Evidence map›Paper›PMID 41964388›Full record

ArticlePlant signaling & behavior2026

COP1 regulates the abundance and stability of the Arabidopsis retromer protein AtVPS29 via the proteasome pathway.

Wang Ki Min, Seung Ju Lee, Jong Tae Song, Hak Soo Seo

Abstract read
In one paragraph

Article in Plant signaling & behavior, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

4 authors.

Wang Ki MinDepartment of Agriculture, Forestry and Bioresources, Research Institute for Agriculture and Life Sciences, and Plant Genomics and Breeding Institute, Seoul National University, Seoul, Korea.ORCID 0000-0002-1666-0527
Seung Ju LeeDepartment of Agriculture, Forestry and Bioresources, Research Institute for Agriculture and Life Sciences, and Plant Genomics and Breeding Institute, Seoul National University, Seoul, Korea.ORCID 0009-0007-6393-4862
Jong Tae SongDepartment of Applied Biosciences, Kyungpook National University, Daegu, Korea.ORCID 0000-0002-2052-6582
Hak Soo SeoDepartment of Agriculture, Forestry and Bioresources, Research Institute for Agriculture and Life Sciences, and Plant Genomics and Breeding Institute, Seoul National University, Seoul, Korea.ORCID 0000-0002-0148-9931

Funding

Non-US Government Research Support type
6 · The paper itself

Abstract

Vacuolar protein sorting 29 (VPS29) is a pivotal component of the retromer complex, which plays a central role in endosomal trafficking. Numerous studies have investigated its functions in various eukaryotic systems; however, research in plants is still at an early stage. Moreover, the mechanisms controlling its abundance and stability remain largely unknown. In this study, we elucidated the role of constitutive photomorphogenic 1 (COP1) in regulating the abundance of Arabidopsis VPS29 (AtVPS29), a component of the trimeric retromer complex. Degradation of AtVPS29 is delayed by treatment with the proteasome inhibitor MG132, resulting in the accumulation of ubiquitinated AtVPS29 in MG132-treated plants. The AtVPS29 level is higher in

Indexed as

ArabidopsisArabidopsis ProteinsProteasome Endopeptidase ComplexUbiquitin-Protein LigasesVesicular Transport ProteinsGene Expression Regulation, PlantLeupeptinsMutationProtein StabilityUbiquitinationArabidopsis ProteinsAT2G32950 protein, Arabidopsisbenzyloxycarbonylleucyl-leucyl-leucine aldehydeLeupeptinsProteasome Endopeptidase ComplexUbiquitin-Protein LigasesVesicular Transport ProteinsAtVPS29COP1E3 ubiquitin ligaseretromerubiquitination

Identifiers

PMID41964388
PMCPMC13078200

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.