expected to produce full-length protein. One mutations distorted an actin-binding loop second domain and abolished F-actin bundling revealed by cryo-EM reconstruction interaction assays....

10.1038/s41413-020-0095-2 article EN cc-by Bone Research 2020-05-22

ABSTRACT Plastins/fimbrins are conserved actin-bundling proteins contributing to motility, cytokinesis, and other cellular processes by organizing actin assemblies of strikingly different geometries as in aligned bundles branched networks. We propose that this unique ability stems from an allosteric communication between plastins’ two actin-binding domains (ABD1/2) engaged a tight spatial association. found although ABD1 binds first, ABD2 can bind three orders magnitude stronger if not...

10.1101/2021.12.01.470822 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2021-12-01
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