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

Phase separation of zonula occludens proteins drives formation of tight junctions

Oliver Beutel, Riccardo Maraspini, Karina Pombo-Garcia, Cécilie Martin-Lemaitre, Alf Honigmann
doi: https://doi.org/10.1101/589580
Oliver Beutel
1Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Riccardo Maraspini
1Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Karina Pombo-Garcia
1Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Cécilie Martin-Lemaitre
1Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Alf Honigmann
1Max Planck Institute of Molecular Cell Biology and Genetics, Dresden, Germany
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • For correspondence: honigmann@mpi-cbg.de
  • Abstract
  • Full Text
  • Info/History
  • Metrics
  • Preview PDF
Loading

Abstract

Tight junctions are cell adhesion complexes that seal tissues and are involved in cell polarity and signalling. Supra-molecular assembly and positioning of tight junctions as continuous networks of adhesion strands is dependent on the two membrane associated scaffolding proteins ZO1 and ZO2. To understand how ZO proteins organize junction assembly, we performed quantitative cell biology and in vitro reconstitution experiments. We discovered that ZO proteins self-organize membrane attached compartments via phase separation. We identified the multivalent interactions of the conserved PDZ-SH3-GuK supra-domain as the driver of phase separation. These interactions are regulated by phosphorylation and intra-molecular binding. Formation of condensed ZO protein compartments is sufficient to specifically enrich and localize tight junction proteins including adhesion receptors, cytoskeletal adapters and transcription factors. Our results suggest that an active phase transition of ZO proteins into a condensed membrane bound compartment drives claudin polymerization and coalescence of a continuous tight junction belt.

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 March 26, 2019.
Download PDF
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.
Phase separation of zonula occludens proteins drives formation of tight junctions
(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
Phase separation of zonula occludens proteins drives formation of tight junctions
Oliver Beutel, Riccardo Maraspini, Karina Pombo-Garcia, Cécilie Martin-Lemaitre, Alf Honigmann
bioRxiv 589580; doi: https://doi.org/10.1101/589580
Reddit logo Twitter logo Facebook logo LinkedIn logo Mendeley logo
Citation Tools
Phase separation of zonula occludens proteins drives formation of tight junctions
Oliver Beutel, Riccardo Maraspini, Karina Pombo-Garcia, Cécilie Martin-Lemaitre, Alf Honigmann
bioRxiv 589580; doi: https://doi.org/10.1101/589580

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 (4691)
  • Biochemistry (10381)
  • Bioengineering (7698)
  • Bioinformatics (26381)
  • Biophysics (13553)
  • Cancer Biology (10735)
  • Cell Biology (15465)
  • Clinical Trials (138)
  • Developmental Biology (8509)
  • Ecology (12844)
  • Epidemiology (2067)
  • Evolutionary Biology (16890)
  • Genetics (11417)
  • Genomics (15499)
  • Immunology (10643)
  • Microbiology (25261)
  • Molecular Biology (10242)
  • Neuroscience (54610)
  • Paleontology (402)
  • Pathology (1671)
  • Pharmacology and Toxicology (2900)
  • Physiology (4356)
  • Plant Biology (9265)
  • Scientific Communication and Education (1588)
  • Synthetic Biology (2562)
  • Systems Biology (6789)
  • Zoology (1472)