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Journal articles on the topic 'AP-1 adaptor complex'

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Published: 15 June 2024

Last updated: 31 July 2025

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1

Yeung, Bonny G., Huan L. Phan, and Gregory S. Payne. "Adaptor Complex-independent Clathrin Function in Yeast." Molecular Biology of the Cell 10, no. 11 (1999): 3643–59. http://dx.doi.org/10.1091/mbc.10.11.3643.

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Clathrin-associated adaptor protein (AP) complexes are major structural components of clathrin-coated vesicles, functioning in clathrin coat assembly and cargo selection. We have carried out a systematic biochemical and genetic characterization of AP complexes inSaccharomyces cerevisiae. Using coimmunoprecipitation, the subunit composition of two complexes, AP-1 and AP-2R, has been defined. These results allow assignment of the 13 potential AP subunits encoded in the yeast genome to three AP complexes. As assessed by in vitro binding assays and coimmunoprecipitation, only AP-1 interacts with c

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2

Salazar, G., B. Craige, M. L. Styers, et al. "BLOC-1 Complex Deficiency Alters the Targeting of Adaptor Protein Complex-3 Cargoes." Molecular Biology of the Cell 17, no. 9 (2006): 4014–26. http://dx.doi.org/10.1091/mbc.e06-02-0103.

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Mutational analyses have revealed many genes that are required for proper biogenesis of lysosomes and lysosome-related organelles. The proteins encoded by these genes assemble into five distinct complexes (AP-3, BLOC-1-3, and HOPS) that either sort membrane proteins or interact with SNAREs. Several of these seemingly distinct complexes cause similar phenotypic defects when they are rendered defective by mutation, but the underlying cellular mechanism is not understood. Here, we show that the BLOC-1 complex resides on microvesicles that also contain AP-3 subunits and membrane proteins that are

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3

Tong, Xiao, Werner Boll, Tomas Kirchhausen, and Peter M. Howley. "Interaction of the Bovine Papillomavirus E6 Protein with the Clathrin Adaptor Complex AP-1." Journal of Virology 72, no. 1 (1998): 476–82. http://dx.doi.org/10.1128/jvi.72.1.476-482.1998.

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ABSTRACT The E6 gene of the bovine papillomavirus type 1 (BPV-1) is expressed in fibropapillomas caused by BPV-1 and in tissue culture cells transformed by BPV-1. It encodes one of the two major oncoproteins of BPV-1. In this study, we demonstrate an interaction between the BPV-1 E6 protein and AP-1, the TGN (trans-Golgi network)-specific clathrin adaptor complex. AP-1 is a four-subunit protein complex required for clathrin-mediated cellular transport from the TGN. The AP-1/E6 interaction was observed in vitro and in cells. The E6 binding site on AP-1 was mapped to the N-terminal trunk domain

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4

Peden, Andrew A., Viola Oorschot, Boris A. Hesser, Cary D. Austin, Richard H. Scheller, and Judith Klumperman. "Localization of the AP-3 adaptor complex defines a novel endosomal exit site for lysosomal membrane proteins." Journal of Cell Biology 164, no. 7 (2004): 1065–76. http://dx.doi.org/10.1083/jcb.200311064.

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The adaptor protein (AP) 3 adaptor complex has been implicated in the transport of lysosomal membrane proteins, but its precise site of action has remained controversial. Here, we show by immuno-electron microscopy that AP-3 is associated with budding profiles evolving from a tubular endosomal compartment that also exhibits budding profiles positive for AP-1. AP-3 colocalizes with clathrin, but to a lesser extent than does AP-1. The AP-3– and AP-1–bearing tubular compartments contain endocytosed transferrin, transferrin receptor, asialoglycoprotein receptor, and low amounts of the cation-indep

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5

Camus, Grégory, Carolina Segura-Morales, Dorothee Molle, et al. "The Clathrin Adaptor Complex AP-1 Binds HIV-1 and MLV Gag and Facilitates Their Budding." Molecular Biology of the Cell 18, no. 8 (2007): 3193–203. http://dx.doi.org/10.1091/mbc.e06-12-1147.

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Retroviral assembly is driven by Gag, and nascent viral particles escape cells by recruiting the machinery that forms intralumenal vesicles of multivesicular bodies. In this study, we show that the clathrin adaptor complex AP-1 is involved in retroviral release. The absence of AP-1μ obtained by genetic knock-out or by RNA interference reduces budding of murine leukemia virus (MLV) and HIV-1, leading to a delay of viral propagation in cell culture. In contrast, overexpression of AP-1μ enhances release of HIV-1 Gag. We show that the AP-1 complex facilitates retroviral budding through a direct in

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6

Lefkir, Yaya, Marilyne Malbouyres, Daniel Gotthardt, et al. "Involvement of the AP-1 Adaptor Complex in Early Steps of Phagocytosis and Macropinocytosis." Molecular Biology of the Cell 15, no. 2 (2004): 861–69. http://dx.doi.org/10.1091/mbc.e03-06-0365.

