VPS29–VPS35 intermediate of retromer is stable and may be involved in the retromer complex assembly process

Fuse, Atsuhito; Furuya, Norihiko; Kakuta, Soichiro; Inose, Aki; Sato, Mariko; Koike, Masato; Saiki, Sachio

doi:10.1016/j.febslet.2015.04.040

Cited by 37 publications

(25 citation statements)

References 29 publications

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“…reported by(Fuse et al (2015) decrease in expression of VPS26 was also observed in VPS35177 KD cell which eventually tells us expression as well as functionality of VPS subunits are 178 interdependent (Fig. S2B).…”

mentioning

confidence: 58%

Retromer retrieves the Wilson Disease protein, ATP7B from lysosomes in a copper-dependent mode

Gupta

Das

Maji

et al. 2020

Preprint

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localizes with lysosomal marker, Lamp1 and the core member of retromer complex, Vps35. 11Knocking down VPS35 did not alter copper-responsive vesicularization of ATP7B; rather upon 12 subsequent copper chelation, ATP7B failed to relocalize to TGN that could be rescued by 13 overexpressing wtVPS35. Using super-resolution microscopy and proximity ligation assays we 14 demonstrate that VPS35 and ATP7B are juxtaposed on the same lysosomal compartment and 15 their interaction is indirect. Utilizing in-cell photoamino acid-based UV-crosslinking and 16 subsequent immunoprecipitation, we detected ATP7B and retromer subunits, VPS35 and 17 VPS26 in a large complex in high copper conditions, hence confirming their interaction. We 18 demonstrate that retromer regulates lysosome to TGN trafficking of the copper transporter 19 ATP7B and it is dependent upon cellular copper level. 20

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mentioning

confidence: 58%

Retromer retrieves the Wilson Disease protein, ATP7B from lysosomes in a copper-dependent mode

Gupta

Das

Maji

et al. 2020

Preprint

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“…Consistent with this, loss of VPS35 destabilizes the retromer complex, resulting in reduced VPS26 and VPS29 protein, and this result has been confirmed both in vitro and in vivo (Cui et al, 2019;Liu et al, 2014;Wang et al, 2014). Similarly, knockdown or knockout of VPS29 in mammalian epithelial cell culture compromises retromer stability, causing loss of the other components (Fuse et al, 2015;Jimenez-Orgaz et al, 2017). Surprisingly, in the absence of Vps29 in Drosophila, we found that Vps35 and Vps26 are present at normal levels and remain tightly associated.…”

Section: Vps29 Is Required For Retromer Recruitment Via Rab7 and Tbc1d5mentioning

confidence: 74%

“…In prior studies of HeLa cell cultures, VPS29 knockdown caused reduced levels of both VPS35 and VPS26, likely due to destabilization of the retromer trimer complex and subunit turnover (Fuse et al, 2015;Jimenez-Orgaz et al, 2017). Reciprocally, enhancing interactions between VPS29 and VPS35 promotes retromer stability (Mecozzi et al, 2014;Young et al, 2018).…”

Section: Vps29 Regulates Retromer Localization and Is Required In Thementioning

confidence: 94%

“…Deletion of Vps29 in yeast or C. elegans phenocopies Vps35 loss-of-function (Lorenowicz et al, 2014;Seaman et al, 1997). In mammalian epithelial cell culture, reducing VPS29 results in apparent destabilization and degradation of both VPS35 and VPS26 (Fuse et al, 2015;Jimenez-Orgaz et al, 2017). Reciprocally, pharmacological chaperones targeting the VPS35-VPS29 interface can stabilize the complex and enhance retromer function (Mecozzi et al, 2014;Young et al, 2018).…”

Section: Introductionmentioning

confidence: 99%

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Retromer subunit, VPS29, regulates synaptic transmission and is required for endolysosomal function in the aging brain

