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Journal articles on the topic 'Complexe adapteur AP-1'

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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

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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4

Kim, Myung-Hee, and Louis B. Hersh. "The Vesicular Acetylcholine Transporter Interacts with Clathrin-associated Adaptor Complexes AP-1 and AP-2." Journal of Biological Chemistry 279, no. 13 (2004): 12580–87. http://dx.doi.org/10.1074/jbc.m310681200.

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5

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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6

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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7

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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8

Nie, Z. "The Arf GAPs AGAP1 and AGAP2 distinguish between the adaptor protein complexes AP-1 and AP-3." Journal of Cell Science 118, no. 15 (2005): 3555–66. http://dx.doi.org/10.1242/jcs.02486.

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9

Barone, Maria Elena, Alexis Lim, Madison Woody, et al. "Adaptor Protein Complexes in HIV-1 Pathogenesis: Mechanisms and Therapeutic Potential." Viruses 17, no. 5 (2025): 715. https://doi.org/10.3390/v17050715.

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Adaptor protein (AP) complexes are critical components of the cellular membrane transport machinery. They mediate cargo selection during endocytosis and intracellular vesicular trafficking. Five AP complexes have been characterized (AP1-5), and together their roles extend to diverse cellular processes including the homeostasis of membranous organelles, membrane protein turnover, and immune responses. Human Immunodeficiency Virus type 1 (HIV-1) and other lentiviruses co-opt these complexes to support immune evasion and the assembly of maximally infectious particles. HIV-1 Nef interacts with AP1
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10

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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11

Coleman, Scott H., Nanette Van Damme, John R. Day, et al. "Leucine-Specific, Functional Interactions between Human Immunodeficiency Virus Type 1 Nef and Adaptor Protein Complexes." Journal of Virology 79, no. 4 (2005): 2066–78. http://dx.doi.org/10.1128/jvi.79.4.2066-2078.2005.

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ABSTRACT The human immunodeficiency virus type 1 virulence protein Nef interacts with the endosomal sorting machinery via a leucine-based motif. Similar sequences within the cytoplasmic domains of cellular transmembrane proteins bind to the adaptor protein (AP) complexes of coated vesicles to modulate protein traffic, but the molecular basis of the interactions between these motifs and the heterotetrameric complexes is controversial. To identify the target of the Nef leucine motif, the native sequence was replaced with either leucine- or tyrosine-based AP-binding sequences from cellular protei
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12

LUNDMARK, Richard, та Sven R. CARLSSON. "The β-appendages of the four adaptor-protein (AP) complexes: structure and binding properties, and identification of sorting nexin 9 as an accessory protein to AP-2". Biochemical Journal 362, № 3 (2002): 597–607. http://dx.doi.org/10.1042/bj3620597.

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Adaptor protein (AP) complexes are essential components for the formation of coated vesicles and the recognition of cargo proteins for intracellular transport. Each AP complex exposes two appendage domains with that function to bind regulatory accessory proteins in the cytosol. Secondary structure predictions, sequence alignments and CD spectroscopy were used to relate the β-appendages of all human AP complexes to the previously published crystal structure of AP-2. The results suggested that the β-appendages of AP-1, AP-2 and AP-3 have similar structures, consisting of two subdomains, whereas
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13

Boehm, Markus, and Juan S. Bonifacino. "Adaptins." Molecular Biology of the Cell 12, no. 10 (2001): 2907–20. http://dx.doi.org/10.1091/mbc.12.10.2907.

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Adaptins are subunits of adaptor protein (AP) complexes involved in the formation of intracellular transport vesicles and in the selection of cargo for incorporation into the vesicles. In this article, we report the results of a survey for adaptins from sequenced genomes including those of man, mouse, the fruit fly Drosophila melanogaster, the nematode Caenorhabditis elegans, the plant Arabidopsis thaliana, and the yeasts, Saccharomyces cerevisiae andSchizosaccharomyces pombe. We find that humans, mice, and Arabidopsis thaliana have four AP complexes (AP-1, AP-2, AP-3, and AP-4), whereas D. me
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14

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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15

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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16

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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17

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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18

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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19

Chakrabarti, R., M. Joly, and S. Corvera. "Redistribution of clathrin-coated vesicle adaptor complexes during adipocytic differentiation of 3T3-L1 cells." Journal of Cell Biology 123, no. 1 (1993): 79–87. http://dx.doi.org/10.1083/jcb.123.1.79.

