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Journal articles on the topic 'Molecular adaptor'

Author: Grafiati

Published: 14 March 2023

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1

Pucadyil, Thomas J., and Sachin S. Holkar. "Comparative analysis of adaptor-mediated clathrin assembly reveals general principles for adaptor clustering." Molecular Biology of the Cell 27, no. 20 (October 15, 2016): 3156–63. http://dx.doi.org/10.1091/mbc.e16-06-0399.

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Clathrin-mediated endocytosis (CME) manages the sorting and uptake of the bulk of membrane proteins (or cargo) from the plasma membrane. CME is initiated by the formation of clathrin-coated pits (CCPs), in which adaptors nucleate clathrin assembly. Clathrin adaptors display diversity in both the type and number of evolutionarily conserved clathrin-binding boxes. How this diversity relates to the process of adaptor clustering as clathrin assembles around a growing pit remains unclear. Using real-time, fluorescence microscopy–based assays, we compare the formation kinetics and distribution of clathrin assemblies on membranes that display five unique clathrin adaptors. Correlations between equilibrium and kinetic parameters of clathrin assembly to the eventual adaptor distribution indicate that adaptor clustering is determined not by the amount of clathrin recruited or the degree of clathrin clustered but instead by the rate of clathrin assembly. Together our results emphasize the need to analyze kinetics of protein interactions to better understand mechanisms that regulate CME.

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2

Ades, Sarah E. "Proteolysis: Adaptor, Adaptor, Catch Me a Catch." Current Biology 14, no. 21 (November 2004): R924—R926. http://dx.doi.org/10.1016/j.cub.2004.10.015.

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3

D'Souza, Cynthia R., Ken V. Deugau, and John H. Spencer. "A simplified procedure for cDNA and genomic library construction using nonpalindromic oligonucleotide adaptors." Biochemistry and Cell Biology 67, no. 4-5 (April 1, 1989): 205–9. http://dx.doi.org/10.1139/o89-031.

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The properties and characteristics of oligonucleotide adaptors for use in a simplified procedure for the construction of cDNA and genomic DNA libraries are described. The adaptors are suitable for joining to blunt ended cDNA or sheared genomic DNA, and then to the cohesive ends of restriction sites in vectors. Each adaptor consists of two oligonucleotides with complementary but nonpalindromic sequences that include an internal restriction site, a 5′ phosphorylated blunt end, and an overlapping or staggered 5′ hydroxylated end corresponding to a restriction endonuclease site in a vector of choice. Ligation of the blunt end to high molecular weight target DNA proceeds efficiently and there is no tandem concatenation of the adaptor. Insertion into the appropriate vector only requires ligation of the cohesive ends. There is no requirement for methylation, restriction enzyme cleavage, G-C tailing, or denaturation after ligation of the adaptor to the target DNA, all characteristics of other procedures.Key words: library, genomic, cDNA, oligonucleotides, adaptors.

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4

Maldonado-Báez, Lymarie, Michael R. Dores, Edward M. Perkins, Theodore G. Drivas, Linda Hicke, and Beverly Wendland. "Interaction between Epsin/Yap180 Adaptors and the Scaffolds Ede1/Pan1 Is Required for Endocytosis." Molecular Biology of the Cell 19, no. 7 (July 2008): 2936–48. http://dx.doi.org/10.1091/mbc.e07-10-1019.

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The spatial and temporal regulation of the interactions among the ∼60 proteins required for endocytosis is under active investigation in many laboratories. We have identified the interaction between monomeric clathrin adaptors and endocytic scaffold proteins as a critical prerequisite for the recruitment and/or spatiotemporal dynamics of endocytic proteins at early and late stages of internalization. Quadruple deletion yeast cells (ΔΔΔΔ) lacking four putative adaptors, Ent1/2 and Yap1801/2 (homologues of epsin and AP180/CALM proteins), with a plasmid encoding Ent1 or Yap1802 mutants, have defects in endocytosis and growth at 37°C. Live-cell imaging revealed that the dynamics of the early- and late-acting scaffold proteins Ede1 and Pan1, respectively, depend upon adaptor interactions mediated by adaptor asparagine-proline-phenylalanine motifs binding to scaffold Eps15 homology domains. These results suggest that adaptor/scaffold interactions regulate transitions from early to late events and that clathrin adaptor/scaffold protein interaction is essential for clathrin-mediated endocytosis.

