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

Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins

Tyler S. Harmon, View ORCID ProfileAlex S. Holehouse, View ORCID ProfileMichael K. Rosen, View ORCID ProfileRohit V. Pappu
doi: https://doi.org/10.1101/164301
Tyler S. Harmon
1Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Alex S. Holehouse
1Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Alex S. Holehouse
Michael K. Rosen
2Department of Biophysics and Howard Hughes Medical Institute, 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
  • ORCID record for Michael K. Rosen
Rohit V. Pappu
1Department of Biomedical Engineering and Center for Biological Systems Engineering, Washington University in St. Louis, St. Louis, MO 63130, USA
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Rohit V. Pappu
  • Abstract
  • Full Text
  • Info/History
  • Metrics
  • Preview PDF
Loading

Abstract

Many intracellular membraneless bodies appear to form via reversible phase transitions of multivalent proteins. Two relevant types of phase transitions are sol-gel transitions (gelation) and phase separation plus gelation. Gelation refers to the formation of a system spanning molecular network. This can either be enabled by phase separation or it can occur independently. Despite relevance for the formation and selectivity of compositionally distinct protein and RNA assemblies, the determinants of gelation as opposed to phase separation plus gelation remain unclear. Here, we focus on linear multivalent proteins that consist of interaction domains that are connected by disordered linkers. Using results from computer simulations and theoretical analysis we show that the lengths and sequence-specific features of disordered linkers determine the coupling between phase separation and gelation. Thus, the precise nature of phase transitions for linear multivalent proteins should be biologically tunable through genetic encoding of or post-translational modifications to linker sequences.

Footnotes

  • ↵* E-mail: pappu{at}wustl.edu

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
Back to top
PreviousNext
Posted July 16, 2017.
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.
Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins
(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
Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins
Tyler S. Harmon, Alex S. Holehouse, Michael K. Rosen, Rohit V. Pappu
bioRxiv 164301; doi: https://doi.org/10.1101/164301
Reddit logo Twitter logo Facebook logo LinkedIn logo Mendeley logo
Citation Tools
Intrinsically disordered linkers determine the interplay between phase separation and gelation in multivalent proteins
Tyler S. Harmon, Alex S. Holehouse, Michael K. Rosen, Rohit V. Pappu
bioRxiv 164301; doi: https://doi.org/10.1101/164301

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 (4397)
  • Biochemistry (9624)
  • Bioengineering (7119)
  • Bioinformatics (24935)
  • Biophysics (12664)
  • Cancer Biology (9989)
  • Cell Biology (14395)
  • Clinical Trials (138)
  • Developmental Biology (7986)
  • Ecology (12145)
  • Epidemiology (2067)
  • Evolutionary Biology (16022)
  • Genetics (10948)
  • Genomics (14777)
  • Immunology (9899)
  • Microbiology (23732)
  • Molecular Biology (9502)
  • Neuroscience (51041)
  • Paleontology (370)
  • Pathology (1544)
  • Pharmacology and Toxicology (2692)
  • Physiology (4037)
  • Plant Biology (8692)
  • Scientific Communication and Education (1512)
  • Synthetic Biology (2404)
  • Systems Biology (6455)
  • Zoology (1349)