An A/ENTH Domain-Containing Protein Functions as an Adaptor for Clathrin-Coated Vesicles on the Growing Cell Plate in Arabidopsis Root Cells

Song, Kyungyoung; Jang, Mihue; Kim, Soo Youn; Lee, Go-Eun; Lee, Gil Je; Kim, Dae Heon; Lee, Yong-Jik; Cho, Wonhwa; Hwang, Inhwan

doi:10.1104/pp.112.199380

Cited by 61 publications

(70 citation statements)

References 61 publications

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“…As none of the clathrin isoforms were retrieved in the TAP experiments, we tested whether AP-2 interacted with clathrin in vivo by performing coimmunoprecipitation experiments in Arabidopsis seedlings expressing CLC2-GFP (Konopka et al, 2008). Protein gel blot analysis with an antibody directed against the two AP2A proteins (Song et al, 2012) revealed that AP2A coimmunoprecipitated with CLC2-GFP ( Figure 2B). Additional BiFC experiments validated that AP2A1 and clathrin (CLC2 and CHC) interacted with a GFP signal localized at the PM, in agreement with the coimmunoprecipitation data ( Figure 2C; see Supplemental Table 2 and Supplemental Figure 2 online).…”

Section: Isolation Of the Arabidopsis Ap-2 Complexmentioning

confidence: 99%

The Clathrin Adaptor Complex AP-2 Mediates Endocytosis of BRASSINOSTEROID INSENSITIVE1 inArabidopsis

et al. 2013

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Clathrin-mediated endocytosis (CME) regulates many aspects of plant development, including hormone signaling and responses to environmental stresses. Despite the importance of this process, the machinery that regulates CME in plants is largely unknown. In mammals, the heterotetrameric ADAPTOR PROTEIN COMPLEX-2 (AP-2) is required for the formation of clathrin-coated vesicles at the plasma membrane (PM). Although the existence of AP-2 has been predicted in Arabidopsis thaliana, the biochemistry and functionality of the complex is still uncharacterized. Here, we identified all the subunits of the Arabidopsis AP-2 by tandem affinity purification and found that one of the large AP-2 subunits, AP2A1, localized at the PM and interacted with clathrin. Furthermore, endocytosis of the leucine-rich repeat receptor kinase, BRASSINOSTEROID INSENSITIVE1 (BRI1), was shown to depend on AP-2. Knockdown of the two Arabidopsis AP2A genes or overexpression of a dominant-negative version of the medium AP-2 subunit, AP2M, impaired BRI1 endocytosis and enhanced the brassinosteroid signaling. Our data reveal that the CME machinery in Arabidopsis is evolutionarily conserved and that AP-2 functions in receptormediated endocytosis.

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Section: Isolation Of the Arabidopsis Ap-2 Complexmentioning

confidence: 99%

The Clathrin Adaptor Complex AP-2 Mediates Endocytosis of BRASSINOSTEROID INSENSITIVE1 inArabidopsis

et al. 2013

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“…Plant genomes also encode many clathrin-associated sorting proteins (CLASPs) that aid adaptin-mediated formation of CCVs, including AP180/ epsin N-terminal homology (A/ENTH) domain proteins and dynamin-related proteins (DRPs) that facilitate membrane curvature and vesicle scission, respectively (Chen et al, 2011). Clathrin, A/ENTH domain proteins, DRPs, and the adaptin-related TPLATE have also been detected at the CP (Konopka and Bednarek, 2008a;Konopka et al, 2008;Fujimoto et al, 2010;Van Damme et al, 2011;Ito et al, 2012;Song et al, 2012), suggesting that a mechanism similar to CME and clathrin-mediated membrane retrieval at the TGN facilitates membrane recycling from the CP during plant cytokinesis.…”

