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Journal articles on the topic 'Expressed Protein Ligation (EPL)'

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Published: 9 March 2023

Last updated: 10 March 2023

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1

Flavell, Robert R., and Tom W. Muir. "Expressed Protein Ligation (EPL) in the Study of Signal Transduction, Ion Conduction, And Chromatin Biology." Accounts of Chemical Research 42, no. 1 (January 20, 2009): 107–16. http://dx.doi.org/10.1021/ar800129c.

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2

Westerlind, Ulrika. "Synthetic glycopeptides and glycoproteins with applications in biological research." Beilstein Journal of Organic Chemistry 8 (May 30, 2012): 804–18. http://dx.doi.org/10.3762/bjoc.8.90.

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Over the past few years, synthetic methods for the preparation of complex glycopeptides have been drastically improved. The need for homogenous glycopeptides and glycoproteins with defined chemical structures to study diverse biological phenomena further enhances the development of methodologies. Selected recent advances in synthesis and applications, in which glycopeptides or glycoproteins serve as tools for biological studies, are reviewed. The importance of specific antibodies directed to the glycan part, as well as the peptide backbone has been realized during the development of synthetic glycopeptide-based anti-tumor vaccines. The fine-tuning of native chemical ligation (NCL), expressed protein ligation (EPL), and chemoenzymatic glycosylation techniques have all together enabled the synthesis of functional glycoproteins. The synthesis of structurally defined, complex glycopeptides or glyco-clusters presented on natural peptide backbones, or mimics thereof, offer further possibilities to study protein-binding events.

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3

Jing, Yihang, Dongbo Ding, Gaofei Tian, Ka Chun Jonathan Kwan, Zheng Liu, Toyotaka Ishibashi, and Xiang David Li. "Semisynthesis of site-specifically succinylated histone reveals that succinylation regulates nucleosome unwrapping rate and DNA accessibility." Nucleic Acids Research 48, no. 17 (August 7, 2020): 9538–49. http://dx.doi.org/10.1093/nar/gkaa663.

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Abstract Posttranslational modifications (PTMs) of histones represent a crucial regulatory mechanism of nucleosome and chromatin dynamics in various of DNA-based cellular processes, such as replication, transcription and DNA damage repair. Lysine succinylation (Ksucc) is a newly identified histone PTM, but its regulation and function in chromatin remain poorly understood. Here, we utilized an expressed protein ligation (EPL) strategy to synthesize histone H4 with site-specific succinylation at K77 residue (H4K77succ), an evolutionarily conserved succinylation site at the nucleosomal DNA-histone interface. We then assembled mononucleosomes with the semisynthetic H4K77succ in vitro. We demonstrated that this succinylation impacts nucleosome dynamics and promotes DNA unwrapping from the histone surface, which allows proteins such as transcription factors to rapidly access buried regions of the nucleosomal DNA. In budding yeast, a lysine-to-glutamic acid mutation, which mimics Ksucc, at the H4K77 site reduced nucleosome stability and led to defects in DNA damage repair and telomere silencing in vivo. Our findings revealed this uncharacterized histone modification has important roles in nucleosome and chromatin dynamics.

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4

Zasłona, Zbigniew, Carlos H. Serezani, Katsuhide Okunishi, David M. Aronoff, and Marc Peters-Golden. "Prostaglandin E2 restrains macrophage maturation via E prostanoid receptor 2/protein kinase A signaling." Blood 119, no. 10 (March 8, 2012): 2358–67. http://dx.doi.org/10.1182/blood-2011-08-374207.

