Vps10p Transport from the<i>trans</i>-Golgi Network to the Endosome Is Mediated by Clathrin-coated Vesicles

Deloche, Olivier; Yeung, Bonny G.; Payne, Grégory S.; Schekman, Randy

doi:10.1091/mbc.12.2.475

Cited by 58 publications

(71 citation statements)

References 67 publications

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“…Impairment of Golgi glycosylation may also result from the mislocalization of mannosyltransferases, as described for Mnn1p in clathrin heavy chain thermosensitive mutant cells (Graham et al, 1994). Indeed, the location of various late Golgi membrane-bound proteins is known to depend on their continual clathrin-dependent sorting to the late endosome, followed by retrieval to the TGN (Deloche et al, 2001). Recent results have suggested that the sorting of late Golgi proteins may also include trafficking through early endosomes, and that several retrieval pathways, possibly overlapping, may be involved in maintaining the steady-state levels of various late Golgi proteins (Lewis et al, 2000).…”

Section: Deletions That Directly or Indirectly Impair Golgi Glycosylamentioning

confidence: 97%

Mutants defective in secretory/vacuolar pathways in the EUROFAN collection of yeast disruptants

Avaro

Belgareh‐Touzé

Sibella-Argüelles

et al. 2002

Yeast

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We have screened the EUROFAN (European Functional Analysis Network) deletion strain collection for yeast mutants defective in secretory/vacuolar pathways and/or associated biochemical modifications. We used systematic Western immunoblotting to analyse the electrophoretic pattern of several markers of the secretory/vacuolar pathways, the soluble a-factor, the periplasmic glycoprotein invertase, the plasma membrane GPIanchored protein Gas1p, and two vacuolar proteins, the soluble carboxypeptidase Y and the membrane-bound alkaline phosphatase, which are targeted to the vacuole by different pathways. We also used colony immunoblotting to monitor the secretion of carboxypeptidase Y into the medium, to identify disruptants impaired in vacuolar targeting. We identified 25 mutants among the 631 deletion strains. Nine of these mutants were disrupted in genes identified in recent years on the basis of their involvement in trafficking (VPS53, VAC7, VAM6, APM3, SYS1), or glycosylation (ALG12, ALG9, OST4, ROT2). Three of these genes were identified on the basis of trafficking defects by ourselves and others within the EUROFAN project (TLG2, RCY1, MON2). The deletion of ERV29, which encodes a COPII vesicle protein, impaired carboxypeptidase Y trafficking from the endoplasmic reticulum to the Golgi apparatus. We also identified eight unknown ORFs, the deletion of which reduced Golgi glycosylation or impaired the Golgi to vacuole trafficking of carboxypeptidase Y. YJR044c, which we identified as a new VPS gene, encodes a protein with numerous homologues of unknown function in sequence databases.

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Section: Deletions That Directly or Indirectly Impair Golgi Glycosylamentioning

confidence: 97%

Mutants defective in secretory/vacuolar pathways in the EUROFAN collection of yeast disruptants

Avaro

Belgareh‐Touzé

Sibella-Argüelles

et al. 2002

Yeast

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“…This resembles protein stabilization in cells defective in vesicular fusion with endosomes. For example, a mutant CPY receptor Vps10p, lacking the TGN retrieval signal is stabilized in pep12⌬, vps45 and vps21 mutant cells because vacuolar transport is prevented by a block in Journal of Cell Science 121 (3) the fusion of TGN-derived vesicles with late endosomes (Bryant and Stevens, 1998;Deloche et al, 2001;Gerrard et al, 2000a). Therefore, the increased stability of Pep12p in ent3⌬ cells may indicate a block in the forward transport of Pep12p to late endosomes.…”

Section: Ent3p Function As Cargo Adaptor For Pep12p Requires the Fsd mentioning

confidence: 99%

ENTH domain proteins are cargo adaptors for multiple SNARE proteins at the TGN endosome

