Skip to main content
bioRxiv
  • Home
  • About
  • Submit
  • ALERTS / RSS
Advanced Search
New Results

Spectrin is a mechanoresponsive protein shaping the architecture of intercellular invasion

Rui Duan, Ji Hoon Kim, Khurts Shilagardi, Eric Schiffhauer, Sungmin Son, Donghoon Lee, Shuo Li, Graham Thomas, Tianzhi Luo, Daniel A. Fletcher, Douglas N. Robinson, Elizabeth H. Chen
doi: https://doi.org/10.1101/154831
Rui Duan
1Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Ji Hoon Kim
1Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Khurts Shilagardi
1Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Eric Schiffhauer
2Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Sungmin Son
3Department of Bioengineering, University of California, Berkeley, Berkeley, CA 94720, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Donghoon Lee
4Department of Molecular Biology, UT Southwestern Medical Center, Dallas, TX 75390, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Shuo Li
1Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Graham Thomas
5Departments of Biology and of Biochemistry and Molecular Biology, Penn State University, University Park, PA 16802
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Tianzhi Luo
6Department of Modern Mechanics, University of Science and Technology of China, Hefei, China
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Daniel A. Fletcher
3Department of Bioengineering, University of California, Berkeley, Berkeley, CA 94720, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Douglas N. Robinson
2Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Elizabeth H. Chen
1Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA
4Department of Molecular Biology, UT Southwestern Medical Center, Dallas, TX 75390, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • Abstract
  • Full Text
  • Info/History
  • Metrics
  • Supplementary material
  • Preview PDF
Loading

Abstract

Spectrin is a membrane skeletal protein best known for its structural role in maintaining cell shape and protecting cells from mechanical damage1-3. Here, we report that spectrin dynamically accumulates and dissolves at the fusogenic synapse, where an attacking fusion partner mechanically invades its receiving partner with actin-propelled protrusions to promote cell-cell fusion4-7. Using genetics, cell biology, biophysics and mathematical modeling, we demonstrate that unlike myosin II that responds to dilation deformation, spectrin exhibits a mechanosensitive accumulation in response to shear deformation, which is highly elevated at the fusogenic synapse. The accumulated spectrin forms an uneven network, which functions as a “sieve” to constrict the invasive fingerlike protrusions, thus putting the fusogenic synapse under high mechanical tension to promote cell membrane fusion. Taken together, our study has revealed a previously unrecognized function of spectrin as a dynamic mechanoresponsive protein that shapes the architecture of intercellular invasion. These findings have general implications for understanding spectrin function in other dynamic cellular processes beyond cell-cell fusion.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. All rights reserved. No reuse allowed without permission.
Back to top
PreviousNext
Posted June 23, 2017.
Download PDF

Supplementary Material

Email

Thank you for your interest in spreading the word about bioRxiv.

NOTE: Your email address is requested solely to identify you as the sender of this article.

Enter multiple addresses on separate lines or separate them with commas.
Spectrin is a mechanoresponsive protein shaping the architecture of intercellular invasion
(Your Name) has forwarded a page to you from bioRxiv
(Your Name) thought you would like to see this page from the bioRxiv website.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Share
Spectrin is a mechanoresponsive protein shaping the architecture of intercellular invasion
Rui Duan, Ji Hoon Kim, Khurts Shilagardi, Eric Schiffhauer, Sungmin Son, Donghoon Lee, Shuo Li, Graham Thomas, Tianzhi Luo, Daniel A. Fletcher, Douglas N. Robinson, Elizabeth H. Chen
bioRxiv 154831; doi: https://doi.org/10.1101/154831
Digg logo Reddit logo Twitter logo Facebook logo Google logo LinkedIn logo Mendeley logo
Citation Tools
Spectrin is a mechanoresponsive protein shaping the architecture of intercellular invasion
Rui Duan, Ji Hoon Kim, Khurts Shilagardi, Eric Schiffhauer, Sungmin Son, Donghoon Lee, Shuo Li, Graham Thomas, Tianzhi Luo, Daniel A. Fletcher, Douglas N. Robinson, Elizabeth H. Chen
bioRxiv 154831; doi: https://doi.org/10.1101/154831

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Subject Area

  • Cell Biology
Subject Areas
All Articles
  • Animal Behavior and Cognition (3600)
  • Biochemistry (7567)
  • Bioengineering (5519)
  • Bioinformatics (20781)
  • Biophysics (10325)
  • Cancer Biology (7977)
  • Cell Biology (11633)
  • Clinical Trials (138)
  • Developmental Biology (6602)
  • Ecology (10200)
  • Epidemiology (2065)
  • Evolutionary Biology (13608)
  • Genetics (9539)
  • Genomics (12844)
  • Immunology (7919)
  • Microbiology (19538)
  • Molecular Biology (7657)
  • Neuroscience (42070)
  • Paleontology (308)
  • Pathology (1257)
  • Pharmacology and Toxicology (2201)
  • Physiology (3267)
  • Plant Biology (7037)
  • Scientific Communication and Education (1294)
  • Synthetic Biology (1951)
  • Systems Biology (5426)
  • Zoology (1116)