Section: Introductionmentioning

confidence: 99%

Mediation of Clathrin-Dependent Trafficking during Cytokinesis and Cell Expansion by Arabidopsis STOMATAL CYTOKINESIS DEFECTIVE Proteins

et al. 2013

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STOMATAL CYTOKINESIS DEFECTIVE1 (SCD1) encodes a putative Rab guanine nucleotide exchange factor that functions in membrane trafficking and is required for cytokinesis and cell expansion in Arabidopsis thaliana. Here, we show that the loss of SCD2 function disrupts cytokinesis and cell expansion and impairs fertility, phenotypes similar to those observed for scd1 mutants. Genetic and biochemical analyses showed that SCD1 function is dependent upon SCD2 and that together these proteins are required for plasma membrane internalization. Further specifying the role of these proteins in membrane trafficking, SCD1 and SCD2 proteins were found to be associated with isolated clathrin-coated vesicles and to colocalize with clathrin light chain at putative sites of endocytosis at the plasma membrane. Together, these data suggest that SCD1 and SCD2 function in clathrin-mediated membrane transport, including plasma membrane endocytosis, required for cytokinesis and cell expansion.

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“…GFP-tagged ECA1 (AT2G01600), ECA2 (AT1G03050), and ECA4 (AT2G25430) (and ECA1-specific antibody signal) localize to the PM and the nascent cell plate and to some extent to punctate structures (Figure 3). In the case of ECA1, these punctae were further identified as EEs, mainly via colocalization with early endocytosed FM4-64 and colocalization also after treatment with Brefeldin A (BFA; Song et al, 2012). Analysis of spatiotemporal dynamics of ECA1 labeling at the nascent cell plate revealed a pattern that is suggestive of a role in endocytosis from the forming cell plate (reviewed in Jürgens, 2005).…”

Section: Anths: a Large Group Involved In Endocytosismentioning

confidence: 99%

“…For another three ANTH proteins, involvement in CCV formation at the cell plate has been postulated (Song et al, 2012). GFP-tagged ECA1 (AT2G01600), ECA2 (AT1G03050), and ECA4 (AT2G25430) (and ECA1-specific antibody signal) localize to the PM and the nascent cell plate and to some extent to punctate structures (Figure 3).…”

Section: Anths: a Large Group Involved In Endocytosismentioning

confidence: 99%

Helping Hands for Budding Prospects: ENTH/ANTH/VHS Accessory Proteins in Endocytosis, Vacuolar Transport, and Secretion

Zouhar

Sauer

2014

The Plant Cell

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Coated vesicles provide a major mechanism for the transport of proteins through the endomembrane system of plants. Transport between the endoplasmic reticulum and the Golgi involves vesicles with COPI and COPII coats, whereas clathrin is the predominant coat in endocytosis and post-Golgi trafficking. Sorting of cargo, coat assembly, budding, and fission are all complex and tightly regulated processes that involve many proteins. The mechanisms and responsible factors are largely conserved in eukaryotes, and increasing organismal complexity tends to be associated with a greater numbers of individual family members. Among the key factors is the class of ENTH/ANTH/VHS domain-containing proteins, which link membrane subdomains, clathrin, and other adapter proteins involved in early steps of clathrin coated vesicle formation. More than 30 Arabidopsis thaliana proteins contain this domain, but their generally low sequence conservation has made functional classification difficult. Reports from the last two years have greatly expanded our knowledge of these proteins and suggest that ENTH/ANTH/VHS domain proteins are involved in various instances of clathrin-related endomembrane trafficking in plants. This review aims to summarize these new findings and discuss the broader context of clathrin-dependent plant vesicular transport.

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An A/ENTH Domain-Containing Protein Functions as an Adaptor for Clathrin-Coated Vesicles on the Growing Cell Plate in Arabidopsis Root Cells

Cited by 61 publications

References 61 publications

The Clathrin Adaptor Complex AP-2 Mediates Endocytosis of BRASSINOSTEROID INSENSITIVE1 inArabidopsis

The Clathrin Adaptor Complex AP-2 Mediates Endocytosis of BRASSINOSTEROID INSENSITIVE1 inArabidopsis

Mediation of Clathrin-Dependent Trafficking during Cytokinesis and Cell Expansion by Arabidopsis STOMATAL CYTOKINESIS DEFECTIVE Proteins

Helping Hands for Budding Prospects: ENTH/ANTH/VHS Accessory Proteins in Endocytosis, Vacuolar Transport, and Secretion

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