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 Aug 11;78(4):1745–1763. doi: 10.1007/s00018-020-03610-y

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

© The Author(s) 2020

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/.

PMC Copyright notice

Fig. 6 — Schematic representation of the interplay between scaffold protein ITSN1 and RNA-binding protein SAM68. Due to the presence of RG repeats and KH domain that promote protein oligomerization and phase separation, SAM68 tends to form insoluble aggregates in vitro and SNBs in cells. Increasing the amount of mRNA favors the solubilization of SAM68, since RG repeats and KH domain are involved in mRNA binding. Stimulated by the interaction between SH3D and mRNA, ITSN1 promotes the solubilization of SAM68 through the interaction between ITSN1 SH3A and SAM68 P0