Coordinated regulation of AP2 uncoating from clathrin-coated vesicles by rab5 and hRME-6

Semerdjieva, Sophia; Shortt, B. J.; Maxwell, Emma; Singh, Sukhdeep; Fonarev, Paul; Hansen, Jonathan J.; Schiavo, Giampietro; Grant, Barth D.; Smythe, Elizabeth

doi:10.1083/jcb.200806016

Cited by 113 publications

(109 citation statements)

References 62 publications

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“…It is possible that AP-2 contacts exomer at endosomes. A requirement for this hypothesis would be that the coated vesicle reaches the endosome and that vesicle uncoating is a sequential process (Trahey and Hay 2010;Semerdjieva 2008) so that clathrin is released from the coat before AP-2 contacts exomer. This hypothesis would be in agreement with the observation that Cfr1 interacts physically with clathrin adaptors but not with clathrin, suggesting that the interaction might take place before clathrin incorporates to the coats or after it dissociates from them.…”

Section: Discussionmentioning

confidence: 99%

Traffic Through the Trans-Golgi Network and the Endosomal System Requires Collaboration Between Exomer and Clathrin Adaptors in Fission Yeast

et al. 2017

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Despite its biological and medical relevance, traffic from the Golgi to the plasma membrane (PM) is one of the least understood steps of secretion. Exomer is a protein complex that mediates the trafficking of certain cargoes from the trans-Golgi network/early endosomes to the PM in budding yeast. Here, we show that in Schizosaccharomyces pombe the Cfr1 and Bch1 proteins constitute the simplest form of an exomer. Cfr1 co-immunoprecipitates with Assembly Polypeptide adaptor 1 (AP-1), AP-2, and Golgi-localized, gamma-adaptin ear domain homology, ARF-binding (GGA) subunits, and cfr1 + interacts genetically with AP-1 and GGA genes. Exomer-defective cells exhibit multiple mild defects, including alterations in the morphology of Golgi stacks and the distribution of the synaptobrevin-like Syb1 protein, carboxypeptidase missorting, and stress sensitivity. S. pombe apm1D cells exhibit a defect in trafficking through the early endosomes that is severely aggravated in the absence of exomer. apm1D cfr1D cells exhibit a dramatic disorganization of intracellular compartments, including massive accumulation of electron-dense tubulovesicular structures. While the trans-Golgi network/early endosomes are severely disorganized in the apm1D cfr1D strain, gga21D gga22D cfr1D cells exhibit a significant disturbance of the prevacuolar/vacuolar compartments. Our findings show that exomer collaborates with clathrin adaptors in trafficking through diverse cellular compartments, and that this collaboration is important to maintain their integrity. These results indicate that the effect of eliminating exomer is more pervasive than that described to date, and suggest that exomer complexes might participate in diverse steps of vesicle transport in other organisms.

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Section: Discussionmentioning

confidence: 99%

Traffic Through the Trans-Golgi Network and the Endosomal System Requires Collaboration Between Exomer and Clathrin Adaptors in Fission Yeast

et al. 2017

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“…AP-2 is released from endocytic vesicles by a combination of factors, including a decrease in the level of PIP 2 and dephosphorylation of m2 on endosomes 35,36 . When AP-2 is released, the CT2 region of STG becomes available for AP-3A binding on the early endosome.…”

Section: Discussionmentioning

confidence: 99%

Stargazin regulates AMPA receptor trafficking through adaptor protein complexes during long-term depression

et al. 2013

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Long-term depression (LTD) underlies learning and memory in various brain regions. Although postsynaptic AMPA receptor trafficking mediates LTD, its underlying molecular mechanisms remain largely unclear. Here we show that stargazin, a transmembrane AMPA receptor regulatory protein, forms a ternary complex with adaptor proteins AP-2 and AP-3A in hippocampal neurons, depending on its phosphorylation state. Inhibiting the stargazin-AP-2 interaction disrupts NMDA-induced AMPA receptor endocytosis, and inhibiting that of stargazin-AP-3A abrogates the late endosomal/lysosomal trafficking of AMPA receptors, thereby upregulating receptor recycling to the cell surface. Similarly, stargazin's interaction with AP-2 or AP-3A is necessary for low-frequency stimulus-evoked LTD in CA1 hippocampal neurons. Thus, stargazin has a crucial role in NMDA-dependent LTD by regulating two trafficking pathways of AMPA receptors-transport from the cell surface to early endosomes and from early endosomes to late endosomes/lysosomes-through its sequential binding to AP-2 and AP-3A.

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“…Other recent evidence suggests that Rab GAPs and guanine exchange factors (GEFs) might not only target different Rab proteins, but also associate with components of the early endocytic pathway, such as the clathrin adapter complex, to control unique traffi cking pathways (Fuchs et al, 2007;Semerdjieva et al, 2008;Lanzetti et al, 2000;Barr & Lambright, 2010;Marat & McPherson, 2010). These recent fi ndings support the possibility that the interaction between CIP85, a putative Rab GAP, and clathrin may infl uence the endocytic traffi cking of Cx43.…”

Section: Discussionmentioning

confidence: 82%

The connexin43-interacting protein, CIP85, mediates the internalization of connexin43 from the plasma membrane

Cochrane

Lau

2013

Cell Communication & Adhesion

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CIP85 was previously identifi ed as a connexin43 (Cx43)-interacting protein that is ubiquitously expressed in multiple mammalian tissues and cell types. The interaction between the SH3 domain of CIP85 and a proline-rich region of Cx43 has previously been associated with an increased rate of Cx43 turnover through lysosomal mechanisms. This report presents biochemical and immunofl uorescence evidence that overexpression of CIP85 reduced the presence of Cx43 in gap junction plaques at the plasma membrane. Furthermore, this effect was dependent upon the interaction of CIP85 with Cx43 at the plasma membrane. These results indicate that CIP85 increases Cx43 turnover by accelerating the internalization of Cx43 from the plasma membrane. CIP85 was also observed to interact with clathrin, which suggested a role for CIP85 in the clathrin-mediated internalization of Cx43.

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Coordinated regulation of AP2 uncoating from clathrin-coated vesicles by rab5 and hRME-6

Cited by 113 publications

References 62 publications

Traffic Through the Trans-Golgi Network and the Endosomal System Requires Collaboration Between Exomer and Clathrin Adaptors in Fission Yeast

Traffic Through the Trans-Golgi Network and the Endosomal System Requires Collaboration Between Exomer and Clathrin Adaptors in Fission Yeast

Stargazin regulates AMPA receptor trafficking through adaptor protein complexes during long-term depression

The connexin43-interacting protein, CIP85, mediates the internalization of connexin43 from the plasma membrane

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