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5

VanHook, A. M., and N. R. Gough. "Two-Way Adaptor." Science Signaling 1, no. 20 (May 20, 2008): ec190-ec190. http://dx.doi.org/10.1126/stke.120ec190.

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6

Luo, Leo Y., and William C. Hahn. "Oncogenic Signaling Adaptor Proteins." Journal of Genetics and Genomics 42, no. 10 (October 2015): 521–29. http://dx.doi.org/10.1016/j.jgg.2015.09.001.

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7

Horikawa, H. "Interaction of Synaptophysin with the AP-1 Adaptor Protein γ-Adaptin." Molecular and Cellular Neuroscience 21, no. 3 (November 2002): 454–62. http://dx.doi.org/10.1006/mcne.2002.1191.

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8

Dziurdzik, Samantha K., Björn D. M. Bean, Michael Davey, and Elizabeth Conibear. "A VPS13D spastic ataxia mutation disrupts the conserved adaptor-binding site in yeast Vps13." Human Molecular Genetics 29, no. 4 (January 15, 2020): 635–48. http://dx.doi.org/10.1093/hmg/ddz318.

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Abstract Mutations in each of the four human VPS13 (VPS13A–D) proteins are associated with distinct neurological disorders: chorea-acanthocytosis, Cohen syndrome, early-onset Parkinson’s disease and spastic ataxia. Recent evidence suggests that the different VPS13 paralogs transport lipids between organelles at different membrane contact sites. How each VPS13 isoform is targeted to organelles is not known. We have shown that the localization of yeast Vps13 protein to membranes requires a conserved six-repeat region, the Vps13 Adaptor Binding (VAB) domain, which binds to organelle-specific adaptors. Here, we use a systematic mutagenesis strategy to determine the role of each repeat in recognizing each known adaptor. Our results show that mutation of invariant asparagines in repeats 1 and 6 strongly impacts the binding of all adaptors and blocks Vps13 membrane recruitment. However, we find that repeats 5–6 are sufficient for localization and interaction with adaptors. This supports a model where a single adaptor-binding site is found in the last two repeats of the VAB domain, while VAB domain repeat 1 may influence domain conformation. Importantly, a disease-causing mutation in VPS13D, which maps to the highly conserved asparagine residue in repeat 6, blocks adaptor binding and Vps13 membrane recruitment when modeled in yeast. Our findings are consistent with a conserved adaptor binding role for the VAB domain and suggest the presence of as-yet-unidentified adaptors in both yeast and humans.

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9

Wong, W. "Zap70 as an Adaptor." Science Signaling 3, no. 150 (November 30, 2010): ec363-ec363. http://dx.doi.org/10.1126/scisignal.3150ec363.

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10

Dell’Angelica, Esteban C., Chean Eng Ooi, and Juan S. Bonifacino. "β3A-adaptin, a Subunit of the Adaptor-like Complex AP-3." Journal of Biological Chemistry 272, no. 24 (June 13, 1997): 15078–84. http://dx.doi.org/10.1074/jbc.272.24.15078.

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11

Bachmaier, K. "Regulation of autoimmunity by the molecular adaptor Cbl-b." Biomedicine & Pharmacotherapy 54, no. 4 (May 2000): 219. http://dx.doi.org/10.1016/s0753-3322(00)89029-0.

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12

Reichow, Steve L., and Gabriele Varani. "Nop10 Is a Conserved H/ACA snoRNP Molecular Adaptor†." Biochemistry 47, no. 23 (June 2008): 6148–56. http://dx.doi.org/10.1021/bi800418p.

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13

Kojima, T. "The molecular functions of the adaptor Sck/ShcB protein." Neuroscience Research 38 (2000): S67. http://dx.doi.org/10.1016/s0168-0102(00)81248-1.

