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A SUMO-dependent feedback loop senses and controls the biogenesis of nuclear pore subunits

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A SUMO-dependent feedback loop senses and controls the biogenesis of nuclear pore subunits. / Rouvière, Jérôme O.; Bulfoni, Manuel; Tuck, Alex; Cosson, Bertrand; Devaux, Frédéric; Palancade, Benoit.

I: Nature Communications, Bind 9, 1665, 25.04.2018.

Publikation: Bidrag til tidsskrift/Konferencebidrag i tidsskrift /Bidrag til avisTidsskriftartikelForskningpeer review

Harvard

Rouvière, JO, Bulfoni, M, Tuck, A, Cosson, B, Devaux, F & Palancade, B 2018, 'A SUMO-dependent feedback loop senses and controls the biogenesis of nuclear pore subunits', Nature Communications, bind 9, 1665. https://doi.org/10.1038/s41467-018-03673-3

APA

Rouvière, J. O., Bulfoni, M., Tuck, A., Cosson, B., Devaux, F., & Palancade, B. (2018). A SUMO-dependent feedback loop senses and controls the biogenesis of nuclear pore subunits. Nature Communications, 9, [1665]. https://doi.org/10.1038/s41467-018-03673-3

CBE

MLA

Vancouver

Rouvière JO, Bulfoni M, Tuck A, Cosson B, Devaux F, Palancade B. A SUMO-dependent feedback loop senses and controls the biogenesis of nuclear pore subunits. Nature Communications. 2018 apr 25;9. 1665. https://doi.org/10.1038/s41467-018-03673-3

Author

Rouvière, Jérôme O. ; Bulfoni, Manuel ; Tuck, Alex ; Cosson, Bertrand ; Devaux, Frédéric ; Palancade, Benoit. / A SUMO-dependent feedback loop senses and controls the biogenesis of nuclear pore subunits. I: Nature Communications. 2018 ; Bind 9.

Bibtex

@article{1bd5c2a3aa7a4bc8aad4bdbdbb5cec0c,
title = "A SUMO-dependent feedback loop senses and controls the biogenesis of nuclear pore subunits",
abstract = "While the activity of multiprotein complexes is crucial for cellular metabolism, little is known about the mechanisms that collectively control the expression of their components. Here, we investigate the regulations targeting the biogenesis of the nuclear pore complex (NPC), the macromolecular assembly mediating nucleocytoplasmic exchanges. Systematic analysis of RNA-binding proteins interactomes, together with in vivo and in vitro assays, reveal that a subset of NPC mRNAs are specifically bound by Hek2, a yeast hnRNP K-like protein. Hek2-dependent translational repression and protein turnover are further shown to finely tune the levels of NPC subunits. Strikingly, mutations or physiological perturbations altering pore integrity decrease the levels of the NPC-associated SUMO protease Ulp1, and trigger the accumulation of sumoylated versions of Hek2 unable to bind NPC mRNAs. Our results support the existence of a quality control mechanism involving Ulp1 as a sensor of NPC integrity and Hek2 as a repressor of NPC biogenesis.",
author = "Rouvi{\`e}re, {J{\'e}r{\^o}me O.} and Manuel Bulfoni and Alex Tuck and Bertrand Cosson and Fr{\'e}d{\'e}ric Devaux and Benoit Palancade",
year = "2018",
month = "4",
day = "25",
doi = "10.1038/s41467-018-03673-3",
language = "English",
volume = "9",
journal = "Nature Communications",
issn = "2041-1723",
publisher = "Nature Publishing Group",

}

RIS

TY - JOUR

T1 - A SUMO-dependent feedback loop senses and controls the biogenesis of nuclear pore subunits

AU - Rouvière, Jérôme O.

AU - Bulfoni, Manuel

AU - Tuck, Alex

AU - Cosson, Bertrand

AU - Devaux, Frédéric

AU - Palancade, Benoit

PY - 2018/4/25

Y1 - 2018/4/25

N2 - While the activity of multiprotein complexes is crucial for cellular metabolism, little is known about the mechanisms that collectively control the expression of their components. Here, we investigate the regulations targeting the biogenesis of the nuclear pore complex (NPC), the macromolecular assembly mediating nucleocytoplasmic exchanges. Systematic analysis of RNA-binding proteins interactomes, together with in vivo and in vitro assays, reveal that a subset of NPC mRNAs are specifically bound by Hek2, a yeast hnRNP K-like protein. Hek2-dependent translational repression and protein turnover are further shown to finely tune the levels of NPC subunits. Strikingly, mutations or physiological perturbations altering pore integrity decrease the levels of the NPC-associated SUMO protease Ulp1, and trigger the accumulation of sumoylated versions of Hek2 unable to bind NPC mRNAs. Our results support the existence of a quality control mechanism involving Ulp1 as a sensor of NPC integrity and Hek2 as a repressor of NPC biogenesis.

AB - While the activity of multiprotein complexes is crucial for cellular metabolism, little is known about the mechanisms that collectively control the expression of their components. Here, we investigate the regulations targeting the biogenesis of the nuclear pore complex (NPC), the macromolecular assembly mediating nucleocytoplasmic exchanges. Systematic analysis of RNA-binding proteins interactomes, together with in vivo and in vitro assays, reveal that a subset of NPC mRNAs are specifically bound by Hek2, a yeast hnRNP K-like protein. Hek2-dependent translational repression and protein turnover are further shown to finely tune the levels of NPC subunits. Strikingly, mutations or physiological perturbations altering pore integrity decrease the levels of the NPC-associated SUMO protease Ulp1, and trigger the accumulation of sumoylated versions of Hek2 unable to bind NPC mRNAs. Our results support the existence of a quality control mechanism involving Ulp1 as a sensor of NPC integrity and Hek2 as a repressor of NPC biogenesis.

UR - http://www.scopus.com/inward/record.url?scp=85046124446&partnerID=8YFLogxK

U2 - 10.1038/s41467-018-03673-3

DO - 10.1038/s41467-018-03673-3

M3 - Journal article

C2 - 29695777

AN - SCOPUS:85046124446

VL - 9

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 1665

ER -