Forty Years of Clathrin‐coated Vesicles

Robinson, Margaret S.

doi:10.1111/tra.12335

Cited by 307 publications

(322 citation statements)

References 298 publications

(346 reference statements)

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“…Additionally, CLTC is found at endosomes and the trans -Golgi network to facilitate cargo movement from these structures. Cargo molecules are recognized by adaptor protein complexes, such as AP2 (adaptor related protein complex 2), which form a link to CLTC itself, which acts as a scaffold forming a cage-like structure around clathrin-coated vesicles [19]. The Coxiella Dot/Icm effector CvpA has been shown to bind AP2, and is required for both intracellular replication of Coxiella and CLTC recruitment to the CCV [17].…”

Section: Introductionmentioning

confidence: 99%

Interaction between autophagic vesicles and the Coxiella-containing vacuole requires CLTC (clathrin heavy chain)

Latomanski

Newton

2018

Autophagy

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Coxiella burnetii is an intracellular bacterial pathogen which causes Q fever, a human infection with the ability to cause chronic disease with potentially life-threatening outcomes. In humans, Coxiella infects alveolar macrophages where it replicates to high numbers in a unique, pathogen-directed lysosome-derived vacuole. This compartment, termed the Coxiella-containing vacuole (CCV), has a low internal pH and contains markers both of lysosomes and autophagosomes. The CCV membrane is also enriched with CLTC (clathrin heavy chain) and this contributes to the success of the CCV. Here, we describe a role for CLTC, a scaffolding protein of clathrin-coated vesicles, in facilitating the fusion of autophagosomes with the CCV. During gene silencing of CLTC, CCVs are unable to fuse with each other, a phenotype also seen when silencing genes involved in macroautophagy/autophagy. MAP1LC3B/LC3B, which is normally observed inside the CCV, is excluded from CCVs in the absence of CLTC. Additionally, this study demonstrates that autophagosome fusion contributes to CCV size as cell starvation and subsequent autophagy induction leads to further CCV expansion. This is CLTC dependent, as the absence of CLTC renders autophagosomes no longer able to contribute to the expansion of the CCV. This investigation provides a functional link between CLTC and autophagy in the context of Coxiella infection and highlights the CCV as an important tool to explore the interactions between these vesicular trafficking pathways.

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Section: Introductionmentioning

confidence: 99%

Interaction between autophagic vesicles and the Coxiella-containing vacuole requires CLTC (clathrin heavy chain)

Latomanski

Newton

2018

Autophagy

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“…The adaptor proteins (APs) comprise a family of five heterotetrameric complexes in mammals (Bonifacino, 2014;Robinson, 2015). In addition to AP-2, formed by α, β2, μ2 and σ2 subunits (Table S1), two other AP complexes, AP-1 (γ1, β1, μ1 and σ1) and AP-3 (δ, β3, μ3 and σ3), are binding partners of Nef (Bresnahan et al, 1998;Chaudhuri et al, 2007;Coleman et al, 2005;Doray et al, 2007;Greenberg et al, 1998;Janvier et al, 2003a,b;Mattera et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

“…However, the role of the Nef interaction with AP-1 or AP-3 in CD4 downregulation is poorly understood. AP-1 facilitates CCV-mediated trafficking between the trans-Golgi network (TGN) and endosomes, whereas AP-3 participates in the trafficking to lysosomes and lysosome-related organelles, possibly through clathrin-dependent and clathrinindependent pathways (Robinson, 2015). In addition, it is possible that functional variants of the canonical AP-1, AP-2 and AP-3 complexes exist, given that some of their subunits occur as multiple isoforms encoded by different genes (Table S1).…”

Section: Introductionmentioning

confidence: 99%

CD4 downregulation by the HIV-1 protein Nef reveals distinct roles for the γ1 and γ2 subunits of the AP-1 complex in protein trafficking

Tavares

Silva

Silva-Januário

et al. 2017

Journal of Cell Science

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The HIV accessory protein Nef is a major determinant of viral pathogenesis that facilitates viral particle release, prevents viral antigen presentation and increases infectivity of new virus particles. These functions of Nef involve its ability to remove specific host proteins from the surface of infected cells, including the CD4 receptor. Nef binds to the adaptor protein 2 (AP-2) and CD4 in clathrin-coated pits, forcing CD4 internalization and its subsequent targeting to lysosomes. Herein, we report that this lysosomal targeting requires a variant of AP-1 containing isoform 2 of γ-adaptin (AP1G2, hereafter γ2). Depletion of the γ2 or μ1A (AP1M1) subunits of AP-1, but not of γ1 (AP1G1), precludes Nef-mediated lysosomal degradation of CD4. In γ2-depleted cells, CD4 internalized by Nef accumulates in early endosomes and this alleviates CD4 removal from the cell surface. Depletion of γ2 also hinders EGFR-EGF-complex targeting to lysosomes, an effect that is not observed upon γ1 depletion. Taken together, our data provide evidence that the presence of γ1 or γ2 subunits delineates two distinct variants of AP-1 complexes, with different functions in protein sorting.

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“…According to current paradigms, clathrin adaptors are recruited to the appropriate membrane through coincident low-affinity interactions with different targets (3,4). In this process, phosphoinositides function as key membrane-specific determinants.…”

mentioning

confidence: 99%

Conserved role for Gga proteins in phosphatidylinositol 4-kinase localization to the trans -Golgi network

Daboussi

Costaguta

Ghukasyan

et al. 2017

Proc. Natl. Acad. Sci. U.S.A.

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Phosphoinositides serve as key membrane determinants for assembly of clathrin coat proteins that drive formation of clathrin-coated vesicles. At the trans-Golgi network (TGN), phosphatidylinositol 4-phosphate (PtdIns4P) plays important roles in recruitment of two major clathrin adaptors, Gga (Golgi-localized, gamma-adaptin ear homology, Arf-binding) proteins and the AP-1 (assembly protein-1) complex. The molecular mechanisms that mediate localization of phosphatidylinositol kinases responsible for synthesis of PtdIns4P at the TGN are not well characterized. We identify two motifs in the yeast phosphatidylinositol 4-kinase, Pik1, which are required for binding to the VHS domain of Gga2. Mutations in these motifs that inhibit Gga2-VHS binding resulted in reduced Pik1 localization and delayed accumulation of PtdIns4P and recruitment of AP-1 to the TGN. The Pik1 homolog in mammals, PI4KIIIβ, interacted preferentially with the VHS domain of GGA2 compared with VHS domains of GGA1 and GGA3. Depletion of GGA2, but not GGA1 or GGA3, specifically affected PI4KIIIβ localization. These results reveal a conserved role for Gga proteins in regulating phosphatidylinositol 4-kinase function at the TGN.clathrin | Gga adaptors | phosphatidylinositol 4-kinase | phosphatidylinositol 4-phosphate | trans-Golgi network

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Forty Years of Clathrin‐coated Vesicles

Cited by 307 publications

References 298 publications

Interaction between autophagic vesicles and the Coxiella-containing vacuole requires CLTC (clathrin heavy chain)

Interaction between autophagic vesicles and the Coxiella-containing vacuole requires CLTC (clathrin heavy chain)

CD4 downregulation by the HIV-1 protein Nef reveals distinct roles for the γ1 and γ2 subunits of the AP-1 complex in protein trafficking

Conserved role for Gga proteins in phosphatidylinositol 4-kinase localization to the trans -Golgi network

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