Adaptor Protein Complex 2–Mediated Endocytosis Is Crucial for Male Reproductive Organ Development in <i>Arabidopsis</i>

Kim, Soo Youn; Xu, Zheng‐Yi; Song, Kyungyoung; Kim, Dae Heon; Kang, Hyangju; Reichardt, Ilka; Sohn, Eun Ju; Friml, Jiřı́; Juergens, G.; Hwang, Inhwan

doi:10.1105/tpc.113.114264

Cited by 108 publications

(117 citation statements)

References 67 publications

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“…Various mutants in AP-2 subunits show impaired CME and developmental aberrations that presumably are the consequence of these cellular defects. These results, plus the dynamic spatiotemporal localization of AP-2 components at the PM, support the notion that AP-2 is an early adaptor complex for clathrin recruitment/assembly (Di Rubbo et al, 2013;Fan et al, 2013;Kim et al, 2013;Yamaoka et al, 2013) in plant endocytosis.…”

Section: Anths: a Large Group Involved In Endocytosissupporting

confidence: 72%

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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Section: Anths: a Large Group Involved In Endocytosissupporting

confidence: 72%

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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“…This is consistent with our previous report that the AP-2 subunit AP2M is required for both RPM1-mediated ETI and RPS2-mediated ETI, but not for RPS4-mediated ETI (Hatsugai et al, 2016). AP2M plays a central role in clathrin-mediated endocytotic pathway from the plasma membrane to the vacuole (Di Rubbo et al, 2013;Fan et al, 2013;Kim et al, 2013;Yamaoka et al, 2013). These results suggest that the ETI-related immunesignaling components undergo endocytic internalization.…”

Section: A Possible Function Of Ap-4 Complex In Eti Signalingsupporting

confidence: 82%

Involvement of Adapter Protein Complex 4 in Hypersensitive Cell Death Induced by Avirulent Bacteria

et al. 2017

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Plant immunity to avirulent bacterial pathogens is associated with subcellular membrane dynamics including fusion between the vacuolar and plasma membranes, resulting in hypersensitive cell death. Here, we report that ADAPTOR PROTEIN COMPLEX-4 (AP-4) subunits are involved in plant immunity associated with hypersensitive cell death. We isolated a mutant with a defect in resistance to an avirulent strain of Pseudomonas syringae pv. tomato (Pto) DC3000 avrRpm1 from a vacuolar protein sorting mutant library of Arabidopsis (Arabidopsis thaliana). The mutant was identical to gfs4-1, which has a mutation in the gene encoding the AP-4 subunit AP4B. Thus, we focused on AP4B and another subunit, AP4E. All of the mutants (ap4b-3, ap4b-4, ap4e-1, and ap4e-2) were defective in hypersensitive cell death and resistance to Pto DC3000 with the type III effector AvrRpm1 or AvrRpt2, both of which are recognized on the plasma membrane, while they showed slightly enhanced susceptibility to the type-III-secretion-deficient P. syringae strain hrcC. On the other hand, both ap4b-3 and ap4b-4 showed no defect in resistance to Pto DC3000 with the type III effector AvrRps4, which is recognized in the cytosol and does not induce hypersensitive cell death. Upon infection with Pto DC3000 avrRpt2, the ap4b-3 and ap4b-4 leaf cells did not show fusion between vacuolar and plasma membranes, whereas the wild-type leaf cells did. These results suggest that AP-4 contributes to cell death-associated immunity, possibly via membrane fusion, after type III effector-recognition on the plasma membrane.

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“…In line with such a general role in endocytic sorting, genetic interference with clathrin function in plants results in severe developmental defects, including alterations in root elongation, root and hypocotyl gravitropism, and lateral root primordia initiation Wang et al, 2013). Arabidopsis clathrin chains associate with AP2 subunits and form punctate foci at the plasma membrane (Fan et al, 2013;Kim et al, 2013;Yamaoka et al, 2013). As such, and similar to clathrin mutants, plants impaired in AP2 subunits show alterations in general endocytosis and PIN internalization and/or polarity, as well as defects in the endocytosis of BRI1, which correlates with severe developmental defects (Di Rubbo et al, 2013;Fan et al, 2013;Kim et al, 2013;Yamaoka et al, 2013).…”

Section: Clathrin and Adaptor Proteins: Key Mediators Of Protein Endomentioning

confidence: 99%

“…Arabidopsis clathrin chains associate with AP2 subunits and form punctate foci at the plasma membrane (Fan et al, 2013;Kim et al, 2013;Yamaoka et al, 2013). As such, and similar to clathrin mutants, plants impaired in AP2 subunits show alterations in general endocytosis and PIN internalization and/or polarity, as well as defects in the endocytosis of BRI1, which correlates with severe developmental defects (Di Rubbo et al, 2013;Fan et al, 2013;Kim et al, 2013;Yamaoka et al, 2013). More recently, the activity of another, apparently plant-specific complex -the TPLATE adaptor complex -has been linked to early events in CME.…”

Section: Clathrin and Adaptor Proteins: Key Mediators Of Protein Endomentioning

confidence: 99%

The dynamics of plant plasma membrane proteins: PINs and beyond

2014

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Plants are permanently situated in a fixed location and thus are well adapted to sense and respond to environmental stimuli and developmental cues. At the cellular level, several of these responses require delicate adjustments that affect the activity and steady-state levels of plasma membrane proteins. These adjustments involve both vesicular transport to the plasma membrane and protein internalization via endocytic sorting. A substantial part of our current knowledge of plant plasma membrane protein sorting is based on studies of PIN-FORMED (PIN) auxin transport proteins, which are found at distinct plasma membrane domains and have been implicated in directional efflux of the plant hormone auxin. Here, we discuss the mechanisms involved in establishing such polar protein distributions, focusing on PINs and other key plant plasma membrane proteins, and we highlight the pathways that allow for dynamic adjustments in protein distribution and turnover, which together constitute a versatile framework that underlies the remarkable capabilities of plants to adjust growth and development in their ever-changing environment.

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Adaptor Protein Complex 2–Mediated Endocytosis Is Crucial for Male Reproductive Organ Development in Arabidopsis

Cited by 108 publications

References 67 publications

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

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

Involvement of Adapter Protein Complex 4 in Hypersensitive Cell Death Induced by Avirulent Bacteria

The dynamics of plant plasma membrane proteins: PINs and beyond

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