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14

Capelluto, Daniel G. S., Shuyan Xiao, Sharmistha Mitra, C. Alicia Traughber, Stephanie Gomez, Mary K. Brannon, and Carla V. Finkielstein. "Molecular Mechanism of Membrane Targeting by Endosomal Adaptor Proteins." Biophysical Journal 104, no. 2 (January 2013): 65a—66a. http://dx.doi.org/10.1016/j.bpj.2012.11.399.

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15

Correale, Stefania, Luciano Pirone, Lucia Di Marcotullio, Enrico De Smaele, Azzura Greco, Daniela Mazzà, Marta Moretti, et al. "Molecular organization of the cullin E3 ligase adaptor KCTD11." Biochimie 93, no. 4 (April 2011): 715–24. http://dx.doi.org/10.1016/j.biochi.2010.12.014.

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16

Sada, Kiyonao, and Tomoko Hatani. "Adaptor Protein 3BP2 and Cherubism." Current Medicinal Chemistry 15, no. 6 (March 1, 2008): 549–54. http://dx.doi.org/10.2174/092986708783769795.

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17

Koirala, Sajjan, Huyen T. Bui, Heidi L. Schubert, Debra M. Eckert, Christopher P. Hill, Michael S. Kay, and Janet M. Shaw. "Molecular architecture of a dynamin adaptor: implications for assembly of mitochondrial fission complexes." Journal of Cell Biology 191, no. 6 (December 13, 2010): 1127–39. http://dx.doi.org/10.1083/jcb.201005046.

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Recruitment and assembly of some dynamin-related guanosine triphosphatases depends on adaptor proteins restricted to distinct cellular membranes. The yeast Mdv1 adaptor localizes to mitochondria by binding to the membrane protein Fis1. Subsequent Mdv1 binding to the mitochondrial dynamin Dnm1 stimulates Dnm1 assembly into spirals, which encircle and divide the mitochondrial compartment. In this study, we report that dimeric Mdv1 is joined at its center by a 92-Å antiparallel coiled coil (CC). Modeling of the Fis1–Mdv1 complex using available crystal structures suggests that the Mdv1 CC lies parallel to the bilayer with N termini at opposite ends bound to Fis1 and C-terminal β-propeller domains (Dnm1-binding sites) extending into the cytoplasm. A CC length of appropriate length and sequence is necessary for optimal Mdv1 interaction with Fis1 and Dnm1 and is important for proper Dnm1 assembly before membrane scission. Our results provide a framework for understanding how adaptors act as scaffolds to orient and stabilize the assembly of dynamins on membranes.

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18

Bussell, Katrin. "Death by an unusual adaptor." Nature Reviews Molecular Cell Biology 5, no. 2 (February 2004): 81. http://dx.doi.org/10.1038/nrm1324.

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19

Popova, N. V., I. E. Deyev, and A. G. Petrenko. "Clathrin-Mediated Endocytosis and Adaptor Proteins." Acta Naturae 5, no. 3 (September 15, 2013): 62–73. http://dx.doi.org/10.32607/20758251-2013-5-3-62-73.

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Macromolecules gain access to the cytoplasm of eukaryotic cells using one of several ways of which clathrin-dependent endocytosis is the most researched. Although the mechanism of clathrin-mediated endocytosis is well understood in general, novel adaptor proteins that play various roles in ensuring specific regulation of the mentioned process are being discovered all the time. This review provides a detailed account of the mechanism of clathrin-mediated internalization of activated G protein-coupled receptors, as well as a description of the major proteins involved in this process.

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20

Frew, I. J., and W. Krek. "pVHL: A Multipurpose Adaptor Protein." Science Signaling 1, no. 24 (June 17, 2008): pe30. http://dx.doi.org/10.1126/scisignal.124pe30.

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21

Cayrol, Corinne, Céline Cougoule, and Michel Wright. "The β2-adaptin clathrin adaptor interacts with the mitotic checkpoint kinase BubR1." Biochemical and Biophysical Research Communications 298, no. 5 (November 2002): 720–30. http://dx.doi.org/10.1016/s0006-291x(02)02522-6.

