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PreprintCC BY-NCbioRxiv

Understanding How Actomyosin Dynamics Drive Apical Constriction by Systematically Tagging and Mapping Actin-Binding Proteins

11 affiliations
  1. 1Biology Department, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
  2. 2Curriculum in Cell Biology and Physiology, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
  3. 3Present address: School of Life Sciences, Peking University, Beijing, China
  4. 4Present address: Biology Department, University of Wisconsin-La Crosse, La Crosse, WI, USA
  5. 5Advanced Bioimaging Center, Molecular and Cell Biology Department, University of California Berkeley, Berkeley, CA, USA
  6. 6Department of Biology, Stanford University, Stanford CA, USA
  7. 7Present address: Department of Zoology, The University of British Columbia, Vancouver, BC, Canada
  8. 8Department of Biology, University of Virginia, Charlottesville, VA, USA
  9. 9Department of Cell Biology, University of Virginia School of Medicine, Charlottesville, VA, USA
  10. 10Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
  11. 11Lead contact

Abstract

Apical constriction shapes tissues in fundamental events including gastrulation and neural tube formation. Diverse actin regulators play key roles in shaping cells, but the spatial distribution of most actin regulators in apical constriction is unknown. Here, we describe a systematic approach revealing the endogenous localization of 49 actin regulators in C. elegans gastrulation -- nearly every actin-binding protein (ABP) expressed in the early embryo -- and we use this atlas to test mechanistic hypotheses. We found that many actin regulators localized basolaterally, dependent on the Arp2/3 complex; that linear actin assembly factors enriched apically; and that apically constricting cells had an extra requirement for membrane-cortical linkers present in all cells. These findings answer some key questions about how ABPs function in apical constriction, and they establish a rich resource for investigating actin organization throughout early C. elegans development and a systematic in vivo protein localization reference for the actin cytoskeleton community.

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BibTeX
@misc{zhang2026understanding,
  title = {{Understanding How Actomyosin Dynamics Drive Apical Constriction by Systematically Tagging and Mapping Actin-Binding Proteins}},
  author = {Pu Zhang and Bailey N. de Jesus and Taylor N. Medwig-Kinney and David Q. Matus and Callista Yee and Theresa Gibney and Ariel Pani and Bob Goldstein},
  howpublished = {bioRxiv},
  year = {2026},
  month = oct,
  doi = {10.64898/2026.10.23.761371},
  url = {https://www.biorxiv.org/content/10.64898/2026.10.23.761371v1},
  note = {CC BY-NC},
}
RIS
TY  - UNPB
TI  - Understanding How Actomyosin Dynamics Drive Apical Constriction by Systematically Tagging and Mapping Actin-Binding Proteins
AU  - Pu Zhang
AU  - Bailey N. de Jesus
AU  - Taylor N. Medwig-Kinney
AU  - David Q. Matus
AU  - Callista Yee
AU  - Theresa Gibney
AU  - Ariel Pani
AU  - Bob Goldstein
PY  - 2026
DA  - 2026/10/23
PB  - bioRxiv
DO  - 10.64898/2026.10.23.761371
UR  - https://www.biorxiv.org/content/10.64898/2026.10.23.761371v1
AB  - Apical constriction shapes tissues in fundamental events including gastrulation and neural tube formation. Diverse actin regulators play key roles in shaping cells, but the spatial distribution of most actin regulators in apical constriction is unknown. Here, we describe a systematic approach revealing the endogenous localization of 49 actin regulators in C. elegans gastrulation -- nearly every actin-binding protein (ABP) expressed in the early embryo -- and we use this atlas to test mechanistic hypotheses. We found that many actin regulators localized basolaterally, dependent on the Arp2/3 complex; that linear actin assembly factors enriched apically; and that apically constricting cells had an extra requirement for membrane-cortical linkers present in all cells. These findings answer some key questions about how ABPs function in apical constriction, and they establish a rich resource for investigating actin organization throughout early C. elegans development and a systematic in vivo protein localization reference for the actin cytoskeleton community.
SN  - 2692-8205
ER  -