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Mechanisms for intracellular retention of proteins are induced during adipocytic differentiation of 3T3-L1 cells. To investigate the potential role of clathrin lattices in these retention processes, we performed a morphological and biochemical analysis of coated vesicle components in 3T3-L1 cells. Optical sectioning and image restoration revealed a marked increase in the staining of clathrin and beta adaptins in the perinuclear region of cells with differentiation. In addition, predominance of beta (subunit of the AP-2, plasma membrane adaptor) over beta' (subunit of the AP-1, Golgi adaptor) a
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20

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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21

Theos, Alexander C., Danièle Tenza, José A. Martina, et al. "Functions of Adaptor Protein (AP)-3 and AP-1 in Tyrosinase Sorting from Endosomes to Melanosomes." Molecular Biology of the Cell 16, no. 11 (2005): 5356–72. http://dx.doi.org/10.1091/mbc.e05-07-0626.

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Specialized cells exploit adaptor protein complexes for unique post-Golgi sorting events, providing a unique model system to specify adaptor function. Here, we show that AP-3 and AP-1 function independently in sorting of the melanocyte-specific protein tyrosinase from endosomes to the melanosome, a specialized lysosome-related organelle distinguishable from lysosomes. AP-3 and AP-1 localize in melanocytes primarily to clathrin-coated buds on tubular early endosomes near melanosomes. Both adaptors recognize the tyrosinase dileucine-based melanosome sorting signal, and tyrosinase largely colocal
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22

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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23

Rodionov, Dmitrii G., and Oddmund Bakke. "Medium Chains of Adaptor Complexes AP-1 and AP-2 Recognize Leucine-based Sorting Signals from the Invariant Chain." Journal of Biological Chemistry 273, no. 11 (1998): 6005–8. http://dx.doi.org/10.1074/jbc.273.11.6005.

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24

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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25

Wang, Ying Jie, Jing Wang, Hui Qiao Sun, et al. "Phosphatidylinositol 4 Phosphate Regulates Targeting of Clathrin Adaptor AP-1 Complexes to the Golgi." Cell 114, no. 3 (2003): 299–310. http://dx.doi.org/10.1016/s0092-8674(03)00603-2.

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26

Puffer, Bridget A., S. C. Watkins, and Ronald C. Montelaro. "Equine Infectious Anemia Virus Gag Polyprotein Late Domain Specifically Recruits Cellular AP-2 Adapter Protein Complexes during Virion Assembly." Journal of Virology 72, no. 12 (1998): 10218–21. http://dx.doi.org/10.1128/jvi.72.12.10218-10221.1998.

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ABSTRACT We have identified an interaction between the equine infectious anemia virus (EIAV) late assembly domain and the cellular AP-2 clathrin-associated adapter protein complex. A YXXL motif within the EIAV Gag late assembly domain was previously characterized as a sequence critical for release of assembling virions. We now show that this YXXL sequence interacts in vitro with the AP-50 subunit of the AP-2 complex, while the functionally interchangeable late assembly domains carried by the Rous sarcoma virus p2b protein and human immunodeficiency virus type 1 p6 protein, which utilize PPPY a
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27

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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28

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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29

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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30

Mitsunari, Takashi, Fubito Nakatsu, Noriko Shioda, et al. "Clathrin Adaptor AP-2 Is Essential for Early Embryonal Development." Molecular and Cellular Biology 25, no. 21 (2005): 9318–23. http://dx.doi.org/10.1128/mcb.25.21.9318-9323.2005.

