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m6A enhances the phase separation potential of mRNA
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m6A enhances the phase separation potential of mRNA
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Journal Article
m6A enhances the phase separation potential of mRNA
2019
Overview
N
6
-methyladenosine (m
6
A) is the most prevalent modified nucleotide in mRNA
1
,
2
, with around 25% of mRNAs containing at least one m
6
A. Methylation of mRNA to form m
6
A is required for diverse cellular and physiological processes
3
. Although the presence of m
6
A in an mRNA can affect its fate in different ways, it is unclear how m
6
A directs this process and why the effects of m
6
A can vary in different cellular contexts. Here we show that the cytosolic m
6
A-binding proteins—YTHDF1, YTHDF2 and YTHDF3—undergo liquid–liquid phase separation in vitro and in cells. This phase separation is markedly enhanced by mRNAs that contain multiple, but not single, m
6
A residues. Polymethylated mRNAs act as a multivalent scaffold for the binding of YTHDF proteins, juxtaposing their low-complexity domains and thereby leading to phase separation. The resulting mRNA–YTHDF complexes then partition into different endogenous phase-separated compartments, such as P-bodies, stress granules or neuronal RNA granules. m
6
A-mRNA is subject to compartment-specific regulation, including a reduction in the stability and translation of mRNA. These studies reveal that the number and distribution of m
6
A sites in cellular mRNAs can regulate and influence the composition of the phase-separated transcriptome, and suggest that the cellular properties of m
6
A-modified mRNAs are governed by liquid–liquid phase separation principles.
The cytosolic
N
6
-methyladenosine (m
6
A)-binding proteins YTHDF1, YTHDF2 and YTHDF3 undergo liquid–liquid phase separation in vitro and in cells; this is enhanced by polymethylated mRNAs to form complexes that partition into different cellular phase-separated compartments.
