<scp>SWIP</scp> mediates retromer‐independent membrane recruitment of the <scp>WASH</scp> complex

Dostal, V. A.; Humhalová, Tereza; Beránková, P.; Pácalt, Ondřej; Libusová, Lenka

doi:10.1111/tra.12884

Cited by 10 publications

(5 citation statements)

References 50 publications

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“…A single gene of SWIP (WASHC4) was seen in nearly all the parabasalids and A. ignava . SWIP was also recently identified to mediate the recruitment of the WASH complex to the endomembrane, independent of the Retromer complex (Dostál et al, 2023). The final WASH complex component: Strumpellin / STRUMP (WASHC5) also demonstrates a similar fashion of evolution, with single genes identified in the majority of the parabasalids and A. ignava .…”

Section: Resultsmentioning

confidence: 99%

Tracing back the expansion of the endomembrane rescue systems in parasitic Parabasalids to the ancestral origin in its free-living sister lineage

Shinde,

Kucerova,

Dacks

et al. 2024

Preprint

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Early Endosomes sort transmembrane cargo whether for lysosomal degradation or retrieval to the plasma membrane or the Golgi complex. Endosomal retrieval in eukaryotes is governed by the anciently homologous Retromer or Retriever complexes. Each comprises a core tri-protein subcomplex, membrane-deformation proteins, and interacting partner complexes, together retrieving a variety of known cargo proteins. Trichomonas vaginalis; a sexually transmitted human parasite uses the endomembrane system for pathogenesis. It has massively and selectively expanded its endomembrane protein complement, the evolutionary path of which has been largely unexplored. Our molecular evolutionary study of Retromer, Retriever and associated machinery in parabasalids and its free-living sister lineage of Anaeramoeba, demonstrates specific expansion of the Retromer machinery, contrasting with the Retriever components. We also observe partial loss of Commander complex and Sorting Nexins in Parabasalia but complete retention in Anaeramoeba. Notably, we identify putative parabasalid Sorting Nexin analogues. Finally, we report the first Retriever protein localization in a non- metazoan group along with Retromer protein localization in T. vaginalis. Therefore, we provide a unique genome expansion study of endomembrane trafficking system in parasitic and free- living protists alike.

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Section: Resultsmentioning

confidence: 99%

Tracing back the expansion of the endomembrane rescue systems in parasitic Parabasalids to the ancestral origin in its free-living sister lineage

Shinde,

Kucerova,

Dacks

et al. 2024

Preprint

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“…We could see no disruption to the recruitment of the WASH complex component FAM21 to VPS35 positive puncta, in line with the findings of McGough et al ( Figure 2C,D ) [ 14 , 15 ]. This reflects the complex nature of endosomal recruitment of WASH, that includes a role of ESCRT-0 and direct binding to phosphoinositides [ 27 , 28 ]. We also found no change in the steady state distribution of lysosomal sorting receptors, cation-independent mannose-6-phosphate receptor (CIM6PR, otherwise known as IGFR2) and Sortilin, nor in the processing of a representative cargo, the lysosomal enzyme Cathepsin D ( Figure 3 ).…”

Section: Resultsmentioning

confidence: 99%

The Parkinson's disease related mutant VPS35 (D620N) amplifies the LRRK2 response to endolysosomal stress

McCarron,

Elcocks,

Mortiboys

et al. 2024

Biochemical Journal

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The identification of multiple genes linked to Parkinson’s Disease invites the question as to how they may cooperate. We have generated isogenic cell lines that inducibly express either wild-type or a mutant form of the retromer component VPS35 (D620N), which has been linked to Parkinson’s Disease. This has enabled us to test proposed effects of this mutation in a setting where the relative expression reflects the physiological occurrence. We confirm that this mutation compromises VPS35 association with the WASH complex, but find no defect in WASH recruitment to endosomes, nor in the distribution of lysosomal receptors, cation-independent mannose-6-phosphate receptor and Sortilin. We show VPS35 (D620N) enhances the activity of the Parkinson’s associated kinase LRRK2 towards RAB12 under basal conditions. Furthermore, VPS35 (D620N) amplifies the LRRK2 response to endolysosomal stress resulting in enhanced phosphorylation of RABs 10 and 12. By comparing different types of endolysosomal stresses such as the ionophore nigericin and the membranolytic agent LLOMe, we are able to dissociate phospho-RAB accumulation from membrane rupture.

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“…A single gene of SWIP (WASHC4) was seen in nearly all the parabasalids and A. ignava . SWIP was also recently identified to mediate the recruitment of the WASH complex to the endomembrane, independent of the retromer complex ( Dostál et al, 2023 ). The final WASH complex component, strumpellin or STRUMP (WASHC5), also demonstrates a similar fashion of evolution, with single genes identified in the majority of the parabasalids and A. ignava .…”

Section: Resultsmentioning

confidence: 99%

The retromer and retriever systems are conserved and differentially expanded in parabasalids

Shinde,

Kučerová,

Dacks

et al. 2024

Journal of Cell Science

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Early Endosomes sort transmembrane cargo whether for lysosomal degradation or retrieval to the plasma membrane or the Golgi complex. Endosomal retrieval in eukaryotes is governed by the anciently homologous Retromer or Retriever complexes. Each comprises a core tri-protein subcomplex, membrane-deformation proteins, and interacting partner complexes, together retrieving a variety of known cargo proteins. Trichomonas vaginalis; a sexually transmitted human parasite uses the endomembrane system for pathogenesis. It has massively and selectively expanded its endomembrane protein complement, the evolutionary path of which has been largely unexplored. Our molecular evolutionary study of Retromer, Retriever and associated machinery in parabasalids and its free-living sister lineage of Anaeramoeba, demonstrates specific expansion of the Retromer machinery, contrasting with the Retriever components. We also observe partial loss of Commander complex and Sorting Nexins in Parabasalia but complete retention in Anaeramoeba. Notably, we identify putative parabasalid Sorting Nexin analogues. Finally, we report the first Retriever protein localization in a non-metazoan group along with Retromer protein localization in T. vaginalis.

show abstract

SWIP mediates retromer‐independent membrane recruitment of the WASH complex

Cited by 10 publications

References 50 publications

Tracing back the expansion of the endomembrane rescue systems in parasitic Parabasalids to the ancestral origin in its free-living sister lineage

Tracing back the expansion of the endomembrane rescue systems in parasitic Parabasalids to the ancestral origin in its free-living sister lineage

The Parkinson's disease related mutant VPS35 (D620N) amplifies the LRRK2 response to endolysosomal stress

The retromer and retriever systems are conserved and differentially expanded in parabasalids

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