The Arabidopsis adaptor protein AP-3µ interacts with the G-protein β subunit AGB1 and is involved in abscisic acid regulation of germination and post-germination development

Kansup, Jeeraporn; Tsugama, Daisuke; Liu, Shenkui; Takano, Tetsuo

doi:10.1093/jxb/ert327

Cited by 22 publications

(13 citation statements)

References 53 publications

(72 reference statements)

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“…Thus, ABCG25 is a member of a growing family of proteins whose activity is regulated via endocytosis in plants. In line with this finding, the involvement of clathrin in ABA-mediated processes was reported previously; plants with mutations in clathrin heavy chain display an ABA-hyposensitive phenotype in postgerminative growth (Kansup et al, 2013). However, it should be noted that mutations in the genes encoding subunits of AP-2 and clathrin coat proteins cause pleiotropic phenotypes due to defects in endocytosis of many cargo proteins (Kitakura et al, 2011;Di Rubbo et al, 2013;Kim et al, 2013;Yamaoka et al, 2013).…”

Section: Discussion Sgfp:abcg25 Is Internalized From the Pm Via Endocsupporting

confidence: 81%

Spatial Regulation of ABCG25, an ABA Exporter, Is an Important Component of the Mechanism Controlling Cellular ABA Levels

Park

Kim

et al. 2016

Plant Cell

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The phytohormone abscisic acid (ABA) plays crucial roles in various physiological processes, including responses to abiotic stresses, in plants. Recently, multiple ABA transporters were identified. The loss-of-function and gain-of-function mutants of these transporters show altered ABA sensitivity and stomata regulation, highlighting the importance of ABA transporters in ABA-mediated processes. However, how the activity of these transporters is regulated remains elusive. Here, we show that spatial regulation of ATP BINDING CASETTE G25 (ABCG25), an ABA exporter, is an important mechanism controlling its activity. ABCG25, as a soluble green fluorescent protein (sGFP) fusion, was subject to posttranslational regulation via clathrin-dependent and adaptor protein complex-2-dependent endocytosis followed by trafficking to the vacuole. The levels of sGFP:ABCG25 at the plasma membrane (PM) were regulated by abiotic stresses and exogenously applied ABA; PM-localized sGFP:ABCG25 decreased under abiotic stress conditions via activation of endocytosis in an ABA-independent manner, but increased upon application of exogenous ABA via activation of recycling from early endosomes in an ABA-dependent manner. Based on these findings, we propose that the spatial regulation of ABCG25 is an important component of the mechanism by which plants fine-tune cellular ABA levels according to cellular and environmental conditions.

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Section: Discussion Sgfp:abcg25 Is Internalized From the Pm Via Endocsupporting

confidence: 81%

Spatial Regulation of ABCG25, an ABA Exporter, Is an Important Component of the Mechanism Controlling Cellular ABA Levels

Park

Kim

et al. 2016

Plant Cell

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“…To date, Y2/3H screening has been the primary method used to identify AGB1 interactors 125 (Mudgil et al, 2009;Kobayashi et al, 2012;Tsugama et al, 2012;Kansup et al, 2013;126 Tsugama et al, 2013;Kansup et al, 2014;Xu et al, 2015). In order to identify AGB1-associated 127 proteins in planta, we performed co-IP from transgenic Arabidopsis expressing 35S driven 128 FLAG-tagged AGB1 in the agb1-2 background, or from wild-type plants as a negative control.…”

Section: Identification Of Agb1-associated Proteins By Co-ip and Massmentioning

confidence: 99%

The G Protein β-Subunit, AGB1, Interacts with FERONIA in RALF1-Regulated Stomatal Movement

Chakravorty

Assmann

2018

Plant Physiol.

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“…To determine whether the tonoplast association of PAT10 was compromised in the mutants of other AP-3 subunits, we introduced PAT10-GFP into pat2-2 (a null mutant of AP-3b; , ap-3m-2 (a mutant of AP-3m; Kansup et al, 2013), and ap-3s (a mutant of AP-3s; Supplemental Fig. S4).…”

Section: Targeting Of Pat10 To the Tonoplast Is Independent Of Rab5-mmentioning

confidence: 99%

Adaptor Protein-3-Dependent Vacuolar Trafficking Involves a Subpopulation of COPII and HOPS Tethering Proteins

Feng

Song

et al. 2017

Plant Physiol.

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ORCID IDs: 0000-0001-6345-6855 (J.-G.W.); 0000-0002-3501-5857 (Y.Z.).Plant vacuoles are versatile organelles critical for plant growth and responses to environment. Vacuolar proteins are transported from the endoplasmic reticulum via multiple routes in plants. Two classic routes bear great similarity to other phyla with major regulators known, such as COPII and Rab5 GTPases. By contrast, vacuolar trafficking mediated by adaptor protein-3 (AP-3) or that independent of the Golgi has few recognized cargos and none of the regulators. In search of novel regulators for vacuolar trafficking routes and by using a fluorescence-based forward genetic screen, we demonstrated that the multispan transmembrane protein, Arabidopsis (Arabidopsis thaliana) PROTEIN S-ACYL TRANSFERASE10 (PAT10), is an AP-3-mediated vacuolar cargo. We show that the tonoplast targeting of PAT10 is mediated by the AP-3 complex but independent of the Rab5-mediated post-Golgi trafficking route. We also report that AP-3-mediated vacuolar trafficking involves a subpopulation of COPII and requires the vacuolar tethering complex HOPS. In addition, we have identified two novel mutant alleles of AP-3d, whose point mutations interfered with the formation of the AP-3 complex as well as its membrane targeting. The results presented here shed new light on the vacuolar trafficking route mediated by AP-3 in plant cells.

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The Arabidopsis adaptor protein AP-3µ interacts with the G-protein β subunit AGB1 and is involved in abscisic acid regulation of germination and post-germination development

Cited by 22 publications

References 53 publications

Spatial Regulation of ABCG25, an ABA Exporter, Is an Important Component of the Mechanism Controlling Cellular ABA Levels

Spatial Regulation of ABCG25, an ABA Exporter, Is an Important Component of the Mechanism Controlling Cellular ABA Levels

The G Protein β-Subunit, AGB1, Interacts with FERONIA in RALF1-Regulated Stomatal Movement

Adaptor Protein-3-Dependent Vacuolar Trafficking Involves a Subpopulation of COPII and HOPS Tethering Proteins

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