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The best described function of the adaptor complex-1 (AP-1) is to participate in the budding of clathrin-coated vesicles from the trans-Golgi network and endosomes. Here, we show that AP-1 is also localized to phagocytic cups in murine macrophages as well as in Dictyostelium amoebae. AP-1 is recruited to phagosomal membranes at this early stage of phagosome formation and rapidly dissociates from maturing phagosomes. To establish the role of AP-1 in phagocytosis, we made used of Dictyostelium mutant cells (apm1-cells) disrupted for AP-1 medium chain. In this mutant, phagocytosis drops by 60%, i

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Zlatic, Stephanie A., Emily J. Grossniklaus, Pearl V. Ryder, et al. "Chemical-genetic disruption of clathrin function spares adaptor complex 3–dependent endosome vesicle biogenesis." Molecular Biology of the Cell 24, no. 15 (2013): 2378–88. http://dx.doi.org/10.1091/mbc.e12-12-0860.

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A role for clathrin in AP-3–dependent vesicle biogenesis has been inferred from biochemical interactions and colocalization between this adaptor and clathrin. The functionality of these molecular associations, however, is controversial. We comprehensively explore the role of clathrin in AP-3–dependent vesicle budding, using rapid chemical-genetic perturbation of clathrin function with a clathrin light chain–FKBP chimera oligomerizable by the drug AP20187. We find that AP-3 interacts and colocalizes with endogenous and recombinant FKBP chimeric clathrin polypeptides in PC12-cell endosomes. AP-3

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8

Bonifacino, Juan S. "Adaptor proteins involved in polarized sorting." Journal of Cell Biology 204, no. 1 (2014): 7–17. http://dx.doi.org/10.1083/jcb.201310021.

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Polarized cells such as epithelial cells and neurons exhibit different plasma membrane domains with distinct protein compositions. Recent studies have shown that sorting of transmembrane proteins to the basolateral domain of epithelial cells and the somatodendritic domain of neurons is mediated by recognition of signals in the cytosolic domains of the proteins by adaptors. These adaptors are components of protein coats associated with the trans-Golgi network and/or recycling endosomes. The clathrin-associated adaptor protein 1 (AP-1) complex plays a preeminent role in this process, although ot

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Traub, L. M., J. A. Ostrom, and S. Kornfeld. "Biochemical dissection of AP-1 recruitment onto Golgi membranes." Journal of Cell Biology 123, no. 3 (1993): 561–73. http://dx.doi.org/10.1083/jcb.123.3.561.

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Recruitment of the Golgi-specific AP-1 adaptor complex onto Golgi membranes is thought to be a prerequisite for clathrin coat assembly on the TGN. We have used an in vitro assay to examine the translocation of cytosolic AP-1 onto purified Golgi membranes. Association of AP-1 with the membranes required GTP or GTP analogues and was inhibited by the fungal metabolite, brefeldin A. In the presence of GTP gamma S, binding of AP-1 to Golgi membranes was strictly dependent on the concentration of cytosol added to the assay. AP-1 recruitment was also found to be temperature dependent, and relatively

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10

Duncan, Mara Colleen. "Regulation of clathrin adaptor protein complex‐1(AP‐1) by a Laa1 protein containing complex." FASEB Journal 34, S1 (2020): 1. http://dx.doi.org/10.1096/fasebj.2020.34.s1.00639.

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11

Fölsch, Heike, Marc Pypaert, Peter Schu, and Ira Mellman. "Distribution and Function of Ap-1 Clathrin Adaptor Complexes in Polarized Epithelial Cells." Journal of Cell Biology 152, no. 3 (2001): 595–606. http://dx.doi.org/10.1083/jcb.152.3.595.

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Expression of the epithelial cell–specific heterotetrameric adaptor complex AP-1B is required for the polarized distribution of many membrane proteins to the basolateral surface of LLC-PK1 kidney cells. AP-1B is distinguished from the ubiquitously expressed AP-1A by exchange of its single 50-kD μ subunit, μ1A, being replaced by the closely related μ1B. Here we show that this substitution is sufficient to couple basolateral plasma membrane proteins, such as a low-density lipoprotein receptor (LDLR), to the AP-1B complex and to clathrin. The interaction between LDLR and AP-1B is likely to occur

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12

Okamoto, Curtis T., та Young Y. Jeng. "An immunologically distinct β-adaptin on tubulovesicles of gastric oxyntic cells". American Journal of Physiology-Cell Physiology 275, № 5 (1998): C1323—C1329. http://dx.doi.org/10.1152/ajpcell.1998.275.5.c1323.

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Clathrin and the γ-adaptin subunit of the AP-1 clathrin adaptor have been previously identified on H-K-ATPase-rich tubulovesicles from gastric acid secretory (oxyntic) cells [C. T. Okamoto, S. M. Karam, Y. Y. Jeng, J. G. Forte, and J. Goldenring. Am. J. Physiol. 274 ( Cell Physiol. 43): C1017–C1029]. We further characterized this AP-1 adaptor from rabbit and hog tubulovesicles biochemically and immunologically. Clathrin coat proteins were stripped from purified tubulovesicular membranes and fractionated by hydroxyapatite chromatography. The AP-1 adaptor appears to elute at 200 mM sodium phosph

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13

Craige, Branch, Gloria Salazar, and Victor Faundez. "Phosphatidylinositol-4-Kinase Type II Alpha Contains an AP-3–sorting Motif and a Kinase Domain That Are Both Required for Endosome Traffic." Molecular Biology of the Cell 19, no. 4 (2008): 1415–26. http://dx.doi.org/10.1091/mbc.e07-12-1239.

