The<i>Caenorhabditis elegans</i>GARP complex contains the conserved Vps51 subunit and is required to maintain lysosomal morphology

Luo, Lin; Hannemann, Mandy; Koenig, Sabine; Hegermann, Jan; Ailion, Michael; Cho, Min Kyu; Sasidharan, Nikhil; Zweckstetter, Markus; Rensing, Stefan A.; Eimer, Stefan

doi:10.1091/mbc.e10-06-0493

Cited by 27 publications

(38 citation statements)

References 65 publications

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“…S3) identified as being highly conserved within multicellular eukaryotes (Luo et al, 2011). Our yeast two-hybrid assay shows that UNH/VPS51 interacts with VPS52 (supplementary material Fig.…”

Section: Discussion Unh Is a Member Of Plant Garp Complexmentioning

confidence: 91%

“…Previous genomic analyses show high conservation of the VPS51 domain within eukaryotes (Luo et al, 2011). Of the three Fig.…”

Section: Discussion Unh Is a Member Of Plant Garp Complexmentioning

confidence: 91%

“…UNH contains a well-conserved motif (LVYENYKFISATDT) (supplementary material Fig. S3F) found in the VPS51 domain of higher eukaryotes (Luo et al, 2011) that shares closest homology to Oryza sativa and close similarity to Physcomitrella patens and Chlorella variabilis. Two other genes in Arabidopsis, At1g10385 and At5g16300, are also predicted to encode proteins with VPS51 domains but have considerably less conservation of the motif (supplementary material Fig.…”

Section: Unh Is Required For Leaf Shape and Vein Patternmentioning

confidence: 99%

“…Mutation to VPS51 in other eukaryotes has been shown to affect lysosomal structure and mis-sorting of lysosomal cargo to the extracellular space (Luo et al, 2011;Perez-Victoria et al, 2010b;Reggiori et al, 2003). To establish whether unh-1 causes defects to vacuole structure or targeting, we introduced markers into unh-1 mutants: VAC-YFP, a tonoplast marker including the C terminus of γ-TIP (Nelson et al, 2007); RHA1-YFP (RABF2A), a marker of PVC (Preuss et al, 2004); and AFVY-RFP, which in wild type is targeted to the lytic vacuole (Hunter et al, 2007).…”

Section: Vacuolar Targeting Is Disrupted In Unh-1mentioning

confidence: 99%

“…In yeast (Conibear et al, 2003;Reggiori et al, 2003;Siniossoglou and Pelham, 2002), humans (Perez-Victoria et al, 2010a and C. elegans (Luo et al, 2011), this complex tethers late endosome-derived vesicles at the TGN, allowing retrieval of lysosomal/vacuolar cargo receptors and processing enzymes. Defects to GARP components affect the sorting of lysosomal proteins and maintenance of lysosome function, and result in developmental defects in mice and C. elegans (Luo et al, 2011;Schmitt-John et al, 2005). The GARP complex is evolutionarily conserved and present in all eukaryotes (Koumandou et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Arabidopsis UNHINGED encodes a VPS51 homolog and reveals a role for the GARP complex in leaf shape and vein patterning

et al. 2014

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Asymmetric localization of PIN proteins controls directionality of auxin transport and many aspects of plant development. Directionality of PIN1 within the marginal epidermis and the presumptive veins of developing leaf primordia is crucial for establishing leaf vein pattern. One mechanism that controls PIN protein distribution within the cell membranes is endocytosis and subsequent transport to the vacuole for degradation. The Arabidopsis mutant unhinged-1 (unh-1) has simpler leaf venation with distal non-meeting of the secondary veins and fewer higher order veins, a narrower leaf with prominent serrations, and reduced root and shoot growth. We identify UNH as the Arabidopsis vacuolar protein sorting 51 (VPS51) homolog, a member of the Arabidopsis Golgi-associated retrograde protein (GARP) complex, and show that UNH interacts with VPS52, another member of the complex and colocalizes with trans Golgi network and pre-vacuolar complex markers. The GARP complex in yeast and metazoans retrieves vacuolar sorting receptors to the transGolgi network and is important in sorting proteins for lysosomal degradation. We show that vacuolar targeting is reduced in unh-1. In the epidermal cells of unh-1 leaf margins, PIN1 expression is expanded. The unh-1 leaf phenotype is partially suppressed by pin1 and cuc2-3 mutations, supporting the idea that the phenotype results from expanded PIN1 expression in the marginal epidermis. Our results suggest that UNH is important for reducing expression of PIN1 within margin cells, possibly by targeting PIN1 to the lytic vacuole.

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Section: Discussion Unh Is a Member Of Plant Garp Complexmentioning

confidence: 91%

“…Previous genomic analyses show high conservation of the VPS51 domain within eukaryotes (Luo et al, 2011). Of the three Fig.…”

Section: Discussion Unh Is a Member Of Plant Garp Complexmentioning

confidence: 91%

Section: Unh Is Required For Leaf Shape and Vein Patternmentioning

confidence: 99%

Section: Vacuolar Targeting Is Disrupted In Unh-1mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Arabidopsis UNHINGED encodes a VPS51 homolog and reveals a role for the GARP complex in leaf shape and vein patterning

et al. 2014

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Maintaining order: COG complex controls Golgi trafficking, processing, and sorting

2019

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The conserved oligomeric Golgi (COG) complex, a multisubunit tethering complex of the CATCHR (complexes associated with tethering containing helical rods) family, controls membrane trafficking and ensures Golgi homeostasis by orchestrating retrograde vesicle targeting within the Golgi. In humans, COG defects lead to severe multisystemic diseases known as COG‐congenital disorders of glycosylation (COG‐CDG). The COG complex both physically and functionally interacts with all classes of molecules maintaining intra‐Golgi trafficking, namely SNAREs, SNARE‐interacting proteins, Rabs, coiled‐coil tethers, and vesicular coats. Here, we review our current knowledge of COG‐related trafficking and glycosylation defects in humans and model organisms, and analyze possible scenarios for the molecular mechanism of the COG orchestrated vesicle targeting.

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A computational prediction of structure and function of novel homologue of Arabidopsis thaliana Vps51/Vps67 subunit in Corchorus olitorius

Zaman

Fancy

2012

Interdiscip Sci Comput Life Sci

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Vps mediated vesicular transport is important for transferring macromolecules trapped inside a vesicle. Although highly abundant, Vps shows tremendous sequence variation among diverse array of species. However, this difference in sequence, which seems to also translate into substantial functional variation, is hardly characterized in Corchorus spp. Here, our computational study investigates structural and functional features of one of the Vps subunit namely Vps51/Vps67 in C. olitorius. Broad scale structural characterization revealed novel information about the overall Vps structure and binding sites. Moreover, functional analyses indicate interaction partners which were unexplored to date. Since membrane trafficking is essentially associated with nutrient uptake and chemical de-toxification, characterization of the Vps subunit can well provide us with better insight into important agronomic traits such as stress response, immune response and phytoremediation capacity.

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TheCaenorhabditis elegansGARP complex contains the conserved Vps51 subunit and is required to maintain lysosomal morphology

Cited by 27 publications

References 65 publications

Arabidopsis UNHINGED encodes a VPS51 homolog and reveals a role for the GARP complex in leaf shape and vein patterning

Arabidopsis UNHINGED encodes a VPS51 homolog and reveals a role for the GARP complex in leaf shape and vein patterning

Maintaining order: COG complex controls Golgi trafficking, processing, and sorting

A computational prediction of structure and function of novel homologue of Arabidopsis thaliana Vps51/Vps67 subunit in Corchorus olitorius

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