{"id":588,"date":"2011-04-26T15:28:20","date_gmt":"2011-04-26T19:28:20","guid":{"rendered":"https:\/\/www.bu.edu\/nf-kb\/?page_id=588"},"modified":"2011-04-28T19:43:12","modified_gmt":"2011-04-28T23:43:12","slug":"data-link-5","status":"publish","type":"page","link":"https:\/\/www.bu.edu\/nf-kb\/the-gilmore-lab\/data-link-5\/","title":{"rendered":"Data Link 5"},"content":{"rendered":"

The table below has additional primary references for Table 1 in Wang & Gilmore, 2002., Biochimica et Biophysica Acta – Molecular Cell Research<\/em><\/p>\n

<\/strong><\/p>\n

Table 1\u00a0 Interaction partners of zyxin\/paxillin family proteins<\/span><\/strong><\/p>\n

<\/p>\n\n<\/col>\n<\/col>\n<\/col>\n<\/col>\n<\/col>\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n\n
Protein<\/strong><\/td>\nCytoskeletal and\/or
\nPlasma Membrane<\/strong><\/td>\n		Signaling
\nMolecules<\/strong><\/td>\n		Transcription Factors\/
\nNuclear Proteins<\/strong><\/td>\n		Others<\/strong><\/td>\n<\/tr>\n
Zyxin<\/strong><\/td>\na-actinin [34-36]<\/td>\nVav [41]<\/td>\nHPV E6 protein [22]<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\nMena\/VASP [37,38]<\/td>\nCasL [31]<\/td>\nSON DNA-binding
\nprotein [31]<\/td>\n		<\/td>\n<\/tr>\n
<\/strong><\/td>\nCRP [39]<\/td>\np130Cas<\/sup><\/span> [31]<\/span><\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\nH-warts\/LATS1[40]<\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
Trip6<\/strong><\/td>\nOpaP [42]<\/td>\nGrb2 [79]<\/td>\nThyroid hormone
\nreceptor [15]<\/td>\n		RIL [44]<\/td>\n<\/tr>\n
<\/strong><\/td>\nTropomyosin 4 [31]<\/td>\nPTP-BL\/1E [44,45]<\/td>\nRetinoid X receptor [15]<\/td>\nNovel protein [31]<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\nCasL [31]<\/td>\nv-Rel [17]<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\np130Cas<\/sup><\/span> [31]<\/span><\/td>\nSON DNA-binding
\nprotein [31]<\/td>\n		<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\ngp210 [31]<\/td>\nAtrophin-1 related
\nprotein [31]<\/td>\n		<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\nSynaptic GTPase
\nActivating Protein [31]<\/td>\n		<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
LPP<\/strong><\/td>\nMena\/VASP [8]<\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
Ajuba<\/strong><\/td>\nGrb2 [45]<\/td>\nTTF1 [19]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\nGLT1 [46]<\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
Paxillin<\/strong><\/td>\nb1, b3, a4, and a6
\nsubunits [47-50]<\/td>\n		FAK [54,56,58]<\/td>\nBPV E6 protein [32,33]<\/td>\nPoly(a)-binding
\nprotein 1 [66]<\/td>\n<\/tr>\n
<\/strong><\/td>\nsyndesmos [51]<\/td>\nCAKb\/Pyk2 [58,59]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\ntubulin [52]<\/td>\nILK [60]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\nvinculin [53-56]<\/td>\nSrc [61]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\nactopaxin [57]<\/td>\nPKL [62]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\nschwannomin [77]<\/td>\nPAK [62,64]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\nCsk [65]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\nCrk [66]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\nPTP-PEST [67]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
Hic-5<\/strong><\/td>\nvinculin [69]<\/td>\nFAK [69-71]<\/td>\n<\/td>\nAndrogen
\nreceptor [18]<\/td>\n<\/tr>\n
<\/strong><\/td>\nsyndesmos [51]<\/td>\nCAKb\/Pyk2 [72,73]<\/td>\n<\/td>\nGlucocorticoid
\nreceptor [5]<\/td>\n<\/tr>\n
<\/strong><\/td>\nactopaxin [57]<\/td>\nPKL [63]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\ndopamine
\ntransporter [78]<\/td>\n		Csk [73]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\nPTP-PEST [74]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\nGLT1 [75]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
<\/strong><\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/td>\n<\/tr>\n
Leupaxin<\/strong><\/td>\n<\/td>\nCAKb\/Pyk2 [76]<\/td>\n<\/td>\n<\/td>\n<\/tr>\n<\/tbody>\n<\/table>\n