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The adaptor complex 3 (AP-3) targets membrane proteins from endosomes to lysosomes, lysosome-related organelles and synaptic vesicles. Phosphatidylinositol-4-kinase type II α (PI4KIIα) is one of several proteins possessing catalytic domains that regulate AP-3–dependent sorting. Here we present evidence that PI4KIIα uniquely behaves both as a membrane protein cargo as well as an enzymatic regulator of adaptor function. In fact, AP-3 and PI4KIIα form a complex that requires a dileucine-sorting motif present in PI4KIIα. Mutagenesis of either the PI4KIIα-sorting motif or its kinase-active site ind

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14

Čopič, Alenka, Trevor L. Starr, and Randy Schekman. "Ent3p and Ent5p Exhibit Cargo-specific Functions in Trafficking Proteins between the Trans-Golgi Network and the Endosomes in Yeast." Molecular Biology of the Cell 18, no. 5 (2007): 1803–15. http://dx.doi.org/10.1091/mbc.e06-11-1000.

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The phosphoinositide-binding proteins Ent3p and Ent5p are required for protein transport from the trans-Golgi network (TGN) to the vacuole in Saccharomyces cerevisiae. Both proteins interact with the monomeric clathrin adaptor Gga2p, but Ent5p also interacts with the clathrin adaptor protein 1 (AP-1) complex, which facilitates retention of proteins such as Chs3p at the TGN. When both ENT3 and ENT5 are mutated, Chs3p is diverted from an intracellular reservoir to the cell surface. However, Ent3p and Ent5p are not required for the function of AP-1, but rather they seem to act in parallel with AP

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15

Prandini, Alberto, Valentina Salvi, Francesca Colombo, et al. "Impairment of dendritic cell functions in patients with adaptor protein-3 complex deficiency." Blood 127, no. 26 (2016): 3382–86. http://dx.doi.org/10.1182/blood-2015-06-650689.

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16

Zhu, Yunxiang, Linton M. Traub, and Stuart Kornfeld. "ADP-Ribosylation Factor 1 Transiently Activates High-Affinity Adaptor Protein Complex AP-1 Binding Sites On Golgi Membranes." Molecular Biology of the Cell 9, no. 6 (1998): 1323–37. http://dx.doi.org/10.1091/mbc.9.6.1323.

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Association of the Golgi-specific adaptor protein complex 1 (AP-1) with the membrane is a prerequisite for clathrin coat assembly on the trans-Golgi network (TGN). The AP-1 adaptor is efficiently recruited from cytosol onto the TGN by myristoylated ADP-ribosylation factor 1 (ARF1) in the presence of the poorly hydrolyzable GTP analog guanosine 5′-O-(3-thiotriphosphate) (GTPγS). Substituting GTP for GTPγS, however, results in only poor AP-1 binding. Here we show that both AP-1 and clathrin can be recruited efficiently onto the TGN in the presence of GTP when cytosol is supplemented with ARF1. O

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17

Ooi, Chean Eng, Esteban C. Dell'Angelica, and Juan S. Bonifacino. "ADP-Ribosylation Factor 1 (ARF1) Regulates Recruitment of the AP-3 Adaptor Complex to Membranes." Journal of Cell Biology 142, no. 2 (1998): 391–402. http://dx.doi.org/10.1083/jcb.142.2.391.

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Small GTP-binding proteins such as ADP- ribosylation factor 1 (ARF1) and Sar1p regulate the membrane association of coat proteins involved in intracellular membrane trafficking. ARF1 controls the clathrin coat adaptor AP-1 and the nonclathrin coat COPI, whereas Sar1p controls the nonclathrin coat COPII. In this study, we demonstrate that membrane association of the recently described AP-3 adaptor is regulated by ARF1. Association of AP-3 with membranes in vitro was enhanced by GTPγS and inhibited by brefeldin A (BFA), an inhibitor of ARF1 guanine nucleotide exchange. In addition, recombinant m

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18

Sorkina, T., A. Bild, F. Tebar, and A. Sorkin. "Clathrin, adaptors and eps15 in endosomes containing activated epidermal growth factor receptors." Journal of Cell Science 112, no. 3 (1999): 317–27. http://dx.doi.org/10.1242/jcs.112.3.317.

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Activation of the epidermal growth factor receptor (EGFR) by EGF results in binding of clathrin adaptor protein complex AP-2 to the receptor cytoplasmic tail. The transient interaction with AP-2 is thought to be responsible for the selective recruitment of the EGFR into coated pits during endocytosis. In this study we found that EGF-induced EGFR/AP-2 association, measured by co-immunoprecipitation, persists after receptor internalization. Double-label immunofluorescence of EGF-treated A-431 and COS-1 cells revealed the presence of AP-2, clathrin and eps15, another component of the plasma membr

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BAROIS, Nicolas, and Oddmund BAKKE. "The adaptor protein AP-4 as a component of the clathrin coat machinery: a morphological study." Biochemical Journal 385, no. 2 (2005): 503–10. http://dx.doi.org/10.1042/bj20041010.

