Figure - PMC

Skip to main content

An official website of the United States government

Here's how you know

Here's how you know

Official websites use .gov
A .gov website belongs to an official government organization in the United States.

Secure .gov websites use HTTPS
A lock ( ) or https:// means you've safely connected to the .gov website. Share sensitive information only on official, secure websites.

View full-text article in PMC

. 2020 Jun 30;219(8):e202004062. doi: 10.1083/jcb.202004062

Search in PMC
Search in PubMed
View in NLM Catalog
Add to search

© 2020 Noda et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).

PMC Copyright notice

Figure 1. — Phase separation and transition mediate the assembly of protein condensates with distinct material properties. (A) Multivalent interactions, mediated by proteins containing IDRs (top) or tandem modular interacting domains (bottom, represented by the red circles and blue crescents in two different proteins), drive the formation of phase-separated liquid condensates. Factors affecting interactions, including composition, chaperones, pH, temperature, and various PTMs, modulate LLPS. (B) Liquid-like phase-separated condensates (with highly dynamic constituents) can transition into more stable states, such as the gel-like state (with less mobile constituents) and the inert solid state.