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Abstract Prostaglandin E2 (PGE2) is a lipid mediator that acts by ligating 4 distinct G protein–coupled receptors, E prostanoid (EP) 1 to 4. Previous studies identified the importance of PGE2 in regulating macrophage functions, but little is known about its effect on macrophage maturation. Macrophage maturation was studied in vitro in bone marrow cell cultures, and in vivo in a model of peritonitis. EP2 was the most abundant PGE2 receptor expressed by bone marrow cells, and its expression further increased during macrophage maturation. EP2-deficient (EP2−/−) macrophages exhibited enhanced in vitro maturation compared with wild-type cells, as evidenced by higher F4/80 expression. An EP2 antagonist also increased maturation. In the peritonitis model, EP2−/− mice exhibited a higher percentage of F4/80high/CD11bhigh cells and greater expression of macrophage colony-stimulating factor receptor (M-CSFR) in both the blood and the peritoneal cavity. Subcutaneous injection of the PGE2 analog misoprostol decreased M-CSFR expression in bone marrow cells and reduced the number of peritoneal macrophages in wild-type mice but not EP2−/− mice. The suppressive effect of EP2 ligation on in vitro macrophage maturation was mimicked by a selective protein kinase A agonist. Our findings reveal a novel role for PGE2/EP2/protein kinase A signaling in the suppression of macrophage maturation.

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5

Pujianto, Dwi Ari, Andika Setyoadi, and Asmarinah ,. "Study of Expression and Regulation of Mouse Beta-Defensin 2 as a Model for Understanding Its Role in the Process of Sperm Maturation." Jurnal Biotek Medisiana Indonesia 9, no. 2 (February 5, 2021): 128–38. http://dx.doi.org/10.22435/jbmi.v9i2.4417.

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Abstrak Beberapa gen yang terekspresi spesfik di epididimis diduga terlibat dalam proses pematangan sperma. Ekspresi gen spesifik di epididimis dipengaruhi oleh androgen, faktor testikuler, dan terekspresi pada masa pubertas. Famili gen yang cukup banyak ditemukan terekspresi di epididimis adalah beta-defensin, salah satunya yaitu beta-defensin 2 (Defb2). Penelitian ini bertujuan untuk mengkarakterisasi gen Defb2 terkait dengan perannya pada proses pematangan sperma. Analisis bioinformatika digunakan pada penelitian ini untuk mendapatkan informasi mengenai struktur gen, signal peptide, dan domain fungsional pada gen Defb2. Analisis quantitative reverse transcriptase-Polymerase Chain Reaction (qRT-PCR) untuk mengetahui ekspresi relatif gen Defb2. Hasil yang diperoleh yaitu Defb2 merupakan protein sekretori karena memiliki signal peptide. Defb2 memiliki domain fungsional berupa N-myristoylation dan protein kinase-C. Gen Defb2 terekspresi spesifik di epididimis. Ekspresi Defb2 dipengaruhi oleh androgen dan faktor testikuler terbukti setelah perlakuan gonadektomi dan efferent duct ligation (EDL) terjadi penurunan ekspresi Defb2. Adapun pada analisis postnatal development terlihat ekspresi gen Defb2 mulai terdeteksi pada hari ke-15 yang merupakan masa pubertas mencit jantan. Kata kunci: androgen, beta-defensin 2 (Defb2), epididimis, pematangan sperma Abstract Several specific genes expressed in the epididymis are thought to be involved in the sperm maturation process. Their specific expression in the epididymis are influenced by androgens, testicular factors, and increased expression at puberty. A family of genes that are commonly found expressed in the epididymis is beta-defensin, one of which is beta-defensin 2 (Defb2). This study was aimed to characterize the Defb2 gene related to its role in the sperm maturation process. Bioinformatics analysis was used in this study to obtain information about gene structure, signal peptides, and functional domains in the Defb2 gene. The quantitative reverse transcriptase-polymerase chain reaction (qRT-PCR) analysis was used to determine relative expression of the Defb2 gene. The results showed Defb2 was a secretory protein because it has a signal peptide. Defb2 has a functional domain in the form of N-myristoylation and protein kinase-C. Defb2 gene was specifically expressed in the epididymis. Defb2 expression was influenced by androgens and testicular factors that were proven by post gonadectomy and efferent duct ligation (EDL) decreases in Defb2 expression. As for the postnatal development analysis, the expression of Defb2 gene was initially detected on day 15 which is the puberty of male mice. Keywords: androgen, beta-defensin 2 (Defb2), epididymis, sperm maturation

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6

David, Ralf, Michael P. O. Richter, and Annette G. Beck-Sickinger. "Expressed protein ligation." European Journal of Biochemistry 271, no. 4 (January 27, 2004): 663–77. http://dx.doi.org/10.1111/j.1432-1033.2004.03978.x.