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ABSTRACT The heterotetrameric adaptor protein (AP) complexes AP-1, AP-2, AP-3, and AP-4 play key roles in transport vesicle formation and cargo sorting in post-Golgi trafficking pathways. Studies on cultured mammalian cells have shown that AP-2 mediates rapid endocytosis of a subset of plasma membrane receptors. To determine whether this function is essential in the context of a whole mammalian organism, we carried out targeted disruption of the gene encoding the μ2 subunit of AP-2 in the mouse. We found that μ2 heterozygous mutant mice were viable and had an apparently normal phenotype. In co
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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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32

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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33

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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34

Nadiminti, Sravanthi S. P., Shirley B. Dixit, Neena Ratnakaran та ін. "LRK-1/LRRK2 and AP-3 regulate trafficking of synaptic vesicle precursors through active zone protein SYD-2/Liprin-α". PLOS Genetics 20, № 5 (2024): e1011253. http://dx.doi.org/10.1371/journal.pgen.1011253.

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Synaptic vesicle proteins (SVps) are transported by the motor UNC-104/KIF1A. We show that SVps travel in heterogeneous carriers in C. elegans neuronal processes, with some SVp carriers co-transporting lysosomal proteins (SV-lysosomes). LRK-1/LRRK2 and the clathrin adaptor protein complex AP-3 play a critical role in the sorting of SVps and lysosomal proteins away from each other at the SV-lysosomal intermediate trafficking compartment. Both SVp carriers lacking lysosomal proteins and SV-lysosomes are dependent on the motor UNC-104/KIF1A for their transport. In lrk-1 mutants, both SVp carriers
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35

Braun, Virginie, Chantal Deschamps, Graça Raposo, et al. "AP-1 and ARF1 Control Endosomal Dynamics at Sites of FcR–mediated Phagocytosis." Molecular Biology of the Cell 18, no. 12 (2007): 4921–31. http://dx.doi.org/10.1091/mbc.e07-04-0392.

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Phagocytosis, the mechanism of ingestion of large material and microorganisms, relies on actin polymerization and on the focal delivery of intracellular endocytic compartments. The molecular mechanisms involved in the formation and delivery of the endocytic vesicles that are recruited at sites of phagocytosis are not well characterized. Here we show that adaptor protein (AP)-1 but not AP-2 clathrin adaptor complexes are recruited early below the sites of particle attachment and are required for efficient receptor-mediated phagocytosis in murine macrophages. Clathrin, however, is not recruited
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36

Wyss, Stéphanie, Clarisse Berlioz-Torrent, Michael Boge, et al. "The Highly Conserved C-Terminal Dileucine Motif in the Cytosolic Domain of the Human Immunodeficiency Virus Type 1 Envelope Glycoprotein Is Critical for Its Association with the AP-1 Clathrin Adapter." Journal of Virology 75, no. 6 (2001): 2982–92. http://dx.doi.org/10.1128/jvi.75.6.2982-2992.2001.

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ABSTRACT Short amino acid sequences in the cytosolic domains of transmembrane proteins are recognized by specialized adapter proteins which are part of coated vesicles utilized to transport membrane proteins between the trans-Golgi network (TGN) and the plasma membrane (forward and backward). Previously, we and others reported that the membrane-proximal tyrosine residues Y712 (human immunodeficiency virus [HIV]) and Y721 (simian immunodeficiency virus [SIV]) in the envelope glycoprotein (Env) of the primate lentiviruses are crucial for the association of Env with clathrin-associated adapter co
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37

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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38

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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39

Mitchell, Richard S., Rittik Chaudhuri, O. Wolf Lindwasser, et al. "Competition Model for Upregulation of the Major Histocompatibility Complex Class II-Associated Invariant Chain by Human Immunodeficiency Virus Type 1 Nef." Journal of Virology 82, no. 16 (2008): 7758–67. http://dx.doi.org/10.1128/jvi.02668-07.

