EGF-dependent re-routing of vesicular recycling switches spontaneous phosphorylation suppression to EGFR signaling

Baumdick, Martin; Brüggemann, Yannick; Schmick, Malte; Xouri, Georgia; Sabet, Ola; Davis, Lloyd; Chin, Jason W.; Bastiaens, Philippe I. H.

doi:10.7554/elife.12223

Cited by 63 publications

(98 citation statements)

References 66 publications

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“…SHP2 has been reported to promote breast cancer and liver cancer progression by triggering several biological processes such as cell proliferation and migration . Interestingly, a recent study emphasizes the role of phosphatases in cellular trafficking and rerouting of RTKs . In our study, SHP2 promoted PDGFRα trafficking through EVs.…”

Section: Discussionsupporting

confidence: 63%

Hepatic stellate cell–derived platelet‐derived growth factor receptor‐alpha‐enriched extracellular vesicles promote liver fibrosis in mice through SHP2

Kostallari¹,

Hirsova²,

Prašnická³

et al. 2018

Hepatology

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Section: Discussionsupporting

confidence: 63%

Hepatic stellate cell–derived platelet‐derived growth factor receptor‐alpha‐enriched extracellular vesicles promote liver fibrosis in mice through SHP2

Kostallari¹,

Hirsova²,

Prašnická³

et al. 2018

Hepatology

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“…Combining FLAP with FRAP, we extracted the exchange rates that give rise to the steady-state partitioning of Src on the RE. Modelling Src partitioning with two compartments (Src on the RE vs. the PM and the communicating cytoplasm), photophysical perturbation (FRAP or FLAP) of Src at the RE re-equilibrates in a single-exponential decay towards the steady-state partitioning determined by the ratio: k on /( k on + k off ) 36 . By adding a diffusible fraction, the data can be fit with R 2 adj > 0.99 (Fig.…”

Section: Resultsmentioning

confidence: 99%

Spatial cycles mediated by UNC119 solubilisation maintain Src family kinases plasma membrane localisation

et al. 2017

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The peripheral membrane proto-oncogene Src family protein tyrosine kinases relay growth factor signals to the cytoplasm of mammalian cells. We unravel the spatial cycles of solubilisation, trapping on perinuclear membrane compartments and vesicular transport that counter entropic equilibration to endomembranes for maintaining the enrichment and activity of Src family protein tyrosine kinases at the plasma membrane. The solubilising factor UNC119 sequesters myristoylated Src family protein tyrosine kinases from the cytoplasm, enhancing their diffusion to effectively release Src family protein tyrosine kinases on the recycling endosome by localised Arl2/3 activity. Src is then trapped on the recycling endosome via electrostatic interactions, whereas Fyn is quickly released to be kinetically trapped on the Golgi by palmitoyl acyl-transferase activity. Vesicular trafficking from these compartments restores enrichment of the Src family protein tyrosine kinases to the plasma membrane. Interference with these spatial cycles by UNC119 knockdown disrupts Src family protein tyrosine kinase localisation and signalling activity, indicating that UNC119 could be a drug target to affect oncogenic Src family protein tyrosine kinase signalling.

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“…In contrast, the soma surface-derived receptors that are un-liganded are susceptible to PTP1B-mediated dephosphorylation. Previously, PTP1B has been shown to distinguish between basally versus ligand-bound phosphorylated EGFRs (Baumdick et al, 2015). …”

Section: Discussionmentioning

confidence: 99%

Phospho-Regulation of Soma-to-Axon Transcytosis of Neurotrophin Receptors

et al. 2017

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Summary Axonal targeting of signaling receptors is essential for neuronal responses to extracellular cues. Here, we report that retrograde signaling by target-derived Nerve Growth Factor (NGF) is necessary for soma-to-axon transcytosis of TrkA receptors in sympathetic neurons, and define the molecular underpinnings of this positive feedback regulation that enhances neuronal sensitivity to trophic factors. Activated TrkA receptors are retrogradely transported in signaling endosomes from distal axons to cell bodies, where they are inserted on soma surfaces and promote phosphorylation of resident naive receptors resulting in their internalization. Endocytosed TrkA receptors are then dephosphorylated by PTP1B, an ER-resident protein tyrosine phosphatase, prior to axonal transport. PTP1B inactivation prevents TrkA exit from soma and causes receptor degradation, suggesting a “gate-keeper” mechanism that ensures targeting of inactive receptors to axons to engage with ligand. In mice, PTP1B deletion reduces axonal TrkA levels and attenuates neuron survival and target innervation under limiting NGF (NGF+/−) conditions.

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EGF-dependent re-routing of vesicular recycling switches spontaneous phosphorylation suppression to EGFR signaling

Cited by 63 publications

References 66 publications

Hepatic stellate cell–derived platelet‐derived growth factor receptor‐alpha‐enriched extracellular vesicles promote liver fibrosis in mice through SHP2

Hepatic stellate cell–derived platelet‐derived growth factor receptor‐alpha‐enriched extracellular vesicles promote liver fibrosis in mice through SHP2

Spatial cycles mediated by UNC119 solubilisation maintain Src family kinases plasma membrane localisation

Phospho-Regulation of Soma-to-Axon Transcytosis of Neurotrophin Receptors

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