Ligand-induced downregulation of TrkA is partly regulated through ubiquitination by Cbl (Q24302303)

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Noriaki Shimokawa

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Saeed Esmaeili-Mahani

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Akihito Morita

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Hiroko Masuda

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Toshiharu Iwasaki

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Jun'ichi Tamura

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Noriyuki Koibuchi

Cell signaling by receptor tyrosine kinases

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language of work or name

English

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publication date

23 June 2011

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published in

FEBS Letters

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volume

585

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issue

12

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page(s)

1741-7

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cites work

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Cell signaling by receptor tyrosine kinases

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Endocytosis of growth factor receptors

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Movement of internalized ligand-receptor complexes along a continuous endosomal reticulum

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Molecular mechanisms underlying endocytosis and sorting of ErbB receptor tyrosine kinases

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Cbl: many adaptations to regulate protein tyrosine kinases

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The endophilin-CIN85-Cbl complex mediates ligand-dependent downregulation of c-Met

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Cbl-CIN85-endophilin complex mediates ligand-induced downregulation of EGF receptors

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The tyrosine kinase regulator Cbl enhances the ubiquitination and degradation of the platelet-derived growth factor receptor alpha

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Cbl-directed monoubiquitination of CIN85 is involved in regulation of ligand-induced degradation of EGF receptors

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Multiple monoubiquitination of RTKs is sufficient for their endocytosis and degradation

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Oncogenic rearrangements of the NTRK1/NGF receptor.

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TrkA receptor endolysosomal degradation is both ubiquitin and proteasome dependent

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A novel mouse Nedd4 protein suppresses the activity of the epithelial Na+ channel

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Phosphorylation of Nedd4-2 by Sgk1 regulates epithelial Na(+) channel cell surface expression

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Identification of the prosurvival activity of nerve growth factor on cardiac myocytes

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CIN85 regulates dopamine receptor endocytosis and governs behaviour in mice

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Nerve growth factor mediates signal transduction through trk homodimer receptors

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TrkA Tyrosine Residues Involved in NGF‐induced Neurite Outgrowth of PC12 Cells

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EGF receptor ubiquitination is not necessary for its internalization

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A tale of two Cbls: interplay of c-Cbl and Cbl-b in epidermal growth factor receptor downregulation

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p75 neurotrophin receptor reduces ligand-induced Trk receptor ubiquitination and delays Trk receptor internalization and degradation

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Low density lipoprotein receptor-related protein 1 (LRP1) controls endocytosis and c-CBL-mediated ubiquitination of the platelet-derived growth factor receptor beta (PDGFR beta).

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c-Cbl binds to tyrosine-phosphorylated neurotrophin receptor p75 and induces its ubiquitination

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Cell Survival through Trk Neurotrophin Receptors Is Differentially Regulated by Ubiquitination

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Proteasome inhibitors block a late step in lysosomal transport of selected membrane but not soluble proteins.

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based on heuristic

Phosphotyrosine binding domain-dependent upregulation of the platelet-derived growth factor receptor alpha signaling cascade by transforming mutants of Cbl: implications for Cbl's function and oncogenicity

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