Clathrin-dependent Association of CVAK104 with Endosomes and the<i>Trans</i>-Golgi Network

Düwel, Michael; Ungewickell, Ernst

doi:10.1091/mbc.e06-05-0390

Cited by 35 publications

(50 citation statements)

References 56 publications

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“…It was reported that, in the presence of poly-L-Lys, SCYL2 was able to autophosphorylate and to phosphorylate the b2-adaptin subunit of AP2 (Conner and Schmid, 2005), indicating that SCYL2 has an ability to phosphorylate some proteins under certain circumstances. However, in another report, kinase activity was not detected in immunoprecipitated or bacterially expressed SCYL2/CVAK104 (Düwel and Ungewickell, 2006). We tried to express the several recombinant forms of Arabidopsis SCYL2B with 6xHis or GST tags in Escherichia coli to find out whether it had kinase activity but failed to express the protein, possibly due to the instability of the protein.…”

Section: Discussionmentioning

confidence: 99%

“…6B). In animals, a clathrincoated vesicle-associated kinase of 104 kD (CVAK104), an Arabidopsis SCYL2A/B ortholog, plays an important role in vesicle trafficking and is localized at the Golgi, TGN, and endosomes (Düwel and Ungewickell, 2006;Borner et al, 2007). To determine the subcellular localization of SCYL2B, colocalization studies were performed using several fluorescent protein markers for subcellular organelles such as the Golgi, TGN, PVC, PM, mitochondria, plastids, and peroxisomes.…”

Section: Scyl2b Is Localized At the Golgi Tgn And Pvcmentioning

confidence: 99%

“…In animals, SCYL2 acts as a component of CCVs and can interact with clathrin (Conner and Schmid, 2005;Düwel and Ungewickell, 2006). To determine whether Arabidopsis SCYL2 proteins also can bind to components of CCVs, we conducted a split YFP-based bimolecular fluorescence complementation (BiFC) assay.…”

Section: Scyl2b Interacts With Chc1 Vti11 and Vti12mentioning

confidence: 99%

“…It was shown that animal SCYL2 binds directly to both clathrin and Adaptor Protein-2 (AP2), which is an adaptor protein (Conner and Schmid, 2005;Düwel and Ungewickell, 2006). SCYL2 has been suggested to function as a kinase (Conner and Schmid, 2005) and is found at the Golgi, TGN, and endosomes in animal systems (Düwel and Ungewickell, 2006;Borner et al, 2007).…”

mentioning

confidence: 99%

“…Moreover, SCYL2 selectively induces the lysosomal degradation of Frizzled5, which is a PM receptor involved in the Wnt signaling pathway (Terabayashi et al, 2009). It also has been reported that lysosomal hydrolase cathepsin D is missorted in SCYL2-depleted cells (Düwel and Ungewickell, 2006) and that knockdown of SCYL2 in Xenopus tropicalis causes severe developmental defects (Borner et al, 2007). Recently, it was shown that SCYL2 is a key regulator of neuronal function and survival in mouse brain (Gingras et al, 2015;Pelletier, 2016).…”

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confidence: 99%

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SCYL2 Genes Are Involved in Clathrin-Mediated Vesicle Trafficking and Essential for Plant Growth

et al. 2017

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Protein transport between organelles is an essential process in all eukaryotic cells and is mediated by the regulation of processes such as vesicle formation, transport, docking, and fusion. In animals, SCY1-LIKE2 (SCYL2) binds to clathrin and has been shown to play roles in trans-Golgi network-mediated clathrin-coated vesicle trafficking. Here, we demonstrate that SCYL2A and SCYL2B, which are Arabidopsis (Arabidopsis thaliana) homologs of animal SCYL2, are vital for plant cell growth and root hair development. Studies of the SCYL2 isoforms using multiple single or double loss-of-function alleles show that SCYL2B is involved in root hair development and that SCYL2A and SCYL2B are essential for plant growth and development and act redundantly in those processes. Quantitative reverse transcription-polymerase chain reaction and a b-glucuronidase-aided promoter assay show that SCYL2A and SCYL2B are differentially expressed in various tissues. We also show that SCYL2 proteins localize to the Golgi, trans-Golgi network, and prevacuolar compartment and colocalize with Clathrin Heavy Chain1 (CHC1). Furthermore, bimolecular fluorescence complementation and coimmunoprecipitation data show that SCYL2B interacts with CHC1 and two Soluble NSF Attachment Protein Receptors (SNAREs): Vesicle Transport through t-SNARE Interaction11 (VTI11) and VTI12. Finally, we present evidence that the root hair tip localization of Cellulose Synthase-Like D3 is dependent on SCYL2B. These findings suggest the role of SCYL2 genes in plant cell developmental processes via clathrin-mediated vesicle membrane trafficking.

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Section: Discussionmentioning

confidence: 99%

Section: Scyl2b Is Localized At the Golgi Tgn And Pvcmentioning

confidence: 99%

Section: Scyl2b Interacts With Chc1 Vti11 and Vti12mentioning

confidence: 99%

mentioning

confidence: 99%

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SCYL2 Genes Are Involved in Clathrin-Mediated Vesicle Trafficking and Essential for Plant Growth

et al. 2017

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Proteomic analysis of clathrin‐coated vesicles

McPherson

2010

Proteomics

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For more than 50 years cell biologists have embraced the concept that biochemical and enzymatic analysis of isolated subcellular fractions provides insight into the function and machineries of cellular compartments including organelles. The utility of this approach has been significantly enhanced with the advent of mass spectrometry leading to the broad application of organelle proteomics. Clathrin-coated vesicles (CCVs) form at the plasma membrane where they select protein and lipid cargo for endocytic entry into cells. CCVs also form at the trans-Golgi network, where they function in protein transport from the secretory pathway to the endosomal/lysosomal system. Herein we will describe how organelle proteomics of CCVs has greatly expanded our knowledge of the machineries, mechanisms and sites of clathrin-mediated membrane trafficking.

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