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The four members of the AP (adaptor protein) family are heterotetrameric cytosolic complexes that are involved in the intracellular trafficking of cargo proteins between different organelles. They interact with motifs present in the cytoplasmic tails of their specific cargo proteins at different intracellular locations. While AP-1, AP-2 and AP-3 have been investigated extensively, very few studies have focused on the fourth member, AP-4. In the present study, we report on the intracellular localization of AP-4 in the MDCK (Madin–Darby canine kidney) and MelJuSo cell lines after immunogold labe

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Zhu, Yunxiang, Linton M. Traub, and Stuart Kornfeld. "High-Affinity Binding Of The AP-1 Adaptor Complex to Trans-Golgi Network Membranes Devoid Of Mannose 6-Phosphate Receptors." Molecular Biology of the Cell 10, no. 3 (1999): 537–49. http://dx.doi.org/10.1091/mbc.10.3.537.

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The GTP-binding protein ADP-ribosylation factor (ARF) initiates clathrin-coat assembly at the trans-Goli network (TGN) by generating high-affinity membrane-binding sites for the AP-1 adaptor complex. Both transmembrane proteins, which are sorted into the assembling coated bud, and novel docking proteins have been suggested to be partners with GTP-bound ARF in generating the AP-1-docking sites. The best characterized, and probably the major transmembrane molecules sorted into the clathrin-coated vesicles that form on the TGN, are the mannose 6-phosphate receptors (MPRs). Here, we have examined

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Ghosh, Pradipta, and Stuart Kornfeld. "AP-1 binding to sorting signals and release from clathrin-coated vesicles is regulated by phosphorylation." Journal of Cell Biology 160, no. 5 (2003): 699–708. http://dx.doi.org/10.1083/jcb.200211080.

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The adaptor protein complex-1 (AP-1) sorts and packages membrane proteins into clathrin-coated vesicles (CCVs) at the TGN and endosomes. Here we show that this process is highly regulated by phosphorylation of AP-1 subunits. Cell fractionation studies revealed that membrane-associated AP-1 differs from cytosolic AP-1 in the phosphorylation status of its β1 and μ1 subunits. AP-1 recruitment onto the membrane is associated with protein phosphatase 2A (PP2A)–mediated dephosphorylation of its β1 subunit, which enables clathrin assembly. This Golgi-associated isoform of PP2A exhibits specificity fo

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Scheele, Urte, Christoph Kalthoff, and Ernst Ungewickell. "Multiple Interactions of Auxilin 1 with Clathrin and the AP-2 Adaptor Complex." Journal of Biological Chemistry 276, no. 39 (2001): 36131–38. http://dx.doi.org/10.1074/jbc.m106511200.

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Sawasdee, Nunghathai, Mutita Junking, Piengpaga Ngaojanlar та ін. "Human kidney anion exchanger 1 interacts with adaptor-related protein complex 1 μ1A (AP-1 mu1A)". Biochemical and Biophysical Research Communications 401, № 1 (2010): 85–91. http://dx.doi.org/10.1016/j.bbrc.2010.09.015.

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Fölsch, Heike, Marc Pypaert, Sandra Maday, Laurence Pelletier, and Ira Mellman. "The AP-1A and AP-1B clathrin adaptor complexes define biochemically and functionally distinct membrane domains." Journal of Cell Biology 163, no. 2 (2003): 351–62. http://dx.doi.org/10.1083/jcb.200309020.

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Most epithelial cells contain two AP-1 clathrin adaptor complexes. AP-1A is ubiquitously expressed and involved in transport between the TGN and endosomes. AP-1B is expressed only in epithelia and mediates the polarized targeting of membrane proteins to the basolateral surface. Both AP-1 complexes are heterotetramers and differ only in their 50-kD μ1A or μ1B subunits. Here, we show that AP-1A and AP-1B, together with their respective cargoes, define physically and functionally distinct membrane domains in the perinuclear region. Expression of AP-1B (but not AP-1A) enhanced the recruitment of a

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Newell-Litwa, Karen, Gloria Salazar, Yoland Smith, and Victor Faundez. "Roles of BLOC-1 and Adaptor Protein-3 Complexes in Cargo Sorting to Synaptic Vesicles." Molecular Biology of the Cell 20, no. 5 (2009): 1441–53. http://dx.doi.org/10.1091/mbc.e08-05-0456.

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Neuronal lysosomes and their biogenesis mechanisms are primarily thought to clear metabolites and proteins whose abnormal accumulation leads to neurodegenerative disease pathology. However, it remains unknown whether lysosomal sorting mechanisms regulate the levels of membrane proteins within synaptic vesicles. Using high-resolution deconvolution microscopy, we identified early endosomal compartments where both selected synaptic vesicle and lysosomal membrane proteins coexist with the adaptor protein complex 3 (AP-3) in neuronal cells. From these early endosomes, both synaptic vesicle membrane

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Foote, Christopher, and Steven F. Nothwehr. "The clathrin adaptor complex 1 directly binds to a sorting signal in Ste13p to reduce the rate of its trafficking to the late endosome of yeast." Journal of Cell Biology 173, no. 4 (2006): 615–26. http://dx.doi.org/10.1083/jcb.200510161.

