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Inhibition of TBC1D5 activates Rab7a and can enhance the function of the retromer cargo-selective complex

Seaman, Matthew N. J., Mukadam, Aamir S., Breusegem, Sophia Y.·2018·Journal of Cell Science
DOI 10.1242/jcs.217398PMC PMC6031384
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Abstract

The retromer complex is a vital component of the endosomal protein sorting machinery necessary for sorting into both the endosome-to-Golgi retrieval pathway and also the endosome-to-cell-surface recycling pathway. Retromer mediates cargo selection through a trimeric complex comprising VPS35, VPS29 and VPS26, which is recruited to endosomes by binding to Rab7a and Snx3. Retromer function is linked to two distinct neurodegenerative diseases, Parkinson's disease and Alzheimer's disease and modulating retromer function has been proposed as an avenue to explore for a putative therapy in these conditions. We hypothesised that activating Rab7a to promote the recruitment of retromer to endosomes could positively modulate its activity. Here, we show that inhibition of the GTPase activating protein TBC1D5 can enhance Rab7a activation and lead to a gain of function for retromer.

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  • The Retromer sub-domain proximity proteome included the RAB7 GAP TBC1D5, the RAB21/RAB32/RAB38 GEF VARP, and the RAB10 GEFs DENND4A and DENND4C.

    “These included known Retromer accessory proteins, the RAB7 GAP TBC1D546,77–81, the RAB21/RAB32/RAB38 GEF VARP (a.k.a. ANKRD27)47,48,82, and the RAB10 GEFs DENND4A and DENND4C83,84.”

    From Mapping of endosomal proximity proteomes reveals Retromer as a hub for RAB GTPase regulation (2025) · cites this paper as [79]

  • In the absence of retromer, RAB7 loses its dynamic organisation on endosomes and lysosomes and becomes hyperactivated and immobile on lysosomes.

    “In the absence of retromer, RAB7 loses its dynamic organisation on endosomes and lysosomes and becomes hyperactivated and immobile on lysosomes (Jimenez-Orgaz et al., 2018; Seaman et al., 2018).”

    From Acute inactivation of retromer and ESCPE-1 leads to time-resolved defects in endosomal cargo sorting (2020) · cites this paper as Seaman et al., 2018

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Metadata

Authors
Seaman, M. N. J., Mukadam, A. S., & Breusegem, S. Y.
Affiliations
Department of Clinical Biochemistry , ,   Addenbrookes Biomedical Campus, Cambridge, CB2 0XY , UK
ORCID
Seaman, Matthew N. J.
Venue
Journal of Cell Science
Publisher
The Company of Biologists
Published
2018-06-15
Volume
131
Issue
12
ISSN
  • 1477-9137
  • 0021-9533
DOI
10.1242/jcs.217398
PMC
PMC6031384
Cited by
79
References
2
Language
en
Licence
creativecommons.org/licenses/by/3.0 (vor, 811 d)
Funders
  • Medical Research Council (MR/L007533/1)
  • Wellcome Trust

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