Complete References for Interacting Proteins in Table 1 of Wang & Gilmore, Biochimica et Biophysica Acta – Molecular Cell Research<\/em><\/strong><\/p>\n

5\u00a0\u00a0 Yang, L. et al<\/em>. (2000) Interaction of the t2 transcriptional activation domain of glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5, which localizes to both focal adhesions and the nuclear matrix. Mol Biol Cell<\/em> 11, 2007-2018<\/p>\n

8 <\/em>Petit, M. M. et al<\/em>. (2000) LPP, an actin cytoskeleton protein related to zyxin, harbors a nuclear export signal and transcriptional activation capacity. Mol Biol Cell<\/em> 11, 117-129<\/p>\n

15\u00a0 Lee, J. W. et al.<\/em> (1995) Two classes of proteins dependent on either the presence or absence of thyroid hormone for interaction with the thyroid hormone receptor. Mol Endocrinol<\/em> 9, 243-254<\/p>\n

17 <\/em>Koedood Zhao, M. et al<\/em>. (1999) LIM domain-containing protein Trip6 can act as a coactivator for the v-Rel transcription factor. Gene Expr<\/em> 8, 207-217<\/p>\n

18 <\/em>Fujimoto, N. et al<\/em>. (1999) Cloning and characterization of androgen receptor coactivator, ARA55, in human prostate. J Biol Chem<\/em> 274, 8316-8321<\/p>\n

19 <\/em>Missero, C. et al<\/em>. (2001) The DNA glycosylase T:G mismatch-specific thymine DNA glycosylase represses thyroid transcription factor-1-activated transcription. J Biol Chem<\/em> 276, 33569-33575<\/p>\n

22 <\/em>Degenhardt, Y. Y. and Silverstein, S. (2001) Interaction of zyxin, a focal adhesion protein, with the E6 protein from human papillomavirus type 6 results in its nuclear translocation. J Virol<\/em> 75, 11791-11802<\/p>\n

31\u00a0 Yi J. et al.<\/em> (2002) Members of the zyxin family of LIM proteins interact with members of the p130Cas<\/sup> family of signal transducers. J Biol Chem<\/em> 277, 9580-9589<\/p>\n

32 <\/em>Tong, X. and Howley, P. M. (1997) The bovine papillomavirus E6 oncoprotein interacts with paxillin and disrupts the actin cytoskeleton. Proc Natl Acad Sci USA<\/em> 94, 4412-4417<\/p>\n

33 <\/em>Vande Pol, S. B. et al<\/em>. (1998) Association of bovine papillomavirus type 1 E6 oncoprotein with the focal adhesion protein paxillin through a conserved protein interaction motif. Oncogene<\/em> 16, 43-52<\/p>\n

34 <\/em>Crawford, A. W. et al<\/em>. (1992) An interaction between zyxin and alpha-actinin. J Cell Biol<\/em> 116, 1381-1393<\/p>\n

35 <\/em>Drees, B. E. et al<\/em>. (1999) Molecular dissection of zyxin function reveals its involvement in cell motility. J Cell Biol<\/em> 147, 1549-1560<\/p>\n

36 <\/em>Reinhard, M. et al<\/em>. (1999) An a-actinin binding site of zyxin is essential for subcellular zyxin localization and alpha-actinin recruitment. J Biol Chem<\/em> 274, 13410-13418<\/p>\n