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Yeast trans-Golgi network (TGN) membrane proteins maintain steady-state localization by constantly cycling to and from endosomes. In this study, we examined the trafficking itinerary and molecular requirements for delivery of a model TGN protein A(F→A)–alkaline phosphatase (ALP) to the prevacuolar/endosomal compartment (PVC). A(F→A)-ALP was found to reach the PVC via early endosomes (EEs) with a half-time of ∼60 min. Delivery of A(F→A)-ALP to the PVC was not dependent on either the GGA or adaptor protein 1 (AP-1) type of clathrin adaptors, which are thought to function in TGN to PVC and TGN to

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Margeta, M. A., G. J. Wang, and K. Shen. "Clathrin adaptor AP-1 complex excludes multiple postsynaptic receptors from axons in C. elegans." Proceedings of the National Academy of Sciences 106, no. 5 (2009): 1632–37. http://dx.doi.org/10.1073/pnas.0812078106.

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Bian, Jingwei, Yuzhong Zhu, Panhui Tian, Qiqi Yang, and Zijian Li. "Adaptor protein HIP-55 promotes macrophage M1 polarization through promoting AP-1 complex activation." Cellular Signalling 117 (May 2024): 111124. http://dx.doi.org/10.1016/j.cellsig.2024.111124.

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Roeth, Jeremiah F., Maya Williams, Matthew R. Kasper, Tracey M. Filzen, and Kathleen L. Collins. "HIV-1 Nef disrupts MHC-I trafficking by recruiting AP-1 to the MHC-I cytoplasmic tail." Journal of Cell Biology 167, no. 5 (2004): 903–13. http://dx.doi.org/10.1083/jcb.200407031.

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To avoid immune recognition by cytotoxic T lymphocytes (CTLs), human immunodeficiency virus (HIV)-1 Nef disrupts the transport of major histocompatibility complex class I molecules (MHC-I) to the cell surface in HIV-infected T cells. However, the mechanism by which Nef does this is unknown. We report that Nef disrupts MHC-I trafficking by rerouting newly synthesized MHC-I from the trans-Golgi network (TGN) to lysosomal compartments for degradation. The ability of Nef to target MHC-I from the TGN to lysosomes is dependent on expression of the μ1 subunit of adaptor protein (AP) AP-1A, a cellular

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Lefkir, Yaya, Benoît de Chassey, Annick Dubois, et al. "The AP-1 Clathrin-adaptor Is Required for Lysosomal Enzymes Sorting and Biogenesis of the Contractile Vacuole Complex in Dictyostelium Cells." Molecular Biology of the Cell 14, no. 5 (2003): 1835–51. http://dx.doi.org/10.1091/mbc.e02-10-0627.

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Adaptor protein complexes (AP) are major components of the cytoplasmic coat found on clathrin-coated vesicles. Here, we report the molecular and functional characterization of Dictyostelium clathrin-associated AP-1 complex, which in mammalian cells, participates mainly in budding of clathrin-coated vesicles from the trans-Golgi network (TGN). The γ-adaptin AP-1 subunit was cloned and shown to belong to a Golgi-localized 300-kDa protein complex. Time-lapse analysis of cells expressing γ-adaptin tagged with the green-fluorescent protein demonstrates the dynamics of AP-1–coated structures leaving

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Di Pietro, Santiago M., Juan M. Falcón-Pérez, Danièle Tenza, et al. "BLOC-1 Interacts with BLOC-2 and the AP-3 Complex to Facilitate Protein Trafficking on Endosomes." Molecular Biology of the Cell 17, no. 9 (2006): 4027–38. http://dx.doi.org/10.1091/mbc.e06-05-0379.

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The adaptor protein (AP)-3 complex is a component of the cellular machinery that controls protein sorting from endosomes to lysosomes and specialized related organelles such as melanosomes. Mutations in an AP-3 subunit underlie a form of Hermansky-Pudlak syndrome (HPS), a disorder characterized by abnormalities in lysosome-related organelles. HPS in humans can also be caused by mutations in genes encoding subunits of three complexes of unclear function, named biogenesis of lysosome-related organelles complex (BLOC)-1, -2, and -3. Here, we report that BLOC-1 interacts physically and functionall

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Doray, Balraj, та Stuart Kornfeld. "γ Subunit of the AP-1 Adaptor Complex Binds Clathrin: Implications for Cooperative Binding in Coated Vesicle Assembly". Molecular Biology of the Cell 12, № 7 (2001): 1925–35. http://dx.doi.org/10.1091/mbc.12.7.1925.

