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![[Figure 9]](ag5054fig9mag.jpg)
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Figure 9
A cartoon summarizing the modulation of phase behaviour through dimer choice and possible mechanisms for disease-associated mutants in the C-terminal IDRs of DBHS proteins. (a) Self-interaction of the IDRs of SFPQ as a means to prevent unintended exaggerated phase separation and the possibility for dimer exchange disrupting interactions between IDRs or forming different ones and modulating LLPS. (b) Droplets made up of different types of dimers with potentially different material properties. (c) Possible mechanism for disease-associated cysteine mutants identified in the C-terminal IDRs of human DBHS proteins. Disulfide bonds could also form directly between IDRs with cysteines in them. |
![[Figure 9]](ag5054fig9.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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