CONTINUOUS VASCULAR RING (COV1) is a trans-Golgi Network-Localized Membrane Protein Required for Golgi Morphology and Vacuolar Protein Sorting

Shirakawa, Makoto; Ueda, Haruko; Koumoto, Yasuko; Fuji, Kentaro; Nishiyama, Chiaki; Kohchi, Takayuki; Hara‐Nishimura, Ikuko; Shimada, Tomoo

doi:10.1093/pcp/pct195

Cited by 34 publications

(33 citation statements)

References 53 publications

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“…Many mutants with similar phenotypes have been reported thus far, including mutants of vacuolar sorting receptors, vacuolar processing enzymes, and machinery components of membrane trafficking (Shimada et al, 2003a(Shimada et al, , 2003bTamura et al, 2007;Yamazaki et al, 2008;Ebine et al, 2008Ebine et al, , 2014Takahashi et al, 2010;Contento and Bassham, 2012;Shirakawa et al, 2014;Gao et al, 2015;Reguera Teh et al, 2015). In these mutants, the accumulation of unprocessed precursors is also observed for 2S albumin, a major storage protein in Arabidopsis seeds.…”

Section: How Does Erex Mediate Vacuolar Trafficking With Rab5?mentioning

confidence: 66%

ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN, an Interacting Partner of RAB5 GTPases, Regulates Membrane Trafficking to Protein Storage Vacuoles in Arabidopsis

et al. 2016

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ORCID ID: 0000-0001-7441-0203 (H.T.S.)RAB5 GTPases act as molecular switches that regulate various endosomal functions in animal cells, including homotypic fusion of early endosomes, endosomal motility, endosomal signaling, and subcompartmentalization of the endosomal membrane. RAB5 proteins fulfill these diverse functions through interactions with downstream effector molecules. Two canonical RAB5 members, ARA7 and RAB HOMOLOG1 (RHA1), are encoded in the Arabidopsis thaliana genome. ARA7 and RHA1 play crucial roles in endocytic and vacuolar trafficking pathways. Plant RAB5 GTPases function via interactions with effector molecules, whose identities and functions are currently unclear. In this study, we searched for canonical RAB5 effector molecules of Arabidopsis and identified a candidate, which we called ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN (EREX). The intimate genetic interaction between EREX and RAB5 members, the results from subcellular colocalization experiments, and the direct interaction observed in an in vitro pull-down assay strongly suggest that EREX is a genuine effector of canonical RAB5s in Arabidopsis. We further found that close homologs of EREX play partially redundant functions with EREX in the transport of seed storage proteins. Our results indicate that canonical plant RAB5s acquired distinct effector molecules from those of non-plant systems to fulfill their functions.

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Section: How Does Erex Mediate Vacuolar Trafficking With Rab5?mentioning

confidence: 66%

ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN, an Interacting Partner of RAB5 GTPases, Regulates Membrane Trafficking to Protein Storage Vacuoles in Arabidopsis

et al. 2016

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“…Another mutant with a similar phenotype is continuous vascular ring (cov1; At2g20120) (Parker et al, 2003). Recently, COV1 was identified to be a transGolgi network localized membrane protein, and the cov1 mutant was shown to exhibit abnormal Golgi morphology and defects in vacuolar protein sorting (Shirakawa et al, 2014). The connection between membrane trafficking and vascular cambium development remains to be clarified.…”