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22

Theos, Alexander C., Danièle Tenza, José A. Martina, Ilse Hurbain, Andrew A. Peden, Elena V. Sviderskaya, Abigail Stewart, 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 (November 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 colocalizes with each adaptor on endosomes. In AP-3-deficient melanocytes, tyrosinase accumulates inappropriately in vacuolar and multivesicular endosomes. Nevertheless, a substantial fraction still accumulates on melanosomes, concomitant with increased association with endosomal AP-1. Our data indicate that AP-3 and AP-1 function in partially redundant pathways to transfer tyrosinase from distinct endosomal subdomains to melanosomes and that the AP-3 pathway ensures that tyrosinase averts entrapment on internal membranes of forming multivesicular bodies.

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23

Haynie, Donald T. "Molecular physiology of the tensin brotherhood of integrin adaptor proteins." Proteins: Structure, Function, and Bioinformatics 82, no. 7 (April 10, 2014): 1113–27. http://dx.doi.org/10.1002/prot.24560.

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24

Aoh, Quyen L., Chao-wei Hung, and Mara C. Duncan. "Energy metabolism regulates clathrin adaptors at the trans-Golgi network and endosomes." Molecular Biology of the Cell 24, no. 6 (March 15, 2013): 832–47. http://dx.doi.org/10.1091/mbc.e12-10-0750.

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Glucose is a master regulator of cell behavior in the yeast Saccharomyces cerevisiae. It acts as both a metabolic substrate and a potent regulator of intracellular signaling cascades. Glucose starvation induces the transient delocalization and then partial relocalization of clathrin adaptors at the trans-Golgi network and endosomes. Although these localization responses are known to depend on the protein kinase A (PKA) signaling pathway, the molecular mechanism of this regulation is unknown. Here we demonstrate that PKA and the AMP-regulated kinase regulate adaptor localization through changes in energy metabolism. We show that genetic and chemical manipulation of intracellular ATP levels cause corresponding changes in adaptor localization. In permeabilized cells, exogenous ATP is sufficient to induce adaptor localization. Furthermore, we reveal distinct energy-dependent steps in adaptor localization: a step that requires the ADP-ribosylation factor ARF, an ATP-dependent step that requires the phosphatidyl-inositol-4 kinase Pik1, and third ATP-dependent step for which we provide evidence but for which the mechanism is unknown. We propose that these energy-dependent mechanisms precisely synchronize membrane traffic with overall proliferation rates and contribute a crucial aspect of energy conservation during acute glucose starvation.

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25

Hung, Chao-Wei, and Mara C. Duncan. "Clathrin binding by the adaptor Ent5 promotes late stages of clathrin coat maturation." Molecular Biology of the Cell 27, no. 7 (April 2016): 1143–53. http://dx.doi.org/10.1091/mbc.e15-08-0588.

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Clathrin is a ubiquitous protein that mediates membrane traffic at many locations. To function, clathrin requires clathrin adaptors that link it to transmembrane protein cargo. In addition to this cargo selection function, many adaptors also play mechanistic roles in the formation of the transport carrier. However, the full spectrum of these mechanistic roles is poorly understood. Here we report that Ent5, an endosomal clathrin adaptor in Saccharomyces cerevisiae, regulates the behavior of clathrin coats after the recruitment of clathrin. We show that loss of Ent5 disrupts clathrin-dependent traffic and prolongs the lifespan of endosomal structures that contain clathrin and other adaptors, suggesting a defect in coat maturation at a late stage. We find that the direct binding of Ent5 with clathrin is required for its role in coat behavior and cargo traffic. Surprisingly, the interaction of Ent5 with other adaptors is dispensable for coat behavior but not cargo traffic. These findings support a model in which Ent5 clathrin binding performs a mechanistic role in coat maturation, whereas Ent5 adaptor binding promotes cargo incorporation.

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26

Liu, Yong, Lingxuan Li, Cong Yu, Fuxing Zeng, Fengfeng Niu, and Zhiyi Wei. "Cargo Recognition Mechanisms of Yeast Myo2 Revealed by AlphaFold2-Powered Protein Complex Prediction." Biomolecules 12, no. 8 (July 26, 2022): 1032. http://dx.doi.org/10.3390/biom12081032.