Chidambaram

Zimmermann

Mollard

2008

Journal of Cell Science

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The vesicle-mediated membrane transport is a multi-step process, consisting of vesicle formation (budding), targeting, tethering and membrane fusion (Bonifacino and Glick, 2004;Jahn and Scheller, 2006). Cargo proteins are concentrated at a specialized region on the donor membrane and packed into a nascent vesicle generated by the assembly of coat proteins such as clathrin into a cage-like lattice around the budding vesicle. Adaptor protein complexes (AP) are required to recruit cargo into coated vesicles thus playing an essential role in cargo selectivity of the transport vesicle in traffic between the trans-Golgi network (TGN) and endosomes (Owen et al., 2004). Gga proteins are monomeric clathrin adaptor proteins mediating TGN to the endosome transport (Nakayama and Wakatsuki, 2003). Apart from the AP complexes and the monomeric GGA adaptors, the list is expanding to new sets of adaptors, which are specific to only a particular type of cargo or to one family of cargo (Bonifacino and Rojas, 2006).Recently, the epsin family proteins came into view as cargospecific adaptors. The ENTH (epsin N-terminal homology) domains are phosphotidylinositol binding modules present in both mammalian epsins and in their yeast homologues Ent1p to Ent4p (Duncan and Payne, 2003;Legendre-Guillemin et al., 2004). ANTH (AP180 N-terminal homology) domains are highly related to ENTH domains (Ford et al., 2001) and present in mammalian AP180 (also known as SNAP91), CALM, HIP1, Hip1R and yeast AP180, Sla2p and Ent5p. These domains bind to different phosphoinositides. In addition to ANTH or ENTH domains, these proteins also contain binding motifs for clathrin, AP or GGA allowing them to participate in clathrin-mediated budding at the TGN, endosome or at the plasma membrane. Phylogenetic analysis of ENTH domains suggested two ENTH domain branches, mammalian epsins 1-3 and yeast Ent1p and Ent2p, which are involved in endocytosis at the plasma membrane, and enthoprotin (also known as Clint and epsinR) and yeast Ent3p functioning in transport between the TGN and endosomes (Legendre-Guillemin et al., 2004). EpsinR is localized to the TGN and in endosomal membranes (Kalthoff et al., 2002;Wasiak et al., 2002) and binds to PtdIns4P (Hirst et al., 2003;Mills et al., 2003). It also binds to clathrin, AP1 and GGA2 through its C-terminal domain Mills et al., 2003;Wasiak et al., 2002). Ent3p and Ent5p are partially redundant, bind Gga proteins and AP1 and promote formation of clathrin coats at the TGN-endosome (Costaguta et al., 2006;. ENTH domains of Ent3p and Ent5p bind PtdIns(3,5)P 2 (Eugster et al., 2004;Friant et al., 2003) and PtdIns(4,5)P 2 (Narayan and Lemmon, 2006). Ent5p associates with Vps27p and together with Ent3p is required for ubiquitin-dependent protein sorting into the interior of multivesicular bodies (MVB) (Eugster et al., 2004;Friant et al., 2003). This indicates that Ent3p and Ent5p have two different functions at the TGN-endosome and in MVB.Previously, we reported that the ENTH domains of Ent3p and epsinR specifically interact wi...

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“…The major route involves a receptor-mediated sorting event at the trans-Golgi network (TGN), packaging into clathrincoated vesicles with the help of an AP1-adaptor complex, and receptor-ligand dissociation in a multivesicular prevacuolar/ endosomal compartment (PVC) before delivery into the lysosome/vacuole. This transport pathway is well known for mammalian (Doray et al, 2002;Ghosh et al, 2003;Gruenberg and Stenmark, 2004) and yeast (Wurmser and Emr, 1998;Costaguta et al, 2001;Deloche et al, 2001) cells and has now been established for plants (Paris and Neuhaus, 2002;Juergens, 2004;Tse et al, 2004). A second route, bypassing the PVC and involving the AP3-adaptor complex, but not clathrin, has been shown to be responsible for the transport of some enzymes, such as alkaline phosphatase, to the vacuole in yeast (e.g., Stepp et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

Plant Retromer, Localized to the Prevacuolar Compartment and Microvesicles inArabidopsis, May Interact with Vacuolar Sorting Receptors

et al. 2006

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Receptors for acid hydrolases destined for the lytic compartment in yeast and mammalian cells are retrieved from intermediate, endosomal organelles with the help of a pentameric protein complex called the retromer. We cloned the Arabidopsis thaliana homologs of the three yeast proteins (Vps35, Vps29, and Vps26) constituting the larger subunit of retromer and prepared antisera against them. With these antibodies, we demonstrated the presence of a retromer-like protein complex in salt extracts prepared from Arabidopsis microsomes. This complex is associated with membranes that coequilibrate with prevacuolar compartment markers and with high-density sedimenting membranes. Immunogold negative staining identified these membranes as 90-nm-diameter coated microvesicles. Confocal laser scanning immunofluorescence studies performed on tobacco (Nicotiana tabacum) BY-2 cells revealed high degrees of colabeling between all three retromer antisera and the prevacuolar compartment (PVC) markers PEP12 and vacuolar sorting receptor VSR At-1 . The presence of plant retromer at the surface of multivesicular bodies was also demonstrated by immunogold labeling of sections obtained from high-pressure frozen/freeze-substituted specimens. Treatment of BY-2 cells with wortmannin led to swelling of the PVC and a separation of the VPS35 and VSR signals. Preliminary data suggesting that retromer interacts with the cytosolic domain of a VSR were obtained by immunoprecipitation experiments performed on detergent-solubilized microsomes with Vps35 antibodies.

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Vps10p Transport from thetrans-Golgi Network to the Endosome Is Mediated by Clathrin-coated Vesicles

Cited by 58 publications

References 67 publications

Mutants defective in secretory/vacuolar pathways in the EUROFAN collection of yeast disruptants

Mutants defective in secretory/vacuolar pathways in the EUROFAN collection of yeast disruptants

ENTH domain proteins are cargo adaptors for multiple SNARE proteins at the TGN endosome

Plant Retromer, Localized to the Prevacuolar Compartment and Microvesicles inArabidopsis, May Interact with Vacuolar Sorting Receptors

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