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The heterotetrameric AP-1 adaptor complex is involved in the assembly of clathrin-coated vesicles originating from thetrans-Golgi network (TGN). The β1 subunit of AP-1 is known to contain a consensus clathrin binding sequence, LLNLD (the so-called clathrin box motif), in its hinge segment through which the β chain interacts with the N-terminal domains of clathrin trimers. Here, we report that the hinge region of the γ subunit of human and mouse AP-1 contains two copies of a new variant, LLDLL, of the clathrin box motif that also bind to the terminal domain of the clathrin heavy chain. High-aff

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Keyel, Peter A., James R. Thieman, Robyn Roth та ін. "The AP-2 Adaptor β2 Appendage Scaffolds Alternate Cargo Endocytosis". Molecular Biology of the Cell 19, № 12 (2008): 5309–26. http://dx.doi.org/10.1091/mbc.e08-07-0712.

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The independently folded appendages of the large α and β2 subunits of the endocytic adaptor protein (AP)-2 complex coordinate proper assembly and operation of endocytic components during clathrin-mediated endocytosis. The β2 subunit appendage contains a common binding site for β-arrestin or the autosomal recessive hypercholesterolemia (ARH) protein. To determine the importance of this interaction surface in living cells, we used small interfering RNA-based gene silencing. The effect of extinguishing β2 subunit expression on the internalization of transferrin is considerably weaker than an AP-2

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Schneider, Helga, Margarita Martin, Fernando A. Agarraberes та ін. "Cytolytic T Lymphocyte-Associated Antigen-4 and the TCRζ/CD3 Complex, But Not CD28, Interact with Clathrin Adaptor Complexes AP-1 and AP-2". Journal of Immunology 163, № 4 (1999): 1868–79. http://dx.doi.org/10.4049/jimmunol.163.4.1868.

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Abstract The negative signaling receptor cytolytic T lymphocyte-associated Ag-4 (CTLA-4) resides primarily in intracellular compartments such as the Golgi apparatus of T cells. However, little is known regarding the molecular mechanisms that influence this accumulation. In this study, we demonstrate binding of the clathrin adaptor complex AP-1 with the GVYVKM motif of the cytoplasmic domain of CTLA-4. Binding occurred primarily in the Golgi compartment of T cells, unlike with AP-2 binding that occurs mostly with cell surface CTLA-4. Although evidence was not found to implicate AP-1 binding in

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Morris, Kyle L., Cosmo Buffalo, Xuefeng Ren, and James H. Hurley. "High Resolution cryo-EM Structure of a HIV Nef-Inhibited AP-1 Clathrin Adaptor Complex." Biophysical Journal 114, no. 3 (2018): 163a. http://dx.doi.org/10.1016/j.bpj.2017.11.913.

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Ren, Xuefeng, Ginny G. Farías, Bertram J. Canagarajah, Juan S. Bonifacino, and James H. Hurley. "Structural Basis for Recruitment and Activation of the AP-1 Clathrin Adaptor Complex by Arf1." Cell 152, no. 4 (2013): 755–67. http://dx.doi.org/10.1016/j.cell.2012.12.042.

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Fujita, Hideaki, Masayo Saeki, Kumiko Yasunaga, Tadashi Ueda, Taiji Imoto, and Masaru Himeno. "In VitroBinding Study of Adaptor Protein Complex (AP-1) to Lysosomal Targeting Motif (LI-Motif)." Biochemical and Biophysical Research Communications 255, no. 1 (1999): 54–58. http://dx.doi.org/10.1006/bbrc.1998.0140.

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Larimore, Jennifer, Karine Tornieri, Pearl V. Ryder, et al. "The schizophrenia susceptibility factor dysbindin and its associated complex sort cargoes from cell bodies to the synapse." Molecular Biology of the Cell 22, no. 24 (2011): 4854–67. http://dx.doi.org/10.1091/mbc.e11-07-0592.

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Dysbindin assembles into the biogenesis of lysosome-related organelles complex 1 (BLOC-1), which interacts with the adaptor protein complex 3 (AP-3), mediating a common endosome-trafficking route. Deficiencies in AP-3 and BLOC-1 affect synaptic vesicle composition. However, whether AP-3-BLOC-1–dependent sorting events that control synapse membrane protein content take place in cell bodies upstream of nerve terminals remains unknown. We tested this hypothesis by analyzing the targeting of phosphatidylinositol-4-kinase type II α (PI4KIIα), a membrane protein present in presynaptic and postsynapt

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Burgess, Jason, Miluska Jauregui, Julie Tan, et al. "AP-1 and clathrin are essential for secretory granule biogenesis in Drosophila." Molecular Biology of the Cell 22, no. 12 (2011): 2094–105. http://dx.doi.org/10.1091/mbc.e11-01-0054.

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Regulated secretion of hormones, digestive enzymes, and other biologically active molecules requires the formation of secretory granules. Clathrin and the clathrin adaptor protein complex 1 (AP-1) are necessary for maturation of exocrine, endocrine, and neuroendocrine secretory granules. However, the initial steps of secretory granule biogenesis are only minimally understood. Powerful genetic approaches available in the fruit fly Drosophila melanogaster were used to investigate the molecular pathway for biogenesis of the mucin-containing “glue granules” that form within epithelial cells of the

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Hirst, Jennifer, Georg H. H. Borner, James Edgar, et al. "Interaction between AP-5 and the hereditary spastic paraplegia proteins SPG11 and SPG15." Molecular Biology of the Cell 24, no. 16 (2013): 2558–69. http://dx.doi.org/10.1091/mbc.e13-03-0170.