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Myo2, a yeast class V myosin, transports a broad range of organelles and plays important roles in various cellular processes, including cell division in budding yeast. Despite the fact that several structures of Myo2/cargo adaptor complexes have been determined, the understanding of the versatile cargo-binding modes of Myo2 is still very limited, given the large number of cargo adaptors identified for Myo2. Here, we used ColabFold, an AlphaFold2-powered and easy-to-use tool, to predict the complex structures of Myo2-GTD and its several cargo adaptors. After benchmarking the prediction strategy with three Myo2/cargo adaptor complexes that have been determined previously, we successfully predicted the atomic structures of Myo2-GTD in complex with another three cargo adaptors, Vac17, Kar9 and Pea2, which were confirmed by our biochemical characterizations. By systematically comparing the interaction details of the six complexes of Myo2 and its cargo adaptors, we summarized the cargo-binding modes on the three conserved sites of Myo2-GTD, providing an overall picture of the versatile cargo-recognition mechanisms of Myo2. In addition, our study demonstrates an efficient and effective solution to study protein–protein interactions in the future via the AlphaFold2-powered prediction.

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27

Geng, Liping, and Christopher Rudd. "Adaptor ADAP (Adhesion- and Degranulation-Promoting Adaptor Protein) Regulates β1 Integrin Clustering on Mast Cells." Biochemical and Biophysical Research Communications 289, no. 5 (December 2001): 1135–40. http://dx.doi.org/10.1006/bbrc.2001.6117.

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28

Kouvela, Adamantia, Apostolos Zaravinos, and Vassiliki Stamatopoulou. "Adaptor Molecules Epitranscriptome Reprograms Bacterial Pathogenicity." International Journal of Molecular Sciences 22, no. 16 (August 5, 2021): 8409. http://dx.doi.org/10.3390/ijms22168409.

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The strong decoration of tRNAs with post-transcriptional modifications provides an unprecedented adaptability of this class of non-coding RNAs leading to the regulation of bacterial growth and pathogenicity. Accumulating data indicate that tRNA post-transcriptional modifications possess a central role in both the formation of bacterial cell wall and the modulation of transcription and translation fidelity, but also in the expression of virulence factors. Evolutionary conserved modifications in tRNA nucleosides ensure the proper folding and stability redounding to a totally functional molecule. However, environmental factors including stress conditions can cause various alterations in tRNA modifications, disturbing the pathogen homeostasis. Post-transcriptional modifications adjacent to the anticodon stem-loop, for instance, have been tightly linked to bacterial infectivity. Currently, advances in high throughput methodologies have facilitated the identification and functional investigation of such tRNA modifications offering a broader pool of putative alternative molecular targets and therapeutic avenues against bacterial infections. Herein, we focus on tRNA epitranscriptome shaping regarding modifications with a key role in bacterial infectivity including opportunistic pathogens of the human microbiome.

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29

Gentry, Schuyler B., Scott J. Nowak, Xuelei Ni, Stephanie A. Hill, Lydia R. Wade, William R. Clark, Aidan P. Keelaghan, Daniel P. Morris, and Jonathan L. McMurry. "A real-time assay for cell-penetrating peptide-mediated delivery of molecular cargos." PLOS ONE 16, no. 9 (September 2, 2021): e0254468. http://dx.doi.org/10.1371/journal.pone.0254468.

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Cell-penetrating peptides (CPPs) are capable of transporting molecules to which they are tethered across cellular membranes. Unsurprisingly, CPPs have attracted attention for their potential drug delivery applications, but several technical hurdles remain to be overcome. Chief among them is the so-called ‘endosomal escape problem,’ i.e. the propensity of CPP-cargo molecules to be endocytosed but remain entrapped in endosomes rather than reaching the cytosol. Previously, a CPP fused to calmodulin that bound calmodulin binding site-containing cargos was shown to efficiently deliver cargos to the cytoplasm, effectively overcoming the endosomal escape problem. The CPP-adaptor, “TAT-CaM,” evinces delivery at nM concentrations and more rapidly than we had previously been able to measure. To better understand the kinetics and mechanism of CPP-adaptor-mediated cargo delivery, a real-time cell penetrating assay was developed in which a flow chamber containing cultured cells was installed on the stage of a confocal microscope to allow for observation ab initio. Also examined in this study was an improved CPP-adaptor that utilizes naked mole rat (Heterocephalus glaber) calmodulin in place of human and results in superior internalization, likely due to its lesser net negative charge. Adaptor-cargo complexes were delivered into the flow chamber and fluorescence intensity in the midpoint of baby hamster kidney cells was measured as a function of time. Delivery of 400 nM cargo was observed within seven minutes and fluorescence continued to increase linearly as a function of time. Cargo-only control experiments showed that the minimal uptake which occurred independently of the CPP-adaptor resulted in punctate localization consistent with endosomal entrapment. A distance analysis was performed for cell-penetration experiments in which CPP-adaptor-delivered cargo showing wider dispersions throughout cells as compared to an analogous covalently-bound CPP-cargo. Small molecule endocytosis inhibitors did not have significant effects upon delivery. The real-time assay is an improvement upon static endpoint assays and should be informative in a broad array of applications.