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7

Henager, Samuel H., Nam Chu, Zan Chen, David Bolduc, Daniel R. Dempsey, Yousang Hwang, James Wells, and Philip A. Cole. "Enzyme-catalyzed expressed protein ligation." Nature Methods 13, no. 11 (September 26, 2016): 925–27. http://dx.doi.org/10.1038/nmeth.4004.

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8

Qiao, Yuchen, Ge Yu, Kaci C. Kratch, Xiaoyan Aria Wang, Wesley Wei Wang, Sunshine Z. Leeuwon, Shiqing Xu, Jared S. Morse, and Wenshe Ray Liu. "Expressed Protein Ligation without Intein." Journal of the American Chemical Society 142, no. 15 (March 26, 2020): 7047–54. http://dx.doi.org/10.1021/jacs.0c00252.

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9

Kamei, Ayako, Paul S. Hauser, Jennifer A. Beckstead, Paul M. M. Weers, and Robert O. Ryan. "Expressed protein ligation-mediated template protein extension." Protein Expression and Purification 83, no. 2 (June 2012): 113–16. http://dx.doi.org/10.1016/j.pep.2012.03.014.

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10

Hondal, Robert J., Bradley L. Nilsson, and Ronald T. Raines. "Selenocysteine in Native Chemical Ligation and Expressed Protein Ligation." Journal of the American Chemical Society 123, no. 21 (May 2001): 5140–41. http://dx.doi.org/10.1021/ja005885t.

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11

Karagoz, G. E., T. Sinnige, O. Hsieh, and S. G. D. Rudiger. "Expressed protein ligation for a large dimeric protein." Protein Engineering Design and Selection 24, no. 6 (February 18, 2011): 495–501. http://dx.doi.org/10.1093/protein/gzr007.

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12

Muir, Tom W. "Semisynthesis of Proteins by Expressed Protein Ligation." Annual Review of Biochemistry 72, no. 1 (June 2003): 249–89. http://dx.doi.org/10.1146/annurev.biochem.72.121801.161900.

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13

Muir, Tom W. "Development and Application of Expressed Protein Ligation." Synlett 2001, no. 06 (2001): 0733–40. http://dx.doi.org/10.1055/s-2001-14577.

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14

Vila-Perelló, Miquel, Zhihua Liu, Neel H. Shah, John A. Willis, Juliana Idoyaga, and Tom W. Muir. "Streamlined Expressed Protein Ligation Using Split Inteins." Journal of the American Chemical Society 135, no. 1 (December 24, 2012): 286–92. http://dx.doi.org/10.1021/ja309126m.

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15

Muir, T. W., D. Sondhi, and P. A. Cole. "Expressed protein ligation: A general method for protein engineering." Proceedings of the National Academy of Sciences 95, no. 12 (June 9, 1998): 6705–10. http://dx.doi.org/10.1073/pnas.95.12.6705.

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16

Lovrinovic, Marina, Ralf Seidel, Ron Wacker, Hendrik Schroeder, Oliver Seitz, Martin Engelhard, Roger S. Goody, and Christof M. Niemeyer. "Synthesis of protein–nucleic acid conjugates by expressed protein ligation." Chemical Communications, no. 7 (March 10, 2003): 822–23. http://dx.doi.org/10.1039/b212294d.

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17

Lovrinovic, Marina, Mark Spengler, Carl Deutsch, and Christof M. Niemeyer. "Synthesis of covalent DNA–protein conjugates by expressed protein ligation." Molecular BioSystems 1, no. 1 (2005): 64. http://dx.doi.org/10.1039/b503839a.

