The long life of an endocytic patch that misses AP-2

León, Nagore de; Valdivieso, M.‐Henar

doi:10.1007/s00294-016-0605-3

Cited by 7 publications

(5 citation statements)

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“…dpy-23 is the μ-2 adaptin member of the AP2 complex and is required for the clathrin-dependent endocytosis of various transmembrane receptors [22, 49–51]. Loss of dpy-23 by RNAi leads to the suppression of clathrin-mediated endocytosis, resulting in accumulation of SMA-6 at the plasma membrane and inhibition of BMP signaling [22].…”

Section: Resultsmentioning

confidence: 99%

C. elegans SMA-10 regulates BMP receptor trafficking

et al. 2017

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Signal transduction of the conserved transforming growth factor-β (TGFβ) family signaling pathway functions through two distinct serine/threonine transmembrane receptors, the type I and type II receptors. Endocytosis orchestrates the assembly of signaling complexes by coordinating the entry of receptors with their downstream signaling mediators. Recently, we showed that the C. elegans type I bone morphogenetic protein (BMP) receptor SMA-6, part of the TGFβ family, is recycled through the retromer complex while the type II receptor, DAF-4 is recycled in a retromer-independent, ARF-6 dependent manner. From genetic screens in C. elegans aimed at identifying new modifiers of BMP signaling, we reported on SMA-10, a conserved LRIG (leucine-rich and immunoglobulin-like domains) transmembrane protein. It is a positive regulator of BMP signaling that binds to the SMA-6 receptor. Here we show that the loss of sma-10 leads to aberrant endocytic trafficking of SMA-6, resulting in its accumulation in distinct intracellular endosomes including the early endosome, multivesicular bodies (MVB), and the late endosome with a reduction in signaling strength. Our studies show that trafficking defects caused by the loss of sma-10 are not universal, but affect only a limited set of receptors. Likewise, in Drosophila, we find that the fly homolog of sma-10, lambik (lbk), reduces signaling strength of the BMP pathway, consistent with its function in C. elegans and suggesting evolutionary conservation of function. Loss of sma-10 results in reduced ubiquitination of the type I receptor SMA-6, suggesting a possible mechanism for its regulation of BMP signaling.

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Section: Resultsmentioning

confidence: 99%

C. elegans SMA-10 regulates BMP receptor trafficking

et al. 2017

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“…The transcription factor AP-2 Gamma (TFAP2C) is a member of the activating protein 2 (AP-2) family [63]. Some studies demonstrate that TFAP2C can increase the accumulation of cellular YAP in the nucleus by inactivating MST1/2 [42,64].…”

Section: A Multitude Of Molecules Regulate Apoptosis and Hippo-yapmentioning

confidence: 99%

The Ambivalent Function of YAP in Apoptosis and Cancer

Zhang

Abdelrahman

Vollmar

et al. 2018

IJMS

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Yes-associated protein, a core regulator of the Hippo-YAP signaling pathway, plays a vital role in inhibiting apoptosis. Thus, several studies and reviews suggest that yes-associated protein is a good target for treating cancer. Unfortunately, more and more evidence demonstrates that this protein is also an essential contributor of p73-mediated apoptosis. This questions the concept that yes-associated protein is always a good target for developing novel anti-cancer drugs. Thus, the aim of this review was to evaluate the clinical relevance of yes-associated protein for cancer pathophysiology. This review also summarized the molecules, processes and drugs, which regulate Hippo-YAP signaling and discusses their effect on apoptosis. In addition, issues are defined, which should be addressed in the future in order to provide a solid basis for targeting the Hippo-YAP signaling pathway in clinical trials.

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“…The cargo adaptor protein AP-2 complex is a heterotetrameric endocytic cargo-binding adaptor consisting of four subunits (α, β, μ, and σ) ( 34 ). In yeast, the AP-2 complex is required for vegetative growth and polarized cell responses, and the subunit α (Apl3p) played important roles in dynamics of endocytic sites, morphogenesis, and cell wall integrity ( 35 – 38 ). In Candida albicans , deletion of AP-2 complex subunits resulted in defects in hyphal growth, polarized morphogenesis, and cell wall organization ( 36 , 39 ).…”

Section: Introductionmentioning

confidence: 99%