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30

Hrdinka, M., and V. Horejsi. "PAG - a multipurpose transmembrane adaptor protein." Oncogene 33, no. 41 (November 11, 2013): 4881–92. http://dx.doi.org/10.1038/onc.2013.485.

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31

Waterston, Anthony. "Molecular basis of inflammasome adaptor inhibition by the ASC-C isoform." Biophysical Journal 121, no. 3 (February 2022): 450a—451a. http://dx.doi.org/10.1016/j.bpj.2021.11.512.

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32

Xiong, Wen, Ji Woong Choi, Xiaolin Zhao, Jeff F. Ellena, and Daniel G. S. Capelluto. "Molecular Basis of Ligand Binding by the Endosomal Adaptor Protein Tom1." Biophysical Journal 112, no. 3 (February 2017): 529a. http://dx.doi.org/10.1016/j.bpj.2016.11.2862.

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33

Percario, Zulema Antonia, Muhammad Ali, Giorgio Mangino, and Elisabetta Affabris. "Nef, the shuttling molecular adaptor of HIV, influences the cytokine network." Cytokine & Growth Factor Reviews 26, no. 2 (April 2015): 159–73. http://dx.doi.org/10.1016/j.cytogfr.2014.11.010.

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34

Meyer, Christoph, and Maja Köhn. "A Molecular Tête-à-Tête Arranged by a Designed Adaptor Protein." Angewandte Chemie International Edition 51, no. 33 (July 13, 2012): 8160–62. http://dx.doi.org/10.1002/anie.201203345.

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Novoselova, Tatiana V., Kiran Zahira, Ruth-Sarah Rose, and James A. Sullivan. "Bul Proteins, a Nonredundant, Antagonistic Family of Ubiquitin Ligase Regulatory Proteins." Eukaryotic Cell 11, no. 4 (February 3, 2012): 463–70. http://dx.doi.org/10.1128/ec.00009-12.

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ABSTRACT Like other Nedd4 ligases, Saccharomyces cerevisiae E3 Rsp5p utilizes adaptor proteins to interact with some substrates. Previous studies have indentified Bul1p and Bul2p as adaptor proteins that facilitate the ligase-substrate interaction. Here, we show the identification of a third member of the Bul family, Bul3p, the product of two adjacent open reading frames separated by a stop codon that undergoes readthrough translation. Combinatorial analysis of BUL gene deletions reveals that they regulate some, but not all, of the cellular pathways known to involve Rsp5p. Surprisingly, we find that Bul proteins can act antagonistically to regulate the same ubiquitin-dependent process, and the nature of this antagonistic activity varies between different substrates. We further show, using in vitro ubiquitination assays, that the Bul proteins have different specificities for WW domains and that the two forms of Bul3p interact differently with Rsp5p, potentially leading to alternate functional outcomes. These data introduce a new level of complexity into the regulatory interactions that take place between Rsp5p and its adaptors and substrates and suggest a more critical role for the Bul family of proteins in controlling adaptor-mediated ubiquitination.

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36

Jozic, Daniela, Nayra Cárdenes, Yonathan Lissanu Deribe, Gabriel Moncalián, Daniela Hoeller, Yvonne Groemping, Ivan Dikic, Katrin Rittinger, and Jerónimo Bravo. "Cbl promotes clustering of endocytic adaptor proteins." Nature Structural & Molecular Biology 12, no. 11 (October 9, 2005): 972–79. http://dx.doi.org/10.1038/nsmb1000.

