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

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A YTHDF–PABP interaction is required for m6A-mediated organogenesis in plants. / Due Tankmar, Mathias; Reichel, Marlene; Arribas-Hernández, Laura; Brodersen, Peter.

In: EMBO Reports, Vol. 24, No. 12, e57741, 2023.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Due Tankmar, M, Reichel, M, Arribas-Hernández, L & Brodersen, P 2023, 'A YTHDF–PABP interaction is required for m6A-mediated organogenesis in plants', EMBO Reports, vol. 24, no. 12, e57741. https://doi.org/10.15252/embr.202357741

APA

Due Tankmar, M., Reichel, M., Arribas-Hernández, L., & Brodersen, P. (2023). A YTHDF–PABP interaction is required for m6A-mediated organogenesis in plants. EMBO Reports, 24(12), [e57741]. https://doi.org/10.15252/embr.202357741

Vancouver

Due Tankmar M, Reichel M, Arribas-Hernández L, Brodersen P. A YTHDF–PABP interaction is required for m6A-mediated organogenesis in plants. EMBO Reports. 2023;24(12). e57741. https://doi.org/10.15252/embr.202357741

Author

Due Tankmar, Mathias ; Reichel, Marlene ; Arribas-Hernández, Laura ; Brodersen, Peter. / A YTHDF–PABP interaction is required for m6A-mediated organogenesis in plants. In: EMBO Reports. 2023 ; Vol. 24, No. 12.

Bibtex

@article{4cc3e8fafaca43939afca45057aba26f,
title = "A YTHDF–PABP interaction is required for m6A-mediated organogenesis in plants",
abstract = "N6-methyladenosine (m6A) in mRNA is key to eukaryotic gene regulation. Many m6A functions involve RNA-binding proteins that recognize m6A 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.",
keywords = "Arabidopsis, ECT2, IDR, mA, PABP",
author = "{Due Tankmar}, Mathias and Marlene Reichel and Laura Arribas-Hern{\'a}ndez and Peter Brodersen",
note = "Publisher Copyright: {\textcopyright} 2023 The Authors. Published under the terms of the CC BY NC ND 4.0 license.",
year = "2023",
doi = "10.15252/embr.202357741",
language = "English",
volume = "24",
journal = "E M B O Reports",
issn = "1469-221X",
publisher = "Wiley-Blackwell",
number = "12",

}

RIS

TY - JOUR

T1 - A YTHDF–PABP interaction is required for m6A-mediated organogenesis in plants

AU - Due Tankmar, Mathias

AU - Reichel, Marlene

AU - Arribas-Hernández, Laura

AU - Brodersen, Peter

N1 - Publisher Copyright: © 2023 The Authors. Published under the terms of the CC BY NC ND 4.0 license.

PY - 2023

Y1 - 2023

N2 - N6-methyladenosine (m6A) in mRNA is key to eukaryotic gene regulation. Many m6A functions involve RNA-binding proteins that recognize m6A 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.

AB - N6-methyladenosine (m6A) in mRNA is key to eukaryotic gene regulation. Many m6A functions involve RNA-binding proteins that recognize m6A 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.

KW - Arabidopsis

KW - ECT2

KW - IDR

KW - mA

KW - PABP

U2 - 10.15252/embr.202357741

DO - 10.15252/embr.202357741

M3 - Journal article

C2 - 38009565

AN - SCOPUS:85177807449

VL - 24

JO - E M B O Reports

JF - E M B O Reports

SN - 1469-221X

IS - 12

M1 - e57741

ER -

ID: 375297042