Ojelade

Li‐Kroeger

et al. 2019

Preprint

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AbstractRetromer, including Vps35, Vps26, and Vps29, is a protein complex responsible for recycling proteins within the endolysosomal pathway. Although implicated in both Parkinson’s and Alzheimer’s disease, our understanding of retromer function in the adult brain remains limited, in part because Vps35 and Vps26 are essential for development. In Drosophila, we find that Vps29 is dispensable for embryogenesis but required for retromer function in aging adults, including for synaptic transmission, survival, and locomotion. Unexpectedly, in Vps29 mutants, Vps35 and Vps26 proteins are normally expressed and associated, but retromer is mislocalized from neuropil to soma with the Rab7 GTPase. Further, Vps29 phenotypes are suppressed by reducing Rab7 or overexpressing the GTPase activating protein, TBC1D5. With aging, retromer insufficiency triggers progressive endolysosomal dysfunction, with ultrastructural evidence of impaired substrate clearance and lysosomal stress. Our results reveal the role of Vps29 in retromer localization and function, highlighting requirements for brain homeostasis in aging.Impact StatementVps29 promotes retromer localization in the adult Drosophila brain, engaging Rab7 and TBC1D5, and its loss triggers age-dependent neuronal impairments in endolysosomal trafficking and synaptic transmission.

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“…The over-expression of the top 25 genes in hepatic schistosomula appears to reflect a diversity of physiological activities, including transcriptional (homeobox protein engrailed-like SMOX-2 [47, 48], serum and glucocorticoid-regulated kinase 1 (SGK1) [49] and nuclear receptor subfamily 4 group A [50, 51]) and neuronal (protocadherin FAT4 [52], Aromatic-L-amino-acid decarboxylase [53] and delphilin [54]) activities, together with tegumental integrity (annexin A3 [55, 56]), skeletal morphogenesis (protocadherin FAT4 [57]) and endosome-to-Golgi retrieval (vacuolar protein sorting-associated protein 29 [58]).…”

Section: Resultsmentioning

confidence: 99%

A next-generation microarray further reveals stage-enriched gene expression pattern in the blood fluke Schistosoma japonicum

et al. 2017

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BackgroundSchistosomiasis is caused by infection with blood flukes of the genus Schistosoma, and ranks, in terms of disability-adjusted life years (DALYs), as the third most important neglected tropical disease. Schistosomes have several discrete life stages involving dramatic morphological changes during their development, which require subtle gene expression modulations to complete the complex life-cycle.ResultsIn the current study, we employed a second generation schistosome DNA chip printed with the most comprehensive probe array for studying the Schistosoma japonicum transcriptome, to explore stage-associated gene expression in different developmental phases of S. japonicum. A total of 328, 95, 268 and 532 mRNA transcripts were enriched in cercariae, hepatic schistosomula, adult worms and eggs, respectively. In general, genes associated with transcriptional regulation, cell signalling and motor activity were readily expressed in cercariae; the expression of genes involved in neuronal activities, apoptosis and renewal was modestly upregulated in hepatic schistosomula; transcripts involved in egg production, nutrition metabolism and glycosylation were enriched in adult worms; while genes involved in cell division, microtubule-associated mobility, and host-parasite interplay were relatively highly expressed in eggs.ConclusionsThe study further highlights the expressional features of stage-associated genes in schistosomes with high accuracy. The results provide a better perspective of the biological characteristics among different developmental stages, which may open new avenues for identification of novel vaccine candidates and the development of novel control interventions against schistosomiasis.Electronic supplementary materialThe online version of this article (doi:10.1186/s13071-016-1947-x) contains supplementary material, which is available to authorized users.

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VPS29–VPS35 intermediate of retromer is stable and may be involved in the retromer complex assembly process

Cited by 37 publications

References 29 publications

Retromer retrieves the Wilson Disease protein, ATP7B from lysosomes in a copper-dependent mode

Retromer retrieves the Wilson Disease protein, ATP7B from lysosomes in a copper-dependent mode

Retromer subunit, VPS29, regulates synaptic transmission and is required for endolysosomal function in the aging brain

A next-generation microarray further reveals stage-enriched gene expression pattern in the blood fluke Schistosoma japonicum

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