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The Arabidopsis deubiquitinating enzyme AMSH<sub>3</sub> interacts with ESCRT-III subunits and regulates their localization.

The Arabidopsis deubiquitinating enzyme AMSH3 interacts with ESCRT-III subunits and regulates their localization.

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KATSIARIMPA, Anthi, Franziska ANZENBERGER, Nicole SCHLAGER, Susanne NEUBERT, Marie-Theres HAUSER, Claus SCHWECHHEIMER, Erika ISONO, 2012. The Arabidopsis deubiquitinating enzyme AMSH3 interacts with ESCRT-III subunits and regulates their localization.. In: The Plant Cell. 23(8), pp. 3026-3040. ISSN 1040-4651. eISSN 1532-298X. Available under: doi: 10.1105/tpc.111.087254

@article{Katsiarimpa2012-08-24Arabi-38604, title={The Arabidopsis deubiquitinating enzyme AMSH3 interacts with ESCRT-III subunits and regulates their localization.}, year={2012}, doi={10.1105/tpc.111.087254}, number={8}, volume={23}, issn={1040-4651}, journal={The Plant Cell}, pages={3026--3040}, author={Katsiarimpa, Anthi and Anzenberger, Franziska and Schlager, Nicole and Neubert, Susanne and Hauser, Marie-Theres and Schwechheimer, Claus and Isono, Erika} }

Hauser, Marie-Theres Katsiarimpa, Anthi Schlager, Nicole Hauser, Marie-Theres Schwechheimer, Claus Isono, Erika The Arabidopsis deubiquitinating enzyme AMSH<sub>3</sub> interacts with ESCRT-III subunits and regulates their localization. eng Schlager, Nicole Katsiarimpa, Anthi Ubiquitination and deubiquitination regulate various cellular processes. We have recently shown that the deubiquitinating enzyme Associated Molecule with the SH3 domain of STAM3 (AMSH3) is involved in vacuole biogenesis and intracellular trafficking in Arabidopsis thaliana. However, little is known about the identity of its interaction partners and deubiquitination substrates. Here, we provide evidence that AMSH3 interacts with ESCRT-III subunits VPS2.1 and VPS24.1. The interaction of ESCRT-III subunits with AMSH3 is mediated by the MIM1 domain and depends on the MIT domain of AMSH3. We further show that AMSH3, VPS2.1, and VPS24.1 localize to class E compartments when ESCRT-III disassembly is inhibited by coexpression of inactive Suppressor of K+ transport Defect 1 (SKD1), an AAA-ATPase involved in the disassembly of ESCRT-III. We also provide evidence that AMSH3 and SKD1 compete for binding to VPS2.1. Furthermore, we show that the loss of AMSH3 enzymatic activity leads to the formation of cellular compartments that contain AMSH3, VPS2.1, and VPS24.1. Taken together, our study presents evidence that AMSH3 interacts with classical core ESCRT-III components and thereby provides a molecular framework for the function of AMSH3 in plants. 2012-08-24 2017-04-25T09:25:38Z Anzenberger, Franziska Neubert, Susanne Neubert, Susanne 2017-04-25T09:25:38Z Anzenberger, Franziska Schwechheimer, Claus Isono, Erika

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