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ABSTRACT The human immunodeficiency virus type 1 (HIV-1) Nef protein upregulates the expression of the invariant chain (Ii)/major histocompatibility complex class II (MHC-II) complex at the cell surface. This complex appears to reach the antigen-loading endosomal compartment at least in part via an indirect pathway in which it is internalized from the cell surface via the adaptor protein 2 (AP-2) complex. Here we provide evidence for a competition model to explain how Nef upregulates the expression of Ii at the cell surface. In this model, Nef and Ii compete for binding to AP-2. In support of
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40

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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41

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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42

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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43

Lindwasser, O. Wolf, William J. Smith, Rittik Chaudhuri, Peter Yang, James H. Hurley, and Juan S. Bonifacino. "A Diacidic Motif in Human Immunodeficiency Virus Type 1 Nef Is a Novel Determinant of Binding to AP-2." Journal of Virology 82, no. 3 (2007): 1166–74. http://dx.doi.org/10.1128/jvi.01874-07.

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ABSTRACT A key function of the Nef protein of immunodeficiency viruses is the downregulation of the T-cell and macrophage coreceptor, CD4, from the surfaces of infected cells. CD4 downregulation depends on a conserved (D/E)XXXL(L/I)-type dileucine motif in the C-terminal, flexible loop of Nef, which mediates binding to the clathrin adaptor complexes AP-1, AP-2, and AP-3. We now report the identification of a consensus (D/E)D motif within this loop as a second, conserved determinant of interaction of Nef with AP-2, though not with AP-1 and AP-3. Mutations in this diacidic motif abrogate both AP
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44

Meyer, Daniel M., Pascal Crottet, Bohumil Maco, Elena Degtyar, Dan Cassel, and Martin Spiess. "Oligomerization and Dissociation of AP-1 Adaptors Are Regulated by Cargo Signals and by ArfGAP1-induced GTP Hydrolysis." Molecular Biology of the Cell 16, no. 10 (2005): 4745–54. http://dx.doi.org/10.1091/mbc.e05-06-0568.

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The mechanism of AP-1/clathrin coat formation was analyzed using purified adaptor proteins and synthetic liposomes presenting tyrosine sorting signals. AP-1 adaptors recruited in the presence of Arf1·GTP and sorting signals were found to oligomerize to high-molecular-weight complexes even in the absence of clathrin. The appendage domains of the AP-1 adaptins were not required for oligomerization. On GTP hydrolysis induced by the GTPase-activating protein ArfGAP1, the complexes were disassembled and AP-1 dissociated from the membrane. AP-1 stimulated ArfGAP1 activity, suggesting a role of AP-1
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45

Janvier, Katy, Yukio Kato, Markus Boehm та ін. "Recognition of dileucine-based sorting signals from HIV-1 Nef and LIMP-II by the AP-1 γ–σ1 and AP-3 δ–σ3 hemicomplexes". Journal of Cell Biology 163, № 6 (2003): 1281–90. http://dx.doi.org/10.1083/jcb.200307157.

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The sorting of transmembrane proteins to endosomes and lysosomes is mediated by signals present in the cytosolic tails of the proteins. A subset of these signals conform to the [DE]XXXL[LI] consensus motif and mediate sorting via interactions with heterotetrameric adaptor protein (AP) complexes. However, the identity of the AP subunits that recognize these signals remains controversial. We have used a yeast three-hybrid assay to demonstrate that [DE]XXXL[LI]-type signals from the human immunodeficiency virus negative factor protein and the lysosomal integral membrane protein II interact with c
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46

Coleman, Scott H., Ricardo Madrid, Nanette Van Damme, et al. "Modulation of Cellular Protein Trafficking by Human Immunodeficiency Virus Type 1 Nef: Role of the Acidic Residue in the ExxxLL Motif." Journal of Virology 80, no. 4 (2006): 1837–49. http://dx.doi.org/10.1128/jvi.80.4.1837-1849.2006.