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37

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 (November 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 clathrin. Individual or combined disruption of AP-1 subunit genes in cells expressing a temperature-sensitive clathrin heavy chain results in accentuated growth and α-factor pheromone maturation defects, providing further evidence that AP-1 is a clathrin adaptor complex. However, in cells expressing wild-type clathrin, the same AP subunit deletions have no effect on growth or α-factor maturation. Furthermore, gel filtration chromatography revealed normal elution patterns of clathrin-coated vesicles in cells lacking AP-1. Similarly, combined deletion of genes encoding the β subunits of the three AP complexes did not produce defects in clathrin-dependent sorting in the endocytic and vacuolar pathways or alterations in gel filtration profiles of clathrin-coated vesicles. We conclude that AP complexes are dispensable for clathrin function in S. cerevisiae under normal conditions. Our results suggest that alternative factors assume key roles in stimulating clathrin coat assembly and cargo selection during clathrin-mediated vesicle formation in yeast.

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38

McDonald, Caleb B., Kenneth L. Seldeen, Brian J. Deegan, Marc S. Lewis, and Amjad Farooq. "Grb2 adaptor undergoes conformational change upon dimerization." Archives of Biochemistry and Biophysics 475, no. 1 (July 2008): 25–35. http://dx.doi.org/10.1016/j.abb.2008.04.008.

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39

Knuehl, Christine, and Frances M. Brodsky. "The long and short of adaptor appendages." Nature Structural & Molecular Biology 10, no. 8 (August 2003): 580–82. http://dx.doi.org/10.1038/nsb0803-580.

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40

Katahira, Jun, Hitomi Inoue, Ed Hurt, and Yoshihiro Yoneda. "Adaptor Aly and co-adaptor Thoc5 function in the Tap-p15-mediated nuclear export of HSP70 mRNA." EMBO Journal 28, no. 5 (January 22, 2009): 556–67. http://dx.doi.org/10.1038/emboj.2009.5.

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41

Snyder, Greg, Jiansheng Jiang, Kang Chen, Theresa Fresquez, Patrick Smith, Nathaniel Snyder, Timothy Luchetti, et al. "Structural studies of Toll like receptor signaling adaptors. (136.45)." Journal of Immunology 184, no. 1_Supplement (April 1, 2010): 136.45. http://dx.doi.org/10.4049/jimmunol.184.supp.136.45.

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Abstract Signaling downstream of the Toll like receptors (TLRs) involves Toll-IL-1R homology (TIR) domains as well as recruitment of critical signaling adaptors MyD88 and TIRAP/Mal. Studies in human patients, dominant negative mutants and knockout mice have shown that mutations in Arg196, the BB loop, DD loop, “Poc” site Ile179 are critical for MyD88 TIR domain signaling and appropriate responses to pathogen stimuli. We previously reported the structure of MyD88 TIR domain that showed a unique conformation for its BB loop, as well as a crystallographic lattice that reveals interactions between the BB-DD and BB-EE loops. We now report additional crystal forms which retain BB-DD and BB-EE interactions as well as extend the resolution to 1.4 Å. A yeast two-hybrid analysis of the domain interface residues observed from the crystal structure lattice shows that key residues including the human Arg196Cys mutation are critically important for homotypic TIR domain binding. Additionally, we report NMR solution studies showing binding between MyD88 and bacterial TIR domain protein TcpC, which has been demonstrated to negatively regulate MyD88-dependent TLR adaptor signaling. Finally, we report the X-ray structure of a second critical TIR adaptor protein, TIRAP/Mal. We observe key residues and loops important for TIRAP/Mal adaptor function. Structural insights from these studies may aid our understanding of the molecular mechanisms by which TLRs and TIR domain adaptors interact and signal.

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42

Teber, Iskender, Fumiko Nagano, Joachim Kremerskothen, Konstantinos Bilbilis, Bruno Goud, and Angelika Barnekow. "Rab6 interacts with the mint3 adaptor protein." Biological Chemistry 386, no. 7 (July 1, 2005): 671–77. http://dx.doi.org/10.1515/bc.2005.078.

