Monoclonal antibodies directed against AFAP-110 recognize species- specific and conserved epitopes

Hybridoma

Volumn 18, Issue 2, 1999, Pages 167-175

  Qian, Yong ^a   Guappone, Anne C ^a   Baisden, Joseph M ^a   Hill, M Wynn ^a   Summy, Justin M ^a   Flynn, Daniel C ^a  

^a WEST VIRGINIA UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; COMPLEMENTARY DNA; HYBRID PROTEIN; MONOCLONAL ANTIBODY; MONOCLONAL ANTIBODY 4C3; PROLINE; UNCLASSIFIED DRUG;

ACTIN FILAMENT; ANIMAL CELL; ANTIBODY PRODUCTION; ANTIBODY RESPONSE; ARTICLE; BINDING AFFINITY; CELL CULTURE; CELL STRUCTURE; IMMUNOFLUORESCENCE; MAMMAL; MOUSE; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS;

ANIMALIA; AVES; MAMMALIA;

EID: 0033052571     PISSN: 0272457X     EISSN: None     Source Type: Journal    
DOI: 10.1089/hyb.1999.18.167     Document Type: Article

References (35)

1. Reynolds AB, Roesel DJ, Kanner SB, and Parsons JT: Transformation-specific tyrosine phosphorylation of a novel cellular protein in chicken cells expressing oncogenic variants of the avian cellular Src gene. Mol Cell Biol 1989;9:629-638.
2. Felice GR, Eason P, Nermut MV, and Kellie S: Pp60v-src association with the cytoskeleton induces actin reorganization without affecting polymerization status. Eur J Cell Biol 1990;52:47-59.
3. src substrate. Mol Cell Biol 1993;13:7892-7900.
4. Qian Y, Baisden JM, Westin EH, Guappone AC, Koay T, and Flynn DC: Src can regulate carboxy terminal interactions with AFAP-110 which modulate self-association and cell localization. Oncogene 1998;16:2185-2195.
5. Reynolds AB, Kanner SB, Wang H-C, and Parsons JT: Stable association of activated pp60src with two tyrosine phosphorylated cellular proteins. Mol Cell Biol 1989;9:3951-3958.
6. Kanner SB, Reynolds AB, Wang H-C, and Parsons JT: The SH2 and SH3 domains of pp60src direct stable association with tyrosine phosphorylated proteins p130 and p110. EMBO J 1991;10: 1689-1698.
7. Guappone AC and Flynn DC: The integrity of the SH3 binding motif of AFAP-110 is required to facilitate tyrosine phosphorylation by, and stable complex formation with, Src. Mol Cell Biochem 1997;175, 243-252.
8. Guappone AC, Weimer T, and Flynn DC: Formation of a stable Src-AFAP-110 complex through either an amino terminal or a carboxy terminal SH2-binding motif. Mol Carcinog 1998;22:110-119.
9. Liu M, Qin Y, Liu J, Tanswell AK, and Post M: Mechanical strain induces pp60src activation and translocation to cytoskeleton in fetal rat lung cells. J Biol Chem 1996;271:7066-7071.
10. Gibson TJ, Hyvonen M, Musacchio A, Saraste M, and Birney E: PH domain: The first anniversary. Trends Biochem Sci 1994;19: 349-353.
11. Shaw G: The pleckstrin homology domain: An intriguing multifunctional peptide module. Bioessays 1996;18:35-46.
12. Kanner SB, Reynolds AB, Vines RR, and Parsons JT: Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases. Proc Natl Acad Sci USA 1990;87:3328-3332.
13. Kanner SB, Reynolds AB, and Parsons JT: Immunoaffinity purification of tyrosine-phosphorylated cellular proteins. J Immunol Methods 1989;120:115-124.
14. Qian Y, Baisden JM, Zot HG, and Flynn DC: AFAP-110 interacts with and alters actin filament integrity through carboxy terminal interactions. (Submitted).
15. Guappone AC, Qian Y, Weimer TG, and Flynn DC: An in vivo system for analysis of stable complex formation between Src and AFAP-110. Methods Cell Sci 1996;18:1-11.
16. Luttrell DK, Luttrell LM, and Parsons SJ: Augmented mitogenic responsiveness to epidermal growth factor in murine fibroblasts that overexpress pp60c-src. Mol Cell Biol 1988;8:497-501.
