The Retromer Coat Complex Coordinates Endosomal Sorting and Dynein-Mediated Transport, with Carrier Recognition by the trans-Golgi Network

Wassmer, Thomas; Attar, Naomi; Harterink, Martin; Weering, Jan R.T. van; Traer, Colin J.; Oakley, Jacqueline; Goud, Bruno; Stephens, David; Verkade, Paul; Korswagen, Hendrik C.; Cullen, Peter J.

doi:10.1016/j.devcel.2009.04.016

Cited by 268 publications

(317 citation statements)

References 61 publications

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“…Consistent with our findings, they discovered that SNX6 associates with p150 Glued and that SNX6 interacts with SNX1/2 [40]. They also demonstrated that suppression of p150 Glued redistributes the retromer-labeled endosomes from regions surrounding the TGN to a more peripheral location [40]. In our study, to investigate the role of adaptor protein-mediated motor-cargo interaction, we overexpressed the N-terminus of p150 Glued as a dominant-negative mutant to compete with endogenous WT protein for dynein, and found that this mutant, which lacks the SNX6 interaction site, causes failure in formation, stabilization and exit of retromer-associated transport intermediates from endosomes, therefore blocking CI-MPR retrieval (Figure 8 and Supplementary information, Movies S3-S5).…”

Section: Discussionsupporting

confidence: 80%

“…While this paper was in preparation, the SNX6-p150 Glued interaction was reported by Peter J Cullen's group [40]. Consistent with our findings, they discovered that SNX6 associates with p150 Glued and that SNX6 interacts with SNX1/2 [40].…”

Section: Discussionsupporting

confidence: 79%

Section: Discussionsupporting

confidence: 77%

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The retromer component SNX6 interacts with dynactin p150Glued and mediates endosome-to-TGN transport

et al. 2009

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The retromer is a protein complex that mediates retrograde transport of transmembrane cargoes from endosomes to the trans-Golgi network (TGN). It is comprised of a cargo-selection subcomplex of Vps26, Vps29 and Vps35 and a membrane-binding coat subcomplex of sorting nexins (SNXs). Previous studies identified SNX1/2 as one of the components of the SNX subcomplex, and SNX5/6 as candidates for the second SNX. How the retromer-associated cargoes are recognized and transported by molecular motors are largely unknown. In this study, we found that one of SNX1/2's dimerization partners, SNX6, interacts with the p150 Glued subunit of the dynein/dynactin motor complex. We present evidence that SNX6 is a component of the retromer, and that recruitment of the motor complex to the membrane-associated retromer requires the SNX6-p150 Glued interaction. Disruption of the SNX6-p150 Glued interaction causes failure in formation and detachment of the tubulovesicular sorting structures from endosomes and results in block of CI-MPR retrieval from endosomes to the TGN. These observations indicate that in addition to SNX1/2, SNX6 in association with the dynein/dynactin complex drives the formation and movement of tubular retrograde intermediates.

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Section: Discussionsupporting

confidence: 80%

Section: Discussionsupporting

confidence: 79%

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The retromer component SNX6 interacts with dynactin p150Glued and mediates endosome-to-TGN transport

et al. 2009

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“…Furthermore, we sought to determine whether toca-1(tm2056); toca-2 (ng11) double mutant, or RNAi-mediated depletion of cdc-42 or par-6 by RNAi, effects on ALM polarity are enhanced by retromer mutant vps-29(tm1320). Previous work showed that the Wnt phenotype of vps-29(tm1320) is much weaker than that of vps-26 or vps-35 mutants but shows enhanced phenotypes when combined with mutations in known Wnt-pathway components or retrograde recycling regulators (13,(48)(49)(50). Consistent with published work, we observed only normal ALM polarity in vps-29 (tm1320) single mutants (47).…”

Section: Loss Ofsupporting

confidence: 82%

A TOCA/CDC-42/PAR/WAVE functional module required for retrograde endocytic recycling

Bai

Grant

2015

Proc. Natl. Acad. Sci. U.S.A.