Section: Arabidopsis Mutants With Enhanced Shoot Secondary Developmentmentioning

confidence: 99%

Vascular Cambium Development

Nieminen

Blomster

Helariutta

et al. 2015

The Arabidopsis Book

116

110

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Secondary phloem and xylem tissues are produced through the activity of vascular cambium, the cylindrical secondary meristem which arises among the primary plant tissues. Most dicotyledonous species undergo secondary development, among them Arabidopsis. Despite its small size and herbaceous nature, Arabidopsis displays prominent secondary growth in several organs, including the root, hypocotyl and shoot. Together with the vast genetic resources and molecular research methods available for it, this has made Arabidopsis a versatile and accessible model organism for studying cambial development and wood formation. In this review, we discuss and compare the development and function of the vascular cambium in the Arabidopsis root, hypocotyl, and shoot. We describe the current understanding of the molecular regulation of vascular cambium and compare it to the function of primary meristems. We conclude with a look at the future prospects of cambium research, including opportunities provided by phenotyping and modelling approaches, complemented by studies of natural variation and comparative genetic studies in perennial and woody plant species.

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“…The vacuolar trafficking in plants has been studied by monitoring the transport of reporter proteins to lytic vacuoles in vegetative cells and tissues (Jin et al, 2001;Pimpl et al, 2003;Miao et al, 2008;Niemes et al, 2010). Recently, seed storage proteins became a model cargo for monitoring the transport of endogenous vacuolar proteins in plants (Shimada et al, 2003a;Sanmartín et al, 2007;Isono et al, 2010;Pourcher et al, 2010;Uemura et al, 2012;Shirakawa et al, 2014). During seed maturation, a large amount of storage proteins are synthesized and sorted to specialized vacuoles, the protein storage vacuoles (PSVs).…”

mentioning

confidence: 99%

The Adaptor Complex AP-4 Regulates Vacuolar Protein Sorting at the trans-Golgi Network by Interacting with VACUOLAR SORTING RECEPTOR1

et al. 2015

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Adaptor protein (AP) complexes play critical roles in protein sorting among different post-Golgi pathways by recognizing specific cargo protein motifs. Among the five AP complexes (AP-1-AP-5) in plants, AP-4 is one of the most poorly understood; the AP-4 components, AP-4 cargo motifs, and AP-4 functional mechanism are not known. Here, we identify the AP-4 components and show that the AP-4 complex regulates receptor-mediated vacuolar protein sorting by recognizing VACUOLAR SORTING RECEPTOR1 (VSR1), which was originally identified as a sorting receptor for seed storage proteins to target protein storage vacuoles in Arabidopsis (Arabidopsis thaliana). From the vacuolar sorting mutant library GREEN FLUORESCENT SEED (GFS), we isolated three gfs mutants that accumulate abnormally high levels of VSR1 in seeds and designated them as gfs4, gfs5, and gfs6. Their responsible genes encode three (AP4B, AP4M, and AP4S) of the four subunits of the AP-4 complex, respectively, and an Arabidopsis mutant (ap4e) lacking the fourth subunit, AP4E, also had the same phenotype. Mass spectrometry demonstrated that these four proteins form a complex in vivo. The four mutants showed defects in the vacuolar sorting of the major storage protein 12S globulins, indicating a role for the AP-4 complex in vacuolar protein transport. AP4M bound to the tyrosine-based motif of VSR1. AP4M localized at the trans-Golgi network (TGN) subdomain that is distinct from the AP-1-localized TGN subdomain. This study provides a novel function for the AP-4 complex in VSR1-mediated vacuolar protein sorting at the specialized domain of the TGN.

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CONTINUOUS VASCULAR RING (COV1) is a trans-Golgi Network-Localized Membrane Protein Required for Golgi Morphology and Vacuolar Protein Sorting

Cited by 34 publications

References 53 publications

ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN, an Interacting Partner of RAB5 GTPases, Regulates Membrane Trafficking to Protein Storage Vacuoles in Arabidopsis

ENDOSOMAL RAB EFFECTOR WITH PX-DOMAIN, an Interacting Partner of RAB5 GTPases, Regulates Membrane Trafficking to Protein Storage Vacuoles in Arabidopsis

Vascular Cambium Development

The Adaptor Complex AP-4 Regulates Vacuolar Protein Sorting at the trans-Golgi Network by Interacting with VACUOLAR SORTING RECEPTOR1

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