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The AP-5 complex is a recently identified but evolutionarily ancient member of the family of heterotetrameric adaptor proteins (AP complexes). It is associated with two proteins that are mutated in patients with hereditary spastic paraplegia, SPG11 and SPG15. Here we show that the four AP-5 subunits can be coimmunoprecipitated with SPG11 and SPG15, both from cytosol and from detergent-extracted membranes, with a stoichiometry of ∼1:1:1:1:1:1. Knockdowns of SPG11 or SPG15 phenocopy knockdowns of AP-5 subunits: all six knockdowns cause the cation-independent mannose 6-phosphate receptor to becom

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Pujol, François M., Vibor Laketa, Florian Schmidt, et al. "HIV-1 Vpu Antagonizes CD317/Tetherin by Adaptor Protein-1-Mediated Exclusion from Virus Assembly Sites." Journal of Virology 90, no. 15 (2016): 6709–23. http://dx.doi.org/10.1128/jvi.00504-16.

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ABSTRACTThe host cell restriction factor CD317/tetherin traps virions at the surface of producer cells to prevent their release. The HIV-1 accessory protein Vpu antagonizes this restriction. Vpu reduces the cell surface density of the restriction factor and targets it for degradation; however, these activities are dispensable for enhancing particle release. Instead, Vpu has been suggested to antagonize CD317/tetherin by preventing recycling of internalized CD317/tetherin to the cell surface, blocking anterograde transport of newly synthesized CD317/tetherin, and/or displacing the restriction f

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Martina, José A., Cecilia J. Bonangelino, Rubén C. Aguilar, and Juan S. Bonifacino. "Stonin 2." Journal of Cell Biology 153, no. 5 (2001): 1111–20. http://dx.doi.org/10.1083/jcb.153.5.1111.

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Endocytosis of cell surface proteins is mediated by a complex molecular machinery that assembles on the inner surface of the plasma membrane. Here, we report the identification of two ubiquitously expressed human proteins, stonin 1 and stonin 2, related to components of the endocytic machinery. The human stonins are homologous to the Drosophila melanogaster stoned B protein and exhibit a modular structure consisting of an NH2-terminal proline-rich domain, a central region of homology specific to the stonins, and a COOH-terminal region homologous to the μ subunits of adaptor protein (AP) comple

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Chen, Buxin, David P. Siderovski, Richard R. Neubig, Mark A. Lawson, and JoAnn Trejo. "Regulation of Protease-activated Receptor 1 Signaling by the Adaptor Protein Complex 2 and R4 Subfamily of Regulator of G Protein Signaling Proteins." Journal of Biological Chemistry 289, no. 3 (2013): 1580–91. http://dx.doi.org/10.1074/jbc.m113.528273.

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The G protein-coupled protease-activated receptor 1 (PAR1) is irreversibly proteolytically activated by thrombin. Hence, the precise regulation of PAR1 signaling is important for proper cellular responses. In addition to desensitization, internalization and lysosomal sorting of activated PAR1 are critical for the termination of signaling. Unlike most G protein-coupled receptors, PAR1 internalization is mediated by the clathrin adaptor protein complex 2 (AP-2) and epsin-1, rather than β-arrestins. However, the function of AP-2 and epsin-1 in the regulation of PAR1 signaling is not known. Here,

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Lubben, Nienke B., Daniela A. Sahlender, Alison M. Motley, Paul J. Lehner, Philippe Benaroch, and Margaret S. Robinson. "HIV-1 Nef-induced Down-Regulation of MHC Class I Requires AP-1 and Clathrin but Not PACS-1 and Is Impeded by AP-2." Molecular Biology of the Cell 18, no. 9 (2007): 3351–65. http://dx.doi.org/10.1091/mbc.e07-03-0218.

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Major histocompatibility complex class I is down-regulated from the surface of human immunodeficiency virus (HIV)-1-infected cells by Nef, a virally encoded protein that is thought to reroute MHC-I to the trans-Golgi network (TGN) in a phosphofurin acidic cluster sorting protein (PACS) 1, adaptor protein (AP)-1, and clathrin-dependent manner. More recently, an alternative model has been proposed, in which Nef uses AP-1 to direct MHC-I to endosomes and lysosomes. Here, we show that knocking down either AP-1 or clathrin with small interfering RNA inhibits the down-regulation of HLA-A2 (an MHC-I

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Jakob, Viktor, Alexander Schreiner, Ritva Tikkanen, and Anna Starzinski-Powitz. "Targeting of Transmembrane Protein Shrew-1 to Adherens Junctions Is Controlled by Cytoplasmic Sorting Motifs." Molecular Biology of the Cell 17, no. 8 (2006): 3397–408. http://dx.doi.org/10.1091/mbc.e05-11-1034.