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Endosome-to-Golgi transport is required for the function of many key membrane proteins and lipids, including signaling receptors, small-molecule transporters, and adhesion proteins. The retromer complex is well-known for its role in cargo sorting and vesicle budding from early endosomes, in most cases leading to cargo fusion with the trans-Golgi network (TGN). Transport from recycling endosomes to the TGN has also been reported, but much less is understood about the molecules that mediate this transport step. Here we provide evidence that the F-BAR domain proteins TOCA-1 and TOCA-2 (Transducer of Cdc42 dependent actin assembly), the small GTPase CDC-42 (Cell division control protein 42), associated polarity proteins PAR-6 (Partitioning defective 6) and PKC-3/atypical protein kinase C, and the WAVE actin nucleation complex mediate the transport of MIG-14/Wls and TGN-38/TGN38 cargo proteins from the recycling endosome to the TGN in Caenorhabditis elegans. Our results indicate that CDC-42, the TOCA proteins, and the WAVE component WVE-1 are enriched on RME-1-positive recycling endosomes in the intestine, unlike retromer components that act on early endosomes. Furthermore, we find that retrograde cargo TGN-38 is trapped in early endosomes after depletion of SNX-3 (a retromer component) but is mainly trapped in recycling endosomes after depletion of CDC-42, indicating that the CDC-42-associated complex functions after retromer in a distinct organelle. Thus, we identify a group of interacting proteins that mediate retrograde recycling, and link these proteins to a poorly understood trafficking step, recycling endosome-to-Golgi transport. We also provide evidence for the physiological importance of this pathway in WNT signaling.retromer | endocytic recycling | endosome | toca | wave

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“…The retromer is a multiprotein complex, conserved among eukaryotes, that is involved in the recycling of transmembrane receptors and retrograde transport of cargo proteins from endosomes to the trans-Golgi network (13). In mammals, the retromer consists of two distinct subcomplexes: one composed of a dimer of Sorting Nexins (SNXs) and the other, known as the core retromer, consisting of a trimer of vacuolar protein sorting (VPS) 26, VPS29, and VPS35 proteins (13,14). The Arabidopsis genome contains genes encoding all components of the retromer complex, including three SNX genesdesignated SNX1, SNX2a, and SNX2b-three genes coding for VPS35 isoforms (VPS35a, VPS35b, and VPS35c), two genes encoding VPS26 isoforms (VPS26a and VPS26b), and a single gene encoding VPS29 (12,(15)(16)(17).…”

mentioning

confidence: 99%

Peroxisome extensions deliver the Arabidopsis SDP1 lipase to oil bodies

Thazar-Poulot

Miquel

Fobis-Loisy

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

153

127

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Lipid droplets/oil bodies (OBs) are lipid-storage organelles that play a crucial role as an energy resource in a variety of eukaryotic cells. Lipid stores are mobilized in the case of food deprivation or high energy demands-for example, during certain developmental processes in animals and plants. OB degradation is achieved by lipases that hydrolyze triacylglycerols (TAGs) into free fatty acids and glycerol. In the model plant Arabidopsis thaliana, Sugar-Dependent 1 (SDP1) was identified as the major TAG lipase involved in lipid reserve mobilization during seedling establishment. Although the enzymatic activity of SDP1 is associated with the membrane of OBs, its targeting to the OB surface remains uncharacterized. Here we demonstrate that the core retromer, a complex involved in protein trafficking, participates in OB biogenesis, lipid store degradation, and SDP1 localization to OBs. We also report an as-yet-undescribed mechanism for lipase transport in eukaryotic cells, with SDP1 being first localized to the peroxisome membrane at early stages of seedling growth and then possibly moving to the OB surface through peroxisome tubulations. Finally, we show that the timely transfer of SDP1 to the OB membrane requires a functional core retromer. In addition to revealing previously unidentified functions of the retromer complex in plant cells, our work provides unanticipated evidence for the role of peroxisome dynamics in interorganelle communication and protein transport.oil bodies | retromer | SDP1 lipase | peroxisome | protein trafficking

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The Retromer Coat Complex Coordinates Endosomal Sorting and Dynein-Mediated Transport, with Carrier Recognition by the trans-Golgi Network

Cited by 268 publications

References 61 publications

The retromer component SNX6 interacts with dynactin p150Glued and mediates endosome-to-TGN transport

The retromer component SNX6 interacts with dynactin p150Glued and mediates endosome-to-TGN transport

A TOCA/CDC-42/PAR/WAVE functional module required for retrograde endocytic recycling

Peroxisome extensions deliver the Arabidopsis SDP1 lipase to oil bodies

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