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Protein trafficking

How does monoubiquitin turn down Rab5?

Shin D, Na W, Lee JH, et al. · eLife · 2017

Open access · cc by · source: Europe PMC

Rab5 is monoubiquitinated at specific lysines; ubiquitin at K140/K165 disrupts effector binding and downregulates endocytic trafficking.

Study at a glance

Design
Animal / in-vitro — Mapped Rab5 monoubiquitination sites and tested chemically monoubiquitinated Rab5 function
N
Cell-biochemistry of Rab5 ubiquitin sites K116/K140/K165 — no single sample N
Population
Cultured cells expressing Rab5 variants
Outcome
Site-specific monoubiquitination downregulating Rab5 endocytic signaling

Structured fields used in claim comparison tables when every cited study has a complete layer.

Key findings

Rab5 is monoubiquitinated at K116, K140, and K165; K140/K165 modifications downregulate the Rab5 endocytic pathway via disrupted partners and nucleotide conversion, while K116 has little localization effect.

Methodology

Mapped Rab5 monoubiquitination sites in cultured cells, built chemically monoubiquitinated Rab5, and tested structure, nucleotide handling, effector binding, and endosome localization.

Limitations

Does not identify the endogenous E3 ligase or fully map in vivo tissue roles of each site.

How this study connects

Role on claims

Each row is a claim on a concept or method page where this paper supports, challenges, or qualifies the statement. Roles are hand-checked — not a model guess.

  • SupportsProtein traffickingconcept

    Multiple empirical papers in this library examine protein trafficking with mechanistic biological findings.

    Evidence for the claim as stated.

  • SupportsProtein traffickingconcept

    Rab5 is monoubiquitinated at K116, K140, and K165; K140/K165 modifications downregulate the Rab5 endocytic pathway via disrupted partners and nucleotide conversion, while K116 has little localization effect.

    Evidence for the claim as stated.

  • SupportsProtein traffickingconcept

    Systems and scales differ across protein trafficking studies (species, tissues, methods), so mechanisms should not be over-generalised.

    Evidence for the claim as stated.

  • USP8 is required for Hedgehog-induced Smoothened surface accumulation and keeps Smo out of Rab5 early endosomes. Site-specific monoubiquitination of Rab5 at K140 and K165 (not K116) downregulates the endocytic pathway via disrupted effectors and nucleotide conversion. Both papers use localisation of Smo or Rab5 as a trafficking IF readout.

    Evidence for the claim as stated.

  • IF is a screening camera in Vero cells (berzosertib 100 nM, 48 hpi), a tissue census in TB lung (35 patients), a trafficking assay for Smo/Rab5/spike, and a polarity assay in enteroids. 'Positive staining' in a drug screen is not the same claim as PD-1 on human tissue-resident T cells or as K140/K165 moving Rab5 off endosomes.

    Evidence for the claim as stated.

  • Rab5 monoubiquitination sites were mapped at K116, K140 and K165; chemically monoubiquitinated Rab5 then showed that K140/K165 downregulate the endocytic pathway via disrupted effectors and nucleotide conversion, while K116 has little localisation effect. Site-resolved MS (or MS-informed chemistry) here is a modification map, not an identification of the endogenous E3 ligase.

    Evidence for the claim as stated.

  • Genuine MS designs still disagree about what is being counted. APEX2 inventories membrane-face neighbours in living cells (22 OMM; 72 ERM); caveolar work quantifies a purified coat; Rab5 work maps three ubiquitin lysines; rice work maps histone acylations under stress. A 'proteomics paper' can be spatial, stoichiometric, or epigenetic, and those outputs are not interchangeable.

    Evidence for the claim as stated.

Open questions

Tensions this paper is part of

From concept pages' “where studies disagree.” Disagreement means the same question; scope means different assays, populations, or outcomes.

Related papers in this topic

Same topic cluster — not a recommendation engine.