4.7 Article

A YTHDF-PABP interaction is required for m6A-mediated organogenesis in plants

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EMBO REPORTS
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WILEY
DOI: 10.15252/embr.202357741

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Arabidopsis; ECT2; IDR; m(6)A; PABP

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This study reveals that the Arabidopsis YTH domain protein ECT2 promotes leaf formation through interaction with cytoplasmic poly(A)-binding proteins, providing insights into the molecular mechanism of leaf development.
N6-methyladenosine (m(6)A) in mRNA is key to eukaryotic gene regulation. Many m(6)A functions involve RNA-binding proteins that recognize m(6)A via a YT521-B Homology (YTH) domain. YTH domain proteins contain long intrinsically disordered regions (IDRs) that may mediate phase separation and interaction with protein partners, but whose precise biochemical functions remain largely unknown. The Arabidopsis thaliana YTH domain proteins ECT2, ECT3, and ECT4 accelerate organogenesis through stimulation of cell division in organ primordia. Here, we use ECT2 to reveal molecular underpinnings of this function. We show that stimulation of leaf formation requires the long N-terminal IDR, and we identify two short IDR elements required for ECT2-mediated organogenesis. Of these two, a 19-amino acid region containing a tyrosine-rich motif conserved in both plant and metazoan YTHDF proteins is necessary for binding to the major cytoplasmic poly(A)-binding proteins PAB2, PAB4, and PAB8. Remarkably, overexpression of PAB4 in leaf primordia partially rescues the delayed leaf formation in ect2 ect3 ect4 mutants, suggesting that the ECT2-PAB2/4/8 interaction on target mRNAs of organogenesis-related genes may overcome limiting PAB concentrations in primordial cells.

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