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We recently identified transmembrane protein shrew-1 and showed that it is able to target to adherens junctions in polarized epithelial cells. This suggested shrew-1 possesses specific basolateral sorting motifs, which we analyzed by mutational analysis. Systematic mutation of amino acids in putative sorting signals in the cytoplasmic domain of shrew-1 revealed three tyrosines and a dileucine motif necessary for basolateral sorting. Substitution of these amino acids leads to apical localization of shrew-1. By applying tannic acid to either the apical or basolateral part of polarized epithelial

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Vince, James E., Dedreia L. Tull, Timothy Spurck, et al. "Leishmania Adaptor Protein-1 Subunits Are Required for Normal Lysosome Traffic, Flagellum Biogenesis, Lipid Homeostasis, and Adaptation to Temperatures Encountered in the Mammalian Host." Eukaryotic Cell 7, no. 8 (2008): 1256–67. http://dx.doi.org/10.1128/ec.00090-08.

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ABSTRACT The adaptor protein-1 (AP-1) complex is involved in membrane transport between the Golgi apparatus and endosomes. In the protozoan parasite Leishmania mexicana mexicana, the AP-1 μ1 and σ1 subunits are not required for growth at 27°C but are essential for infectivity in the mammalian host. In this study, we have investigated the function of these AP-1 subunits in order to understand the molecular basis for this loss of virulence. The μ1 and σ1 subunits were localized to late Golgi and endosome membranes of the major parasite stages. Parasite mutants lacking either AP-1 subunit lacked

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Huizing, Marjan, Rangaprasad Sarangarajan, Erin Strovel, Yang Zhao, William A. Gahl, and Raymond E. Boissy. "AP-3 Mediates Tyrosinase but Not TRP-1 Trafficking in Human Melanocytes." Molecular Biology of the Cell 12, no. 7 (2001): 2075–85. http://dx.doi.org/10.1091/mbc.12.7.2075.

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Patients with Hermansky-Pudlak syndrome type 2 (HPS-2) have mutations in the β3A subunit of adaptor complex-3 (AP-3) and functional deficiency of this complex. AP-3 serves as a coat protein in the formation of new vesicles, including, apparently, the platelet's dense body and the melanocyte's melanosome. We used HPS-2 melanocytes in culture to determine the role of AP-3 in the trafficking of the melanogenic proteins tyrosinase and tyrosinase-related protein-1 (TRP-1). TRP-1 displayed a typical melanosomal pattern in both normal and HPS-2 melanocytes. In contrast, tyrosinase exhibited a melanos

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Ishizaki, Ray, Hye-Won Shin, Hiroko Mitsuhashi, and Kazuhisa Nakayama. "Redundant Roles of BIG2 and BIG1, Guanine-Nucleotide Exchange Factors for ADP-Ribosylation Factors in Membrane Traffic between the trans-Golgi Network and Endosomes." Molecular Biology of the Cell 19, no. 6 (2008): 2650–60. http://dx.doi.org/10.1091/mbc.e07-10-1067.

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BIG2 and BIG1 are closely related guanine-nucleotide exchange factors (GEFs) for ADP-ribosylation factors (ARFs) and are involved in the regulation of membrane traffic through activating ARFs and recruiting coat protein complexes, such as the COPI complex and the AP-1 clathrin adaptor complex. Although both ARF-GEFs are associated mainly with the trans-Golgi network (TGN) and BIG2 is also associated with recycling endosomes, it is unclear whether BIG2 and BIG1 share some roles in membrane traffic. We here show that knockdown of both BIG2 and BIG1 by RNAi causes mislocalization of a subset of p

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Almomani, Ensaf Y., Jennifer C. King, Janjuree Netsawang, et al. "Adaptor protein 1 complexes regulate intracellular trafficking of the kidney anion exchanger 1 in epithelial cells." American Journal of Physiology-Cell Physiology 303, no. 5 (2012): C554—C566. http://dx.doi.org/10.1152/ajpcell.00124.2012.

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Distal renal tubular acidosis (dRTA) can be caused by mutations in the gene encoding the anion exchanger 1 (AE1) and is characterized by defective urinary acidification, metabolic acidosis, and renal stones. AE1 is expressed at the basolateral membrane of type A intercalated cells in the renal cortical collecting duct (kAE1). Two dRTA mutations result in the carboxyl-terminal truncation of kAE1; in one case, the protein trafficked in a nonpolarized way in epithelial cells. A recent yeast two-hybrid assay showed that the carboxyl-terminal cytosolic domain of AE1 interacts with adaptor protein c

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Noviello, Colleen M., Serge Benichou та John C. Guatelli. "Cooperative Binding of the Class I Major Histocompatibility Complex Cytoplasmic Domain and Human Immunodeficiency Virus Type 1 Nef to the Endosomal AP-1 Complex via Its μ Subunit". Journal of Virology 82, № 3 (2007): 1249–58. http://dx.doi.org/10.1128/jvi.00660-07.

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ABSTRACT Human immunodeficiency virus type 1 Nef provides immune evasion by decreasing the expression of major histocompatibility complex class I (MHC-I) at the surfaces of infected cells. The endosomal clathrin adaptor protein complex AP-1 is a key cellular cofactor for this activity, and it is recruited to the MHC-I cytoplasmic domain (CD) in the presence of Nef by an uncharacterized mechanism. To determine the molecular basis of this recruitment, we used an MHC-I CD-Nef fusion protein to represent the MHC-I CD/Nef complex during protein interaction assays. The MHC-I CD had no intrinsic abil

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