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Regulation of retromer recruitment to endosomes by sequential action of Rab5 and Rab7

Rojas, Raul, van Vlijmen, Thijs, Mardones, Gonzalo A., Prabhu, Yogikala, Rojas, Adriana L., Mohammed, Shabaz, Heck, Albert J.R., Raposo, Graça, van der Sluijs, Peter, Bonifacino, Juan S.·2008·The Journal of Cell Biology
DOI 10.1083/jcb.200804048PMC PMC2575791
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Abstract

The retromer complex mediates retrograde transport of transmembrane cargo from endosomes to the trans-Golgi network (TGN). Mammalian retromer is composed of a sorting nexin (SNX) dimer that binds to phosphatidylinositol 3-phosphate–enriched endosomal membranes and a vacuolar protein sorting (Vps) 26/29/35 trimer that participates in cargo recognition. The mammalian SNX dimer is necessary but not sufficient for recruitment of the Vps26/29/35 trimer to membranes. In this study, we demonstrate that the guanosine triphosphatase Rab7 contributes to this recruitment. The Vps26/29/35 trimer specifically binds to Rab7–guanosine triphosphate (GTP) and localizes to Rab7-containing endosomal domains. Interference with Rab7 function causes dissociation of the Vps26/29/35 trimer but not the SNX dimer from membranes. This blocks retrieval of mannose 6-phosphate receptors to the TGN and impairs cathepsin D sorting. Rab5-GTP does not bind to the Vps26/29/35 trimer, but perturbation of Rab5 function causes dissociation of both the SNX and Vps26/29/35 components from membranes through inhibition of a pathway involving phosphatidylinositol 3-kinase. These findings demonstrate that Rab5 and Rab7 act in concert to regulate retromer recruitment to endosomes.

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  • An increase in pro-CTSD is a reliable indicator of impaired retromer-dependent trafficking and ultimately lysosomal dysfunction.

    “Thus, an increase in pro-CTSD is considered a reliable indicator of impaired retromer-dependent trafficking (Benes et al., 2008; Rojas et al., 2008; Han et al., 2021), and ultimately lysosomal dysfunction.”

    From The neuronal retromer can regulate both neuronal and microglial phenotypes of Alzheimer's disease (2022) · cites this paper as Rojas et al., 2008

    The Results section (Fig. 9) reports that Rab7 or Vps26 depletion increased precursor cathepsin D and interprets this as evidence of impaired transport to lysosomes, consistent with disrupted retromer function. It does not establish that increased pro-CTSD is a reliable, specific indicator of impaired retromer-dependent trafficking or demonstrate broader lysosomal dysfunction. (LLM, conf=0.84)

    Experimental — accuracy not yet measured

  • Endosomal recruitment of the Retromer requires Rab5 and Rab7.

    “Endosomal recruitment of the Retromer requires Rab5 and Rab7.73”

    From Endosomal protein DENND10 promotes developmental competence of neurite extension (2025) · cites this paper as [73]

  • Retriever and retromer reside on the same endosomal sub-domain, distinct from ESCRT sub-domain.

    “Swelling of individual endosomes through expression of a constitutively active Rab5 (Rab5(Q79L))46 established that endogenous retriever and retromer resided on the same endosomal sub-domain, and that this ‘retrieval’ sub-domain was distinct to the ESCRT sub-domain (Figure 4A).”

    From Retriever is a multiprotein complex for retromer-independent endosomal cargo recycling (2017) · cites this paper as [46]

    The Results (‘Colocalization of Rab7 with retromer,’ page unavailable) place retromer on endosomal buds and tubules, but do not examine retriever or ESCRT. Searches for ‘retriever,’ ‘ESCRT,’ and ‘Rab5a-Q79L’ found no passage establishing that retriever and retromer share a sub-domain distinct from ESCRT. (LLM, conf=0.76)

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Metadata

Authors
Rojas, R., van Vlijmen, T., Mardones, G. A., Prabhu, Y., Rojas, A. L., Mohammed, S., Heck, A. J. R., Raposo, G., van der Sluijs, P., & Bonifacino, J. S.
Venue
The Journal of Cell Biology
Publisher
Rockefeller University Press
Published
2008-11-03
Volume
183
Issue
3
Pages
513-526
ISSN
  • 1540-8140
  • 0021-9525
DOI
10.1083/jcb.200804048
PMC
PMC2575791
Cited by
455
References
2
Language
en

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