17. Chen C, and Okayama H: High-efficiency transformation of mammalian cells by plasmid DNA. Mol Cell Biol 1987;7:2745-2752.
18. Boyer PL, Colmenares C, Stavnezer E, and Hughes SH: Sequence and biological activity of chicken snoN cDNA clones. Oncogene 1993;8:457-466.
19. Smith DB and Johnson KS: Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 1988;67:31-10.
20. Kuneida T, Matsui M, Nomura N, and Ishizaki R: Cloning of an activated human ret gene with a novel 5′ sequence fused by DNA rearrangement. Gene 1991;107:323-328.
21. Flynn DC, Koay TC, Humphries CG, and Guappone AC: AFAP-120: A variant form of the Src SH2/SH3 binding partner AFAP-110 is detected in brain and contains a novel internal sequence which binds to a 67 kDa protein. J Biol Chem 1995;270: 3894-3899.
22. Ren R, Mayer BJ, Cicchetti P, and Baltimore D: Identification of a ten-amino acid proline-rich SH3 binding site. Science 1993; 259:1157-1161.
23. Weng A, Thomas SM, Rickles RJ, Taylor JA, Brauer AW, Seidel-Dugan C, Michael WM, Dreyfuss G, and Brugge JS: Identification of Src, Fyn, and Lyn SH3-binding proteins: Implications for a function of SH3 domains. Mol Cell Biol 1994;14:4509-4521.
24. Cheadle C, Ivashchenko Y, South V, Searfoss GH, French S, Howk R, Ricca GA, and Jaye M: Identification of a Src SH3 domain binding motif by screening a random phage display library. J Biol Chem 1994;269, 24034-24039.
25. Rickles RJ, Botfield MC, Weng Z, Taylor JA, Green OM, Brugge JS, and Zoller MJ: Identification of Src, Fyn, Lyn, PI3-K and Abl SH3 domain ligands using phage display libraries. EMBO J 1994;13:5598-5604.
26. Rickles RJ, Botfield MC, Zhou X-M, Henry PA, Brugge JS, and Zoller MJ: Phage display selection of ligand residues important for Src homology 3 domain binding specificity. Proc Natl Acad Sci USA 1995;92:10909-10913.
27. Sparks AB, Quilliam LA, Thorn JM, Der CJ, and Kay BK: Identification and characterization of Src SH3 ligands from phage-displayed random peptide libraries. J Biol Chem 1994;269:23853-23856.
28. Yao X, Thibodeau A, and Forte JG: Exrin-calpain I interactions in gastric parietal cells. Am J Physiol 1993;265:C36-46.
29. Shuster CB and Herman IM: Indirect association of ezrin with F-actin: Isoform specificity and calcium sensitivity. J Cell Biol 1995;128:837-848.
30. Huttenlocher A, Palecek SP, Lu Q, Zhang W, Mellgren RL, Lauffenburger DA, Ginsberg MH, and Horowitz AF: Regulation of cell migration by the calcium-dependent protease calpain. J Biol Chem 1997;272:32719-32722.
31. Melloni E, Pontremoli S, Michetti M, Sacco O, Sparatore B, Salamino F, and Horecker BL: Binding of protein kinase C to neutrophil membranes in the presence of Ca+2 and its activation by a Ca+2-requiring proteinase. Proc Natl Acad Sci USA 1985; 82:6435-6439.
32. Cooray P, Yuan Y, Schoenwaelder SM, Mithcell CA, Salem HH, and Jackson SP: Focal adhesion kinase (pp125FAK) cleavage and regulation by calpain. Biochem J 1996;318:41-47.
33. Vuori K, and Ruoslahti E: Activation of protein kinase C precedes α5β1 integrin-mediated cell spreading on fibronectin. J Biol Chem 1993;268:21459-21462.
34. Lewis JM, Cheresh DA, and Schwanz MA: Protein kinase C regulates alpha v beta 5-dependent cytoskeletal associations focal adhesion kinase phosphorylation. J Cell Biol 1996;134:1323-1332.
35. Croall DE and Demartino GN: Calcium-activated neurtal protease (calpain) system: Structure, function, and regulation. Physiol Rev 1991;71:813-847.