37 <\/em>Reinhard, M. et al<\/em>. (1995) Identification, purification, and characterization of a zyxin-related protein that binds the focal adhesion and microfilament protein VASP (vasodilator-stimulated phosphoprotein). Proc Natl Acad Sci USA<\/em> 92, 7956-7960<\/p>\n

38 <\/em>Drees, B. et al<\/em>. (2000) Characterization of the interaction between zyxin and members of the Ena\/vasodilator-stimulated phosphoprotein family of proteins. J Biol Chem<\/em> 275, 22503-22511<\/p>\n

39 <\/em>Sadler, I. et al<\/em>. (1992) Zyxin and cCRP: two interactive LIM domain proteins associated with the cytoskeleton. J Cell Biol<\/em> 119, 1573-1587<\/p>\n

40 <\/em>Hirota, T. et al<\/em>. (2000) Zyxin, a regulator of actin filament assembly, targets the mitotic apparatus by interacting with h-warts\/LATS1 tumor suppressor. J Cell Biol<\/em> 149, 1073-1086<\/p>\n

41 <\/em>Hobert, O. et al<\/em>. (1996) SH3 domain-dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin. Oncogene<\/em> 12, 1577-1581<\/p>\n

42 <\/em>Williams, J. M. et al<\/em>. (1998) Using the yeast two-hybrid system to identify human epithelial cell proteins that bind gonococcal Opa proteins: intracellular gonococci bind pyruvate kinase via their Opa proteins and require host pyruvate for growth. Mol Microbiol<\/em> 27, 171-186<\/p>\n

43 <\/em>Murthy, K. K. et al<\/em>. (1999) ZRP-1, a zyxin-related protein, interacts with the second PDZ domain of the cytosolic protein tyrosine phosphatase hPTP1E. J Biol Chem<\/em> 274, 20679-20687<\/p>\n

44 <\/em>Cuppen, E. et al<\/em>. (2000) The zyxin-related protein TRIP6 interacts with PDZ motifs in the adaptor protein RIL and the protein tyrosine phosphatase PTP-BL. Eur J Cell Biol<\/em> 79, 283-293<\/p>\n

45 <\/em>Goyal, R. K. et al<\/em>. (1999) Ajuba, a novel LIM protein, interacts with Grb2, augments mitogen-activated protein kinase activity in fibroblasts, and promotes meiotic maturation of Xenopus oocytes in a Grb2- and Ras-dependent manner. Mol Cell Biol<\/em> 19, 4379-4389<\/p>\n

46 <\/em>Marie, H. et al<\/em>. (2002) The amino terminus of the glial glutamate transporter GLT-1 interacts with the LIM protein Ajuba. Mol Cell Neurosci<\/em> 19, 152-164<\/p>\n

47 <\/em>Schaller, M. D. et al<\/em>. (1995) Focal adhesion kinase and paxillin bind to peptides mimicking b integrin cytoplasmic domains. J Cell Biol<\/em> 130, 1181-1187<\/p>\n

48 <\/em>Liu, S. et al<\/em>. (1999) Binding of paxillin to a4 integrins modifies integrin-dependent biological responses. Nature<\/em> 402, 676-681<\/p>\n

49 <\/em>Chen, L. M. et al<\/em>. (2000) Association of b1 integrin with focal adhesion kinase and paxillin in differentiating Schwann cells. J Neurosci<\/em> 20, 3776-3784<\/p>\n

50 Wine, R. N. et al.<\/em> (2002) Identification of components of protein complexes using a fluorescent photo-cross-linker and mass spectrometry. Anal. Chem.<\/em> 74, 1939-1945<\/p>\n

51 <\/em>Denhez, F. et al<\/em>. (2002) Syndesmos, a syndecan-4 cytoplasmic domain interactor, binds to the focal adhesion adaptor proteins paxillin and hic-5. J Biol Chem<\/em> 277, 12270-12274<\/p>\n

52 Brown, M. C. and Turner, C. E. (2002) Roles for the tubulin- and PTP-PEST-binding paxillin LIM domains in cell adhesion and motility. Int. J. Biochem. Cell Biol.<\/em> 34, 855-863<\/p>\n