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18

Schwarzer, Dirk, and Philip A. Cole. "Protein semisynthesis and expressed protein ligation: chasing a protein's tail." Current Opinion in Chemical Biology 9, no. 6 (December 2005): 561–69. http://dx.doi.org/10.1016/j.cbpa.2005.09.018.

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19

Liu, Jun, Qingqing Chen, and Sharon Rozovsky. "Utilizing Selenocysteine for Expressed Protein Ligation and Bioconjugations." Journal of the American Chemical Society 139, no. 9 (February 27, 2017): 3430–37. http://dx.doi.org/10.1021/jacs.6b10991.

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20

Ziaco, Barbara, Soccorsa Pensato, Luca D. D’Andrea, Ettore Benedetti, and Alessandra Romanelli. "Semisynthesis of Dimeric Proteins by Expressed Protein Ligation." Organic Letters 10, no. 10 (May 2008): 1955–58. http://dx.doi.org/10.1021/ol800457g.

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21

Focke, Paul J., and Francis I. Valiyaveetil. "Studies of ion channels using expressed protein ligation." Current Opinion in Chemical Biology 14, no. 6 (December 2010): 797–802. http://dx.doi.org/10.1016/j.cbpa.2010.09.014.

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22

Conibear, Anne C., Emma E. Watson, Richard J. Payne, and Christian F. W. Becker. "Native chemical ligation in protein synthesis and semi-synthesis." Chemical Society Reviews 47, no. 24 (2018): 9046–68. http://dx.doi.org/10.1039/c8cs00573g.

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23

Tam, Annie, Matthew B. Soellner, and Ronald T. Raines. "Water-Soluble Phosphinothiols for Traceless Staudinger Ligation and Integration with Expressed Protein Ligation." Journal of the American Chemical Society 129, no. 37 (September 2007): 11421–30. http://dx.doi.org/10.1021/ja073204p.

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24

Tanaka, Tomohiro, Anne M. Wagner, John B. Warner, Yanxin J. Wang, and E. James Petersson. "Expressed Protein Ligation at Methionine: N-Terminal Attachment of Homocysteine, Ligation, and Masking." Angewandte Chemie International Edition 52, no. 24 (April 29, 2013): 6210–13. http://dx.doi.org/10.1002/anie.201302065.

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25

Tanaka, Tomohiro, Anne M. Wagner, John B. Warner, Yanxin J. Wang, and E. James Petersson. "Expressed Protein Ligation at Methionine: N-Terminal Attachment of Homocysteine, Ligation, and Masking." Angewandte Chemie 125, no. 24 (April 29, 2013): 6330–33. http://dx.doi.org/10.1002/ange.201302065.

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26

Muir, Tom W. "ChemInform Abstract: Development and Application of Expressed Protein Ligation." ChemInform 32, no. 34 (May 25, 2010): no. http://dx.doi.org/10.1002/chin.200134275.

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27

Severinov, Konstantin, and Tom W. Muir. "Expressed Protein Ligation, a Novel Method for Studying Protein-Protein Interactions in Transcription." Journal of Biological Chemistry 273, no. 26 (June 26, 1998): 16205–9. http://dx.doi.org/10.1074/jbc.273.26.16205.

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28

Pickin, Kerry A., Sidhartha Chaudhury, Blair C. R. Dancy, Jeffrey J. Gray, and Philip A. Cole. "Analysis of Protein Kinase Autophosphorylation Using Expressed Protein Ligation and Computational Modeling." Journal of the American Chemical Society 130, no. 17 (April 2008): 5667–69. http://dx.doi.org/10.1021/ja711244h.

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29

Hofmann, Roseanne M., and Tom W. Muir. "Recent advances in the application of expressed protein ligation to protein engineering." Current Opinion in Biotechnology 13, no. 4 (August 2002): 297–303. http://dx.doi.org/10.1016/s0958-1669(02)00326-9.

