Arabidopsis SH3P2 is an ubiquitin-binding protein that functions together with ESCRT-I and the deubiquitylating enzyme AMSH3

Nagel, Marie-Kristin; Kalinowska, Kamila; Vogel, Karin; Reynolds, Gregory D.; Wu, Zhixiang; Anzenberger, Franziska; Ichikawa, Mie; Tsutsumi, Chie; Sato, Masa H; Isono, Erika

Arabidopsis SH3P2 is an ubiquitin-binding protein that functions together with ESCRT-I and the deubiquitylating enzyme AMSH3

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Datum

2017

Autor:innen

Nagel, Marie-Kristin

Kalinowska, Kamila

Vogel, Karin

Reynolds, Gregory D.

Wu, Zhixiang

Anzenberger, Franziska

Ichikawa, Mie

Tsutsumi, Chie

Sato, Masa H

Isono, Erika

et al.

DOI (zitierfähiger Link)

https://doi.org/10.1073/pnas.1710866114

Sammlungen

Biologie

Publikationstyp

Zeitschriftenartikel

Publikationsstatus

Published

Erschienen in

Proceedings of the National Academy of Sciences of the United States of America (PNAS). 2017, 114(34), pp. E7197-E7204. ISSN 0027-8424. eISSN 1091-6490. Available under: doi: 10.1073/pnas.1710866114

Zusammenfassung

Clathrin-mediated endocytosis of plasma membrane proteins is an essential regulatory process that controls plasma membrane protein abundance and is therefore important for many signaling pathways, such as hormone signaling and biotic and abiotic stress responses. On endosomal sorting, plasma membrane proteins maybe recycled or targeted for vacuolar degradation, which is dependent on ubiquitin modification of the cargos and is driven by the endosomal sorting complexes required for transport (ESCRTs). Components of the ESCRT machinery are highly conserved among eukaryotes, but homologs of ESCRT-0 that are responsible for recognition and concentration of ubiquitylated proteins are absent in plants. Recently several ubiquitin-binding proteins have been identified that serve in place of ESCRT-0; however, their function in ubiquitin recognition and endosomal trafficking is not well understood yet. In this study, we identified Src homology-3 (SH3) domain-containing protein 2 (SH3P2) as a ubiquitin- and ESCRT-I-binding protein that functions in intracellular trafficking. SH3P2 colocalized with clathrin light chain-labeled punctate structures and interacted with clathrin heavy chain in planta, indicating a role for SH3P2 in clathrin-mediated endocytosis. Furthermore, SH3P2 cofractionates with clathrin-coated vesicles (CCVs), suggesting that it associates with CCVs in planta Mutants of SH3P2 and VPS23 genetically interact, suggesting that they could function in the same pathway. Based on these results, we suggest a role of SH3P2 as an ubiquitin-binding protein that binds and transfers ubiquitylated proteins to the ESCRT machinery.

Fachgebiet (DDC)

570 Biowissenschaften, Biologie

Schlagwörter

ubiquitin, ESCRT, DUB, clathrin, Arabidopsis

Zitieren

ISO 690

NAGEL, Marie-Kristin, Kamila KALINOWSKA, Karin VOGEL, Gregory D. REYNOLDS, Zhixiang WU, Franziska ANZENBERGER, Mie ICHIKAWA, Chie TSUTSUMI, Masa H SATO, Erika ISONO, 2017. Arabidopsis SH3P2 is an ubiquitin-binding protein that functions together with ESCRT-I and the deubiquitylating enzyme AMSH3. In: Proceedings of the National Academy of Sciences of the United States of America (PNAS). 2017, 114(34), pp. E7197-E7204. ISSN 0027-8424. eISSN 1091-6490. Available under: doi: 10.1073/pnas.1710866114

BibTex

@article{Nagel2017-08-22Arabi-39856,
  year={2017},
  doi={10.1073/pnas.1710866114},
  title={Arabidopsis SH3P2 is an ubiquitin-binding protein that functions together with ESCRT-I and the deubiquitylating enzyme AMSH3},
  number={34},
  volume={114},
  issn={0027-8424},
  journal={Proceedings of the National Academy of Sciences of the United States of America (PNAS)},
  pages={E7197--E7204},
  author={Nagel, Marie-Kristin and Kalinowska, Kamila and Vogel, Karin and Reynolds, Gregory D. and Wu, Zhixiang and Anzenberger, Franziska and Ichikawa, Mie and Tsutsumi, Chie and Sato, Masa H and Isono, Erika}
}

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