53 <\/em>Turner, C. E. et al<\/em>. (1990) Paxillin: a new vinculin-binding protein present in focal adhesions. J Cell Biol<\/em> 111, 1059-1068<\/p>\n

54 <\/em>Turner, C. E. and Miller, J. T. (1994) Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125Fak-binding region. J Cell Sci<\/em> 107, 1583-1591<\/p>\n

55 <\/em>Wood, C. K. et al<\/em>. (1994) Characterization of the paxillin-binding site and the C-terminal focal adhesion targeting sequence in vinculin. J Cell Sci<\/em> 107, 709-717<\/p>\n

56 <\/em>Brown, M. C. et al<\/em>. (1996) Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding. J Cell Biol<\/em> 135, 1109-1123<\/p>\n

57 <\/em>Nikolopoulos, S. N. and Turner, C. E. (2000) Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion. J Cell Biol<\/em> 151, 1435-1448<\/p>\n

58 <\/em>Hildebrand, J. D. et al<\/em>. (1995) Paxillin, a tyrosine phosphorylated focal adhesion-associated protein binds to the carboxyl terminal domain of focal adhesion kinase. Mol Biol Cell<\/em> 6, 637-647<\/p>\n

59 <\/em>Salgia, R. et al<\/em>. (1996) The related adhesion focal tyrosine kinase forms a complex with paxillin in hematopoietic cells. J Biol Chem<\/em> 271, 31222-31226<\/p>\n

60 <\/em>Nikolopoulos, S. N. and Turner, C. E. (2001) Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions. J Biol Chem<\/em> 276, 23499-23505<\/p>\n

61 <\/em>Weng, Z. et al<\/em>. (1993) Detection of Src homology 3-binding proteins, including paxillin, in normal and v-Src-transformed Balb\/c 3T3 cells. J Biol Chem<\/em> 268, 14956-14963<\/p>\n

62 <\/em>Turner, C. E. et al<\/em>. (1999) Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: a role in cytoskeletal remodeling. J Cell Biol<\/em> 145, 851-863<\/p>\n

63 <\/em>West, K. A. et al<\/em>. (2001) The LD4 motif of paxillin regulates cell spreading and motility through an interaction with paxillin kinase linker (PKL). J Cell Biol<\/em> 154, 161-176<\/p>\n

64 <\/em>Hashimoto, S. et al<\/em>. (2001) Interaction of paxillin with p21-activated Kinase (PAK). Association of paxillin alpha with the kinase-inactive and the Cdc42-activated forms of PAK3. J Biol Chem<\/em> 276, 6037-6045<\/p>\n

65 <\/em>Sabe, H. et al<\/em>. (1994) Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src. Proc Natl Acad Sci USA<\/em> 91, 3984-3988<\/p>\n

66 <\/em>Schaller, M. D. and Parsons, J. T. (1995) pp125FAK<\/sup>-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol Cell Biol<\/em> 15, 2635-2645<\/p>\n

67 <\/em>Cote, J. F. et al<\/em>. (1999) Intact LIM 3 and LIM 4 domains of paxillin are required for the association to a novel polyproline region (Pro 2) of protein-tyrosine phosphatase-PEST. J Biol Chem<\/em> 274, 20550-20560<\/p>\n

68 <\/em>Woods, A. J. et al<\/em>. (2002) Paxillin associates with poly(A)-binding protein 1 at the dense endoplasmic reticulum and the leading edge of migrating cells. J Biol Chem<\/em> 277, 6428-6437<\/p>\n

69 <\/em>Thomas, S. M. et al<\/em>. (1999) Characterization of a focal adhesion protein, Hic-5, that shares extensive homology with paxillin. J Cell Sci<\/em> 112, 181-190<\/p>\n

70 <\/em>Fujita, H. et al<\/em>. (1998) Interaction of Hic-5, a senescence-related protein, with focal kinase. J Biol Chem<\/em> 273, 26516-26521<\/p>\n

