Type II Transforming Growth Factor-β Receptor Recycling Is Dependent upon the Clathrin Adaptor Protein Dab2

Penheiter, Sumedha G.; Singh, Ramandeep; Repellin, Claire E.; Wilkes, Mark C.; Edens, Maryanne; Howe, Philip H.; Pagano, Richard E.; Leof, Edward B.

doi:10.1091/mbc.e09-12-1019

Cited by 55 publications

(54 citation statements)

References 60 publications

(120 reference statements)

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“…DAB-1 may also play a role in intracellular clathrin mediated trafficking on the Golgi and/or endosomes. This is suggested by synthetic phenotypes with intracellular clathrin adaptors AP1 and AP2, and reports of disabled family proteins affecting receptor recycling in mammalian cells (Chibalina et al, 2007; PMID 18029400; Fu et al, 2012; PMID 21995445; Holmes et al, 2007; PMID 17636000; Kamikura and Cooper, 2006; PMID 16497226; Penheiter et al, 2010; PMID 20881059; Wang et al, 2008; PMID 18298590).…”

Section: Endocytosis: Screens and Assaysmentioning

confidence: 96%

C. elegans as a model for membrane traffic

et al. 2014

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The counterbalancing action of the endocytosis and secretory pathways maintains a dynamic equilibrium that regulates the composition of the plasma membrane, allowing it to maintain homeostasis and to change rapidly in response to changes in the extracellular environment and/or intracellular metabolism. These pathways are intimately integrated with intercellular signaling systems and play critical roles in all cells. Studies in Caenorhabditis elegans have revealed diverse roles of membrane trafficking in physiology and development and have also provided molecular insight into the fundamental mechanisms that direct cargo sorting, vesicle budding, and membrane fisson and fusion. In this review, we summarize progress in understanding membrane trafficking mechanisms derived from work in C. elegans, focusing mainly on work done in non-neuronal cell-types, especially the germline, early embryo, coelomocytes, and intestine.

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Section: Endocytosis: Screens and Assaysmentioning

confidence: 96%

C. elegans as a model for membrane traffic

et al. 2014

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“…Both internalization and recycling of TGF-b receptors occur in the absence and presence of ligand binding . Recycling of TbRI is promoted by interaction with the adaptor CIN85 and is dependent on Rab11-containing recycling vesicles (Yakymovych et al 2015), and recycling of TbRII is promoted by the adaptor protein DAB2 (Penheiter et al 2010). More- over, there appears to exist an intracellular pool of TGF-b receptors (Wu and Derynck 2009), which can be mobilized to presentation at the cell surface by Akt-induced phosphorylation of the endosomal membrane-associated RabGTPase AS160 (Budi et al 2015).…”

Section: Tgf-b Receptor Regulation By Endocytosismentioning

confidence: 99%

Signaling Receptors for TGF-β Family Members

Heldin

Moustakas

2016

Cold Spring Harb Perspect Biol

519

480

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Transforming growth factor b (TGF-b) family members signal via heterotetrameric complexes of type I and type II dual specificity kinase receptors. The activation and stability of the receptors are controlled by posttranslational modifications, such as phosphorylation, ubiquitylation, sumoylation, and neddylation, as well as by interaction with other proteins at the cell surface and in the cytoplasm. Activation of TGF-b receptors induces signaling via formation of Smad complexes that are translocated to the nucleus where they act as transcription factors, as well as via non-Smad pathways, including the Erk1/2, JNK and p38 MAP kinase pathways, and the Src tyrosine kinase, phosphatidylinositol 3 0 -kinase, and Rho GTPases.

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“…In neurons the retromer is recruited to the receptor by beclin-1, a component of the type III phosphatidylinositol-3-kinase complex [89]. SH2-and SH3-containing adaptor proteins CIN85 and Dab2 promote recycling of TβRI and TβRII, respectively [86,90].…”

Section: Recyclingmentioning

confidence: 99%

Intracellular trafficking of transforming growth factor β receptors

Yakymovych

Heldin

2018

ABBS

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Transforming growth factor β (TGFβ) family members signal via heterotetrameric complexes of type I (TβRI) and type II (TβRII) dual specificity kinase receptors. The availability of the receptors on the cell surface is controlled by several mechanisms. Newly synthesized TβRI and TβRII are delivered from the Golgi apparatus to the cell surface via separate routes. On the cell surface, TGFβ receptors are distributed between different microdomains of the plasma membrane and can be internalized via clathrin-and caveolae-mediated endocytic mechanisms. Although receptor endocytosis is not essential for TGFβ signaling, localization of the activated receptor complexes on the early endosomes promotes TGFβ-induced Smad activation. Caveolae-mediated endocytosis, which is widely regarded as a mechanism that facilitates the degradation of TGFβ receptors, has been shown to be required for TGFβ signaling via non-Smad pathways. The importance of proper control of TGFβ receptor intracellular trafficking is emphasized by clinical data, as mislocalization of receptors has been described in connection with several human diseases. Thus, control of intracellular trafficking of the TGFβ receptors together with the regulation of their expression, posttranslational modifications and down-regulation, ensure proper regulation of TGFβ signaling.

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Type II Transforming Growth Factor-β Receptor Recycling Is Dependent upon the Clathrin Adaptor Protein Dab2

Cited by 55 publications

References 60 publications

C. elegans as a model for membrane traffic

C. elegans as a model for membrane traffic

Signaling Receptors for TGF-β Family Members

Intracellular trafficking of transforming growth factor β receptors

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Type II Transforming Growth Factor-β Receptor Recycling Is Dependent upon the Clathrin Adaptor Protein Dab2

Cited by 55 publications

References 60 publications

C. elegans as a model for membrane traffic

C. elegans as a model for membrane traffic

Signaling Receptors for TGF-β Family Members

Intracellular trafficking of transforming growth factor &beta; receptors

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Intracellular trafficking of transforming growth factor β receptors