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30

Berrade, Luis, and Julio A. Camarero. "Expressed protein ligation: a resourceful tool to study protein structure and function." Cellular and Molecular Life Sciences 66, no. 24 (August 15, 2009): 3909–22. http://dx.doi.org/10.1007/s00018-009-0122-3.

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31

Scheibner, Kara A., Zhongsen Zhang, and Philip A. Cole. "Merging fluorescence resonance energy transfer and expressed protein ligation to analyze protein–protein interactions." Analytical Biochemistry 317, no. 2 (June 2003): 226–32. http://dx.doi.org/10.1016/s0003-2697(03)00087-3.

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32

Richter, Michael, and Annette Beck-Sickinger. "Expressed Protein Ligation to Obtain Selectively Modified Aldo/Keto Reductases." Protein & Peptide Letters 12, no. 8 (November 1, 2005): 777–81. http://dx.doi.org/10.2174/0929866054864210.

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33

Frutos, Silvia, Jose Luis Hernández, Anabel Otero, Carme Calvis, Jaume Adan, Francesc Mitjans, and Miquel Vila-Perelló. "Site-Specific Antibody Drug Conjugates Using Streamlined Expressed Protein Ligation." Bioconjugate Chemistry 29, no. 11 (October 22, 2018): 3503–8. http://dx.doi.org/10.1021/acs.bioconjchem.8b00630.

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34

Lovrinovic, Marina, and Christof M. Niemeyer. "Rapid synthesis of DNA–cysteine conjugates for expressed protein ligation." Biochemical and Biophysical Research Communications 335, no. 3 (September 2005): 943–48. http://dx.doi.org/10.1016/j.bbrc.2005.08.001.

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35

Budisa, Nediljko. "Adding New Tools to the Arsenal of Expressed Protein Ligation." ChemBioChem 5, no. 9 (September 2, 2004): 1176–79. http://dx.doi.org/10.1002/cbic.200400141.

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36

De Rosa, Lucia, Aitziber L. Cortajarena, Alessandra Romanelli, Lynne Regan, and Luca Domenico D'Andrea. "Site-specific protein double labeling by expressed protein ligation: applications to repeat proteins." Org. Biomol. Chem. 10, no. 2 (2012): 273–80. http://dx.doi.org/10.1039/c1ob06397a.

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37

Lovrinovic, Marina, Ljiljana Fruk, Hendrik Schröder, and Christof M. Niemeyer. "Site-specific labeling of DNA–protein conjugates by means of expressed protein ligation." Chem. Commun., no. 4 (2007): 353–55. http://dx.doi.org/10.1039/b614978b.

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38

Anderson, Lori, Garland Marshall, and Thomas Baranski. "Expressed Protein Ligation to Study Protein Interactions: Semi-Synthesis of the G-Protein Alpha Subunit." Protein & Peptide Letters 12, no. 8 (November 1, 2005): 783–87. http://dx.doi.org/10.2174/0929866054864175.

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39

Wang, Yanxin J., D. Miklos Szantai-Kis, and E. James Petersson. "Semi-synthesis of thioamide containing proteins." Organic & Biomolecular Chemistry 13, no. 18 (2015): 5074–81. http://dx.doi.org/10.1039/c5ob00224a.

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To make thioamide protein folding experiments applicable to full-sized proteins, our laboratory has used a combination of native chemical ligation of thiopeptide fragments, unnatural amino acid mutagenesis to install fluorophore partners in expressed protein fragments, and chemoenzymatic protein modification to render these expressed protein ligations traceless.

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40

Ayers, Brenda, Ulrich K. Blaschke, Julio A. Camarero, Graham J. Cotton, Mande Holford, and Tom W. Muir. "Introduction of unnatural amino acids into proteins using expressed protein ligation." Biopolymers 51, no. 5 (1999): 343–54. http://dx.doi.org/10.1002/(sici)1097-0282(1999)51:5<343::aid-bip4>3.0.co;2-w.

