ErbB-3 BINDING PROTEIN 1 Regulates Translation and Counteracts RETINOBLASTOMA RELATED to Maintain the Root Meristem. / Lokdarshi, Ansul ; Papdi, Csaba; Pettkó-Szandtner, Aladár ; Dorokhov, Stefan ; Scheres, Ben; Magyar, Zoltan ; von Arnim, Albrecht G. ; Bogre, Laszlo; Horvath, Beatrix.

In: Plant physiology, Vol. 182, No. 2, 31.01.2020, p. 919-932.

Research output: Contribution to journalArticlepeer-review

E-pub ahead of print

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ErbB-3 BINDING PROTEIN 1 Regulates Translation and Counteracts RETINOBLASTOMA RELATED to Maintain the Root Meristem. / Lokdarshi, Ansul ; Papdi, Csaba; Pettkó-Szandtner, Aladár ; Dorokhov, Stefan ; Scheres, Ben; Magyar, Zoltan ; von Arnim, Albrecht G. ; Bogre, Laszlo; Horvath, Beatrix.

In: Plant physiology, Vol. 182, No. 2, 31.01.2020, p. 919-932.

Research output: Contribution to journalArticlepeer-review

Harvard

Lokdarshi, A, Papdi, C, Pettkó-Szandtner, A, Dorokhov, S, Scheres, B, Magyar, Z, von Arnim, AG, Bogre, L & Horvath, B 2020, 'ErbB-3 BINDING PROTEIN 1 Regulates Translation and Counteracts RETINOBLASTOMA RELATED to Maintain the Root Meristem', Plant physiology, vol. 182, no. 2, pp. 919-932. https://doi.org/10.1104/pp.19.00805

APA

Lokdarshi, A., Papdi, C., Pettkó-Szandtner, A., Dorokhov, S., Scheres, B., Magyar, Z., von Arnim, A. G., Bogre, L., & Horvath, B. (2020). ErbB-3 BINDING PROTEIN 1 Regulates Translation and Counteracts RETINOBLASTOMA RELATED to Maintain the Root Meristem. Plant physiology, 182(2), 919-932. https://doi.org/10.1104/pp.19.00805

Vancouver

Lokdarshi A, Papdi C, Pettkó-Szandtner A, Dorokhov S, Scheres B, Magyar Z et al. ErbB-3 BINDING PROTEIN 1 Regulates Translation and Counteracts RETINOBLASTOMA RELATED to Maintain the Root Meristem. Plant physiology. 2020 Jan 31;182(2):919-932. https://doi.org/10.1104/pp.19.00805

Author

Lokdarshi, Ansul ; Papdi, Csaba ; Pettkó-Szandtner, Aladár ; Dorokhov, Stefan ; Scheres, Ben ; Magyar, Zoltan ; von Arnim, Albrecht G. ; Bogre, Laszlo ; Horvath, Beatrix. / ErbB-3 BINDING PROTEIN 1 Regulates Translation and Counteracts RETINOBLASTOMA RELATED to Maintain the Root Meristem. In: Plant physiology. 2020 ; Vol. 182, No. 2. pp. 919-932.

BibTeX

@article{a37bbd5856854681b294e2edea1a5525,
title = "ErbB-3 BINDING PROTEIN 1 Regulates Translation and Counteracts RETINOBLASTOMA RELATED to Maintain the Root Meristem",
abstract = "The ErbB-3 BINDING PROTEIN 1 (EBP1) drives growth, however, the mechanism of how it acts in plants is little understood. We show that EBP1 expression and protein abundance are predominantly confined to meristematic cells, induced by sucrose and partly dependent on TARGET OF RAPAMYCIN (TOR) kinase activity. Consistent with being downstream to TOR, silencing of EBP1 restrains, while overexpression promotes root growth mostly under sucrose-limiting conditions. RETINOBLASTOMA RELATED (RBR) is a sugar-dependent transcriptional repressor of cell proliferation. Inducible RBR overexpression depletes meristematic activity and causes precocious differentiation, which is attenuated by EBP1. To understand the molecular mechanism, we searched for EBP1- and RBR-interacting proteins by affinity purification and mass spectrometry. In line with the dsRNA-binding activity of EBP1 in human cells, the overwhelming majority of EBP1 interactors are part of ribonucleoprotein complexes regulating many aspects of protein synthesis, including ribosome biogenesis and mRNA translation. We confirmed that EBP1 associates with ribosomes and that EBP1 silencing hinders the rRNA processing. Unexpectedly, we revealed that RBR also interacts with a set of EBP1-associated nucleolar proteins as well as factors that function in protein translation. This suggests that EBP1 and RBR act antagonistically on common processes that determine the capacity for translation to tune meristematic activity in relation to available resources.",
keywords = "Erb3 binding protein, RETINOBLASTOMA-RELATED PROTEIN, TOR, protein translation control, Growth and Development, CELL CYCLE",
author = "Ansul Lokdarshi and Csaba Papdi and Alad{\'a}r Pettk{\'o}-Szandtner and Stefan Dorokhov and Ben Scheres and Zoltan Magyar and {von Arnim}, {Albrecht G.} and Laszlo Bogre and Beatrix Horvath",
year = "2020",
month = jan,
day = "31",
doi = "10.1104/pp.19.00805",
language = "English",
volume = "182",
pages = "919--932",
journal = "Plant physiology",
issn = "0032-0889",
publisher = "American Society of Plant Biologists",
number = "2",