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ABSTRACT The nef gene contributes to the replication of primate lentiviruses by altering the trafficking of cellular proteins involved in adaptive immunity (class I and II major histocompatibility complex [MHC]) and viral transmission (CD4 and DC-SIGN). A conserved acidic leucine-based sequence (E160xxxLL) within human immunodeficiency virus type 1 (HIV-1) Nef binds to the cellular adaptor protein (AP) complexes, which mediate protein sorting into endosomal vesicles. The leucine residues in this motif are required for the down-regulation of CD4 and for the up-regulation of DC-SIGN and the inva
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47

Crottet, Pascal, Daniel M. Meyer, Jack Rohrer, and Martin Spiess. "ARF1·GTP, Tyrosine-based Signals, and Phosphatidylinositol 4,5-Bisphosphate Constitute a Minimal Machinery to Recruit the AP-1 Clathrin Adaptor to Membranes." Molecular Biology of the Cell 13, no. 10 (2002): 3672–82. http://dx.doi.org/10.1091/mbc.e02-05-0309.

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At the trans-Golgi network, clathrin coats containing AP-1 adaptor complexes are formed in an ARF1-dependent manner, generating vesicles transporting cargo proteins to endosomes. The mechanism of site-specific targeting of AP-1 and the role of cargo are poorly understood. We have developed an in vitro assay to study the recruitment of purified AP-1 adaptors to chemically defined liposomes presenting peptides corresponding to tyrosine-based sorting motifs. AP-1 recruitment was found to be dependent on myristoylated ARF1, GTP or nonhydrolyzable GTP-analogs, tyrosine signals, and small amounts of
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48

Suckow, Arthur T., Branch Craige, Victor Faundez, William J. Cain та Steven D. Chessler. "An AP-3-dependent mechanism drives synaptic-like microvesicle biogenesis in pancreatic islet β-cells". American Journal of Physiology-Endocrinology and Metabolism 299, № 1 (2010): E23—E32. http://dx.doi.org/10.1152/ajpendo.00664.2009.

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Pancreatic islet β-cells contain synaptic-like microvesicles (SLMVs). The origin, trafficking, and role of these SLMVs are poorly understood. In neurons, synaptic vesicle (SV) biogenesis is mediated by two different cytosolic adaptor protein complexes, a ubiquitous AP-2 complex and the neuron-specific AP-3B complex. Mice lacking AP-3B subunits exhibit impaired GABAergic (inhibitory) neurotransmission and reduced neuronal vesicular GABA transporter (VGAT) content. Since β-cell maturation and exocytotic function seem to parallel that of the inhibitory synapse, we predicted that AP-3B-associated
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49

Fessart, Delphine, May Simaan та Stéphane A. Laporte. "c-Src Regulates Clathrin Adapter Protein 2 Interaction with β-Arrestin and the Angiotensin II Type 1 Receptor during Clathrin- Mediated Internalization". Molecular Endocrinology 19, № 2 (2005): 491–503. http://dx.doi.org/10.1210/me.2004-0246.

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Abstract β-Arrestins are multifunctional adapters involved in the internalization and signaling of G protein-coupled receptors (GPCRs). They target receptors to clathrin-coated pits (CCPs) through binding with clathrin and clathrin adapter 2 (AP-2) complex. They also act as transducers of signaling by recruiting c-Src kinase to certain GPCRs. Here we sought to determine whether c-Src regulates the recruitment of AP-2 to β-arrestin and the angiotensin II (Ang II) type 1 receptor (AT1R) during internalization. We show that the agonist stimulation of native AT1R in vascular smooth muscle cells (V
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50

Janvier, Katy, and Juan S. Bonifacino. "Role of the Endocytic Machinery in the Sorting of Lysosome-associated Membrane Proteins." Molecular Biology of the Cell 16, no. 9 (2005): 4231–42. http://dx.doi.org/10.1091/mbc.e05-03-0213.

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The limiting membrane of the lysosome contains a group of transmembrane glycoproteins named lysosome-associated membrane proteins (Lamps). These proteins are targeted to lysosomes by virtue of tyrosine-based sorting signals in their cytosolic tails. Four adaptor protein (AP) complexes, AP-1, AP-2, AP-3, and AP-4, interact with such signals and are therefore candidates for mediating sorting of the Lamps to lysosomes. However, the role of these complexes and of the coat protein, clathrin, in sorting of the Lamps in vivo has either not been addressed or remains controversial. We have used RNA int
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