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41

Gurung, Sadeechya. "Abstract 998: Extracellular proximity labeling (ePL) as a tool to identify protein-protein interactions in the tumor microenvironment." Cancer Research 82, no. 12_Supplement (June 15, 2022): 998. http://dx.doi.org/10.1158/1538-7445.am2022-998.

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Abstract The extracellular matrix (ECM) is a dynamic niche that is extensively reshaped in the development of the tumor microenvironment (TME). Our current understanding of ECM function and dynamics is largely informed by identification of protein-protein interactions (PPIs) using co-immunoprecipitation (co-IP) techniques that may miss transient and weak/unstable interactions. Recent advances in proximity labeling techniques have greatly expanded the interactome networks of numerous intracellular proteins, however these tools have yet to be extended to study PPIs in the ECM. We have recently optimized a systematic approach to identify PPIs in the ECM using fusion constructs of the biotinylating enzymes, BioID2 and TurboID, with the widely expressed matrix regulator TIMP2. BioID2 and TurboID offer differing reaction kinetics that may provide complimentary information on extracellular PPIs (ePPIs). Matrix metalloproteinases (MMPs) and their endogenous inhibitors, tissue inhibitors of metalloproteinases (TIMPs) are crucial regulators of ECM structure and composition. TIMPs are widely expressed multifunctional proteins that serve to promote ECM homeostasis that is often perturbed in many cancers and chronic disorders. Although biochemical data suggests that TIMPs are promiscuous proteins, the TIMP interactome is poorly defined. We have optimized a protocol for the identification of ePPIs for the TIMP family of proteins. Fusion constructs equipped with a promiscuous biotin ligase (BioID2/TurboID) fused to the N- or C-terminal of full length TIMP2 were packaged into retroviral vectors for cellular delivery. Cells were exposed to the extracellular proximity labelling (ePL) fusion proteins and processed in our optimized analysis pipeline. ePPIs were identified via streptavidin pulldown and proteomic techniques. We present our optimized ePL pipeline and show that this technique is an effective tool for the identification of novel ePPIs for multiple extracellular targets. Citation Format: Sadeechya Gurung. Extracellular proximity labeling (ePL) as a tool to identify protein-protein interactions in the tumor microenvironment [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2022; 2022 Apr 8-13. Philadelphia (PA): AACR; Cancer Res 2022;82(12_Suppl):Abstract nr 998.

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42

Li, Jess, Yue Zhang, Olivier Soubias, Domarin Khago, Fa-an Chao, Yifei Li, Katherine Shaw, and R. Andrew Byrd. "Optimization of sortase A ligation for flexible engineering of complex protein systems." Journal of Biological Chemistry 295, no. 9 (January 23, 2020): 2664–75. http://dx.doi.org/10.1074/jbc.ra119.012039.

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Engineering and bioconjugation of proteins is a critically valuable tool that can facilitate a wide range of biophysical and structural studies. The ability to orthogonally tag or label a domain within a multidomain protein may be complicated by undesirable side reactions to noninvolved domains. Furthermore, the advantages of segmental (or domain-specific) isotopic labeling for NMR, or deuteration for neutron scattering or diffraction, can be realized by an efficient ligation procedure. Common methods—expressed protein ligation, protein trans-splicing, and native chemical ligation—each have specific limitations. Here, we evaluated the use of different variants of Staphylococcus aureus sortase A for a range of ligation reactions and demonstrate that conditions can readily be optimized to yield high efficiency (i.e. completeness of ligation), ease of purification, and functionality in detergents. These properties may enable joining of single domains into multidomain proteins, lipidation to mimic posttranslational modifications, and formation of cyclic proteins to aid in the development of nanodisc membrane mimetics. We anticipate that the method for ligating separate domains into a single functional multidomain protein reported here may enable many applications in structural biology.

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43

Steinhagen, Max, Kai Holland-Nell, Morten Meldal, and Annette G. Beck-Sickinger. "Simultaneous “One Pot” Expressed Protein Ligation and CuI-Catalyzed Azide/Alkyne Cycloaddition for Protein Immobilization." ChemBioChem 12, no. 16 (September 8, 2011): 2426–30. http://dx.doi.org/10.1002/cbic.201100434.

