Literature DB >> 21442383

The Arabidopsis ESCRT protein-protein interaction network.

Mojgan Shahriari1, Klaus Richter, Channa Keshavaiah, Aneta Sabovljevic, Martin Huelskamp, Swen Schellmann.   

Abstract

In yeast, endosomal sorting of monoubiquitylated transmembrane proteins is performed by a subset of the 19 "class E vacuolar protein sorting" proteins. The core machinery consists of 11 proteins that are organised in three complexes termed ESCRT I-III (endosomal sorting complex required for transport I-III) and is conserved in eukaryotic cells. While the pathway is well understood in yeast and animals, the plant ESCRT system is largely unexplored. At least one sequence homolog for each ESCRT component can be found in the Arabidopsis genome. Generally, sequence conservation between yeast/animals and the Arabidopsis proteins is low. To understand details about participating proteins and complex organization we have performed a systematic pairwise yeast two hybrid analysis of all Arabidopsis proteins showing homology to the ESCRT core machinery. Positive interactions were validated using bimolecular fluorescence complementation. In our experiments, most putative ESCRT components exhibited interactions with other ESCRT components that could be shown to occur on endosomes suggesting that despite their low homology to their yeast and animal counterparts they represent functional components of the plant ESCRT pathway.

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Year:  2011        PMID: 21442383     DOI: 10.1007/s11103-011-9770-4

Source DB:  PubMed          Journal:  Plant Mol Biol        ISSN: 0167-4412            Impact factor:   4.076


  62 in total

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8.  A novel genetic system to detect protein-protein interactions.

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  20 in total

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Review 5.  Systems analysis of plant functional, transcriptional, physical interaction, and metabolic networks.

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7.  VPS36-Dependent Multivesicular Bodies Are Critical for Plasmamembrane Protein Turnover and Vacuolar Biogenesis.

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