2023
DOI: 10.1101/2023.02.09.527857
|View full text |Cite
Preprint
|
Sign up to set email alerts
|

Condensate formation of the human RNA-binding protein SMAUG1 is controlled by its intrinsically disordered regions and interactions with 14-3-3 proteins

Abstract: SMAUG1 is a human RNA-binding protein that is known to be dysregulated in a wide range of diseases. It is evolutionarily conserved and has been shown to form condensates containing translationally repressed RNAs. This indicates that condensation is central to proper SMAUG1 function; however, the factors governing condensation are largely unknown. In this work, we show that SMAUG1 drives the formation of liquid-like condensates in cells through its non-conventional C-terminal prion-like disordered region. We us… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
1

Citation Types

0
3
0

Year Published

2023
2023
2024
2024

Publication Types

Select...
2
1

Relationship

0
3

Authors

Journals

citations
Cited by 3 publications
(3 citation statements)
references
References 66 publications
(101 reference statements)
0
3
0
Order By: Relevance
“…Stoichiometric binding pocket interactions of 14-3-3ζ dimers with Tau monomers phosphorylated at S214 and S324 make Tau molecules unavailable for multivalent interactions needed for LLPS and, therefore, counteract their co-condensation. The suppression of biomolecular condensation by 14-3-3 binding has been suggested for other physiological and disease-associated 14-3-3 binding partners 49,50 , however, the molecular mechanisms behind this process previously remained uncertain.…”
Section: Resultsmentioning
confidence: 99%
“…Stoichiometric binding pocket interactions of 14-3-3ζ dimers with Tau monomers phosphorylated at S214 and S324 make Tau molecules unavailable for multivalent interactions needed for LLPS and, therefore, counteract their co-condensation. The suppression of biomolecular condensation by 14-3-3 binding has been suggested for other physiological and disease-associated 14-3-3 binding partners 49,50 , however, the molecular mechanisms behind this process previously remained uncertain.…”
Section: Resultsmentioning
confidence: 99%
“…Often the recognition of target proteins by F-box proteins, such as Slmb, depends on prior phosphorylation of the target ( 66 69 ). Mouse and human SAMD4A/Smaug1 were reported to interact with 14-3-3 proteins ( 18 , 70 ), a protein family known to recognize phosphorylated sequences within their protein partners ( 71 ). We detected the Drosophila Smaug interaction to 14-3-3ζ and 14-3-3ε in our ReLo assays ( SI Appendix , Fig.…”
Section: Discussionmentioning
confidence: 99%
“…Often the recognition of target proteins by F-box proteins, such as Slmb, depends on prior phosphorylation of the target (Morais-de-Sá et al , 2013; Mason & Laman, 2020; Frescas & Pagano, 2008; Jia et al , 2005). Mouse and human SAMD4A/Smaug1 were reported to interact with 14-3-3 proteins (Chen et al , 2014b; Fehilly et al , 2023), a protein family known to recognize phosphorylated sequences within their protein partners (Obsilova & Obsil, 2022). We detected the Drosophila Smaug interaction to 14-3-3ζ and 14-3-3ε in our ReLo assays ( Supplemental Figure 8C ), suggesting that Smaug is phosphorylated in these cells.…”
Section: Discussionmentioning
confidence: 99%