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44

Kimura, Richard, and Julio Camarero. "Expressed Protein Ligation: A New Tool for the Biosynthesis of Cyclic Polypeptides." Protein & Peptide Letters 12, no. 8 (November 1, 2005): 789–94. http://dx.doi.org/10.2174/0929866054864274.

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45

Macmillan, Derek, and Lubna Arham. "Cyanogen Bromide Cleavage Generates Fragments Suitable for Expressed Protein and Glycoprotein Ligation." Journal of the American Chemical Society 126, no. 31 (August 2004): 9530–31. http://dx.doi.org/10.1021/ja047855m.

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46

Xia, Yan, Shengchang Tang, and Bradley D. Olsen. "Site-specific conjugation of RAFT polymers to proteins via expressed protein ligation." Chemical Communications 49, no. 25 (2013): 2566. http://dx.doi.org/10.1039/c3cc38976f.

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47

Warden-Rothman, Robert, Ilaria Caturegli, Vladimir Popik, and Andrew Tsourkas. "Sortase-Tag Expressed Protein Ligation: Combining Protein Purification and Site-Specific Bioconjugation into a Single Step." Analytical Chemistry 85, no. 22 (October 28, 2013): 11090–97. http://dx.doi.org/10.1021/ac402871k.

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48

Takeda, Shuji, Shinya Tsukiji, and Teruyuki Nagamune. "Site-specific conjugation of oligonucleotides to the C-terminus of recombinant protein by expressed protein ligation." Bioorganic & Medicinal Chemistry Letters 14, no. 10 (May 2004): 2407–10. http://dx.doi.org/10.1016/j.bmcl.2004.03.023.

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49

Chen, Liguang, George Widhopf, Lang Huynh, Laura Rassenti, Kanti R. Rai, Arthur Weiss, and Thomas J. Kipps. "Expression of ZAP-70 is associated with increased B-cell receptor signaling in chronic lymphocytic leukemia." Blood 100, no. 13 (December 15, 2002): 4609–14. http://dx.doi.org/10.1182/blood-2002-06-1683.

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We examined isolated leukemia B cells of patients with chronic lymphocytic leukemia (CLL) for expression of zeta-associated protein 70 (ZAP-70). CLL B cells that have nonmutated immunoglobulin variable region genes (V genes) expressed levels of ZAP-70 protein that were comparable to those expressed by normal blood T cells. In contrast, CLL B cells that had mutated immunoglobulin variable V genes, or that had low-level expression of CD38, generally did not express detectable amounts of ZAP-70 protein. Leukemia cells from identical twins with CLL were found discordant for expression of ZAP-70, suggesting that B-cell expression of ZAP-70 is not genetically predetermined. Ligation of the B-cell receptor (BCR) complex on CLL cells that expressed ZAP-70 induced significantly greater tyrosine phosphorylation of cytosolic proteins, including p72Syk, than did similar stimulation of CLL cells that did not express ZAP-70. Also, exceptional cases of CLL cells that expressed mutated immunoglobulin V genes and ZAP-70 also experienced higher levels tyrosine phosphorylation of such cytosolic proteins following BCR ligation. Following BCR ligation, ZAP-70 underwent tyrosine phosphorylation and became associated with surface immunoglobulin and CD79b, arguing for the involvement of ZAP-70 in BCR signaling. These data indicate that expression of ZAP-70 is associated with enhanced signal transduction via the BCR complex, which may contribute to the more aggressive clinical course associated with CLL cells that express nonmutated immunoglobulin receptors.

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Tripsianes, Konstantinos, Nam K. Chu, Anders Friberg, Michael Sattler, and Christian F. W. Becker. "Studying Weak and Dynamic Interactions of Posttranslationally Modified Proteins using Expressed Protein Ligation." ACS Chemical Biology 9, no. 2 (December 6, 2013): 347–52. http://dx.doi.org/10.1021/cb400723j.

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