-6-methyladenosine (m6A) promotes the nuclear retention of mRNAs with intact 5' splice site motifs.

In humans, misprocessed mRNAs containing intact 5' Splice Site (5'SS) motifs are nuclear retained and targeted for decay by ZFC3H1, a component of the Poly(A) Exosome Targeting complex, and U1-70K, a component of the U1 snRNP. In , the ZFC3H1 homolog, Red1, binds to the YTH domain-containing protein Mmi1 and targets certain RNA transcripts to nuclear foci for nuclear retention and decay. Here we show that YTHDC1 and YTHDC2, two YTH domain-containing proteins that bind to -6-methyladenosine (m6A) modified RNAs, interact with ZFC3H1 and U1-70K, and are required for the nuclear retention of mRNAs with intact 5'SS motifs.

Ste2 and Ste3 receptors undergo peroxidase-induced heterodimerization when expressed heterologously in .

Ste2 and Ste3 are G-protein-coupled receptors (GPCRs) shown to play roles in hyphal chemotropism and fungal plant pathogenesis in response to activity arising from host-secreted peroxidases. Here, we follow up on the observation that chemotropism is dependent on both Ste2 and Ste3 being present; testing the possibility that this might be due to formation of an Ste2-Ste3 heterodimer. Bioluminescence resonance energy transfer (BRET) analyses were conducted in , where the addition of horse radish peroxidase (HRP) was found to increase the transfer of energy from the inducibly expressed Ste3-Nano luciferase donor, to the constitutively expressed Ste2-yellow fluorescent protein (YFP) acceptor, compared to controls.