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Abstract The Rab6 GTPase regulates a retrograde transport route connecting endosomes and the endoplasmic reticulum (ER) via the Golgi apparatus. Recently it was shown that active (GTP-loaded) Rab6A regulates intracellular processing of the amyloid precursor protein (APP). To characterize the role of Rab6A in APP trafficking and to identify effector proteins of the active Rab6A protein, we screened a human placenta cDNA library using the yeast two-hybrid system. We isolated an interacting cDNA clone encoding part of the adaptor protein mint3. The interaction between Rab6A and mint3 is GTP-dependent and requires the complete phosphotyrosine-binding (PTB) domain of the mint protein, which also mediates the association with APP. By confocal microscopy we show that Rab6A, mint3 and APP co-localize at Golgi membranes in HeLa cells. Density gradient centrifugation of cytosolic extracts confirms a common distribution of these three proteins. Our data suggest that mint3 links Rab6A to APP traffic.

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Zhang, Fang, Yang-In Yim, Sarah Scarselletta, Mark Norton, Evan Eisenberg, and Lois E. Greene. "Clathrin Adaptor GGA1 Polymerizes Clathrin into Tubules." Journal of Biological Chemistry 282, no. 18 (March 6, 2007): 13282–89. http://dx.doi.org/10.1074/jbc.m700936200.

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44

Schaller, Michael D. "Paxillin: a focal adhesion-associated adaptor protein." Oncogene 20, no. 44 (October 2001): 6459–72. http://dx.doi.org/10.1038/sj.onc.1204786.

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45

Okabayashi, Yoshinori, Yutaka Sugimoto, Nicholas F. Totty, Justin Hsuan, Yoshiaki Kido, Kazuhiko Sakaguchi, Ivan Gout, Michael D. Waterfield, and Masato Kasuga. "Interaction of Shc with Adaptor Protein Adaptins." Journal of Biological Chemistry 271, no. 9 (March 1996): 5265–69. http://dx.doi.org/10.1074/jbc.271.9.5265.

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46

Borah, Supriya, and Neil A. Bhowmick. "The adaptor protein SHCA launches cancer invasion." Journal of Biological Chemistry 295, no. 31 (July 31, 2020): 10560–61. http://dx.doi.org/10.1074/jbc.h120.014283.

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Cancer cell invasion and metastasis rely on invadopodia, important extensions of the cytoskeleton that initiate degradation of the basement membrane that holds a cell in place. Transforming growth factor-β (TGF-β) is well-known to induce breast cancer migration and invasion, but the mechanism by which TGF-β signaling converts into cell motility is not completely understood. A study from Kiepas et al. revealed a new TGF-β–dependent role for Src homology/collagen adaptor protein (SHCA) in the initiation of dynamic adhesion complexes involved in the formation of invadopodia. These results highlight new therapeutic opportunities for cancer patients that are not sensitive to HER2 antagonists.

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Smits, Veronique A. J., Elisa Cabrera, Raimundo Freire, and David A. Gillespie. "Claspin – checkpoint adaptor and DNA replication factor." FEBS Journal 286, no. 3 (June 29, 2018): 441–55. http://dx.doi.org/10.1111/febs.14594.

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Lherbette, Michael, Lisa Redlingshöfer, Frances M. Brodsky, Iwan A. T. Schaap, and Philip N. Dannhauser. "The AP2 adaptor enhances clathrin coat stiffness." FEBS Journal 286, no. 20 (July 3, 2019): 4074–85. http://dx.doi.org/10.1111/febs.14961.

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Cuneo, Matthew J., and Tanja Mittag. "The ubiquitin ligase adaptor SPOP in cancer." FEBS Journal 286, no. 20 (September 18, 2019): 3946–58. http://dx.doi.org/10.1111/febs.15056.

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Popova, Nadezhda V., Igor E. Deyev, and Alexander G. Petrenko. "Association of adaptor protein TRIP8b with clathrin." Journal of Neurochemistry 118, no. 6 (August 12, 2011): 988–98. http://dx.doi.org/10.1111/j.1471-4159.2011.07384.x.

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