}

RIS

TY - JOUR

T1 - ErbB-3 BINDING PROTEIN 1 Regulates Translation and Counteracts RETINOBLASTOMA RELATED to Maintain the Root Meristem

AU - Lokdarshi, Ansul

AU - Papdi, Csaba

AU - Pettkó-Szandtner, Aladár

AU - Dorokhov, Stefan

AU - Scheres, Ben

AU - Magyar, Zoltan

AU - von Arnim, Albrecht G.

AU - Bogre, Laszlo

AU - Horvath, Beatrix

PY - 2020/1/31

Y1 - 2020/1/31

N2 - The ErbB-3 BINDING PROTEIN 1 (EBP1) drives growth, however, the mechanism of how it acts in plants is little understood. We show that EBP1 expression and protein abundance are predominantly confined to meristematic cells, induced by sucrose and partly dependent on TARGET OF RAPAMYCIN (TOR) kinase activity. Consistent with being downstream to TOR, silencing of EBP1 restrains, while overexpression promotes root growth mostly under sucrose-limiting conditions. RETINOBLASTOMA RELATED (RBR) is a sugar-dependent transcriptional repressor of cell proliferation. Inducible RBR overexpression depletes meristematic activity and causes precocious differentiation, which is attenuated by EBP1. To understand the molecular mechanism, we searched for EBP1- and RBR-interacting proteins by affinity purification and mass spectrometry. In line with the dsRNA-binding activity of EBP1 in human cells, the overwhelming majority of EBP1 interactors are part of ribonucleoprotein complexes regulating many aspects of protein synthesis, including ribosome biogenesis and mRNA translation. We confirmed that EBP1 associates with ribosomes and that EBP1 silencing hinders the rRNA processing. Unexpectedly, we revealed that RBR also interacts with a set of EBP1-associated nucleolar proteins as well as factors that function in protein translation. This suggests that EBP1 and RBR act antagonistically on common processes that determine the capacity for translation to tune meristematic activity in relation to available resources.

AB - The ErbB-3 BINDING PROTEIN 1 (EBP1) drives growth, however, the mechanism of how it acts in plants is little understood. We show that EBP1 expression and protein abundance are predominantly confined to meristematic cells, induced by sucrose and partly dependent on TARGET OF RAPAMYCIN (TOR) kinase activity. Consistent with being downstream to TOR, silencing of EBP1 restrains, while overexpression promotes root growth mostly under sucrose-limiting conditions. RETINOBLASTOMA RELATED (RBR) is a sugar-dependent transcriptional repressor of cell proliferation. Inducible RBR overexpression depletes meristematic activity and causes precocious differentiation, which is attenuated by EBP1. To understand the molecular mechanism, we searched for EBP1- and RBR-interacting proteins by affinity purification and mass spectrometry. In line with the dsRNA-binding activity of EBP1 in human cells, the overwhelming majority of EBP1 interactors are part of ribonucleoprotein complexes regulating many aspects of protein synthesis, including ribosome biogenesis and mRNA translation. We confirmed that EBP1 associates with ribosomes and that EBP1 silencing hinders the rRNA processing. Unexpectedly, we revealed that RBR also interacts with a set of EBP1-associated nucleolar proteins as well as factors that function in protein translation. This suggests that EBP1 and RBR act antagonistically on common processes that determine the capacity for translation to tune meristematic activity in relation to available resources.

KW - Erb3 binding protein

KW - RETINOBLASTOMA-RELATED PROTEIN

KW - TOR

KW - protein translation control

KW - Growth and Development

KW - CELL CYCLE

U2 - 10.1104/pp.19.00805

DO - 10.1104/pp.19.00805

M3 - Article

VL - 182

SP - 919

EP - 932

JO - Plant physiology

JF - Plant physiology

SN - 0032-0889

IS - 2

ER -