71\u00a0 Ishino, K. et al.<\/em> (2000) Specific decrease in the level of Hic-5, a focal adhesion protein, during immortalization of mouse embryonic fibroblasts, and its association with focal adhesion kinase. J Cell Biochem<\/em> 76, 411-419<\/p>\n

72 <\/em>Matsuya, M. et al<\/em>. (1998) Cell adhesion kinase b forms a complex with a new member, Hic-5, of proteins localized at focal adhesions. J Biol Chem<\/em> 273, 1003-1014<\/p>\n

73 <\/em>Ishino, M. et al<\/em>. (2000) Phosphorylation of Hic-5 at tyrosine 60 by CAKb and Fyn. FEBS Lett<\/em> 474, 179-183<\/p>\n

74 <\/em>Nishiya, N. et al<\/em>. (1999) Hic-5, a paxillin homologue, binds to the protein-tyrosine phosphatase PEST (PTP-PEST) through its LIM 3 domain. J Biol Chem<\/em> 274, 9847-9853<\/p>\n

75 Nishiya, N., Shirai, T., Suzuki, W., Nose, K. (2002) Hic-5 Interacts with GIT1 with a different binding mode from paxillin. J Biochem (Tokyo)<\/em> 132, 279-289<\/p>\n

76 <\/em>Lipsky, B. P. et al<\/em>. (1998) Leupaxin is a novel LIM domain protein that forms a\u00a0\u00a0 complex with PYK2. J Biol Chem<\/em> 273, 11709-11713<\/p>\n

77\u00a0 Fernandez-Valle, C., Tang, Y., Ricard, J., Rodenas-Ruano, A., Taylor, A., Hackler, E., Biggerstaff, J., Iacovelli, J. (2002) Paxillin binds schwannomin and regulates its density- dependent localization and effect on cell morphology. Nat Genet<\/em> 31, 354-362<\/p>\n

78 Carneiro, A. M., Ingram, S. L., Beaulieu, J. M., Sweeney, A., Amara, S. G., Thomas, S. M., Caron, M. G., Torres, G. E. (2002) The multiple LIM domain-containing adaptor protein Hic-5 synaptically colocalizes and interacts with the dopamine transporter. J Neurosci<\/em> 22, 7045-7054<\/p>\n

79 Wang, Y. (2002) A molecular and cellular characterization of Trip6 (thyroid hormone receptor interacting protein 6), a LIM domain protein that moves between focal adhesion plaques and the nucleus. PhD thesis, Boston University<\/p>\n","protected":false},"excerpt":{"rendered":"

The table below has additional primary references for Table 1 in Wang & Gilmore, 2002., Biochimica et Biophysica Acta – Molecular Cell Research Table 1\u00a0 Interaction partners of zyxin\/paxillin family proteins Protein Cytoskeletal and\/or Plasma Membrane Signaling Molecules Transcription Factors\/ Nuclear Proteins Others Zyxin a-actinin [34-36] Vav [41] HPV E6 protein [22] Mena\/VASP [37,38] CasL […]<\/p>\n","protected":false},"author":4258,"featured_media":0,"parent":337,"menu_order":19,"comment_status":"closed","ping_status":"open","template":"","meta":[],"_links":{"self":[{"href":"https:\/\/www.bu.edu\/nf-kb\/wp-json\/wp\/v2\/pages\/588"}],"collection":[{"href":"https:\/\/www.bu.edu\/nf-kb\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/www.bu.edu\/nf-kb\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/www.bu.edu\/nf-kb\/wp-json\/wp\/v2\/users\/4258"}],"replies":[{"embeddable":true,"href":"https:\/\/www.bu.edu\/nf-kb\/wp-json\/wp\/v2\/comments?post=588"}],"version-history":[{"count":7,"href":"https:\/\/www.bu.edu\/nf-kb\/wp-json\/wp\/v2\/pages\/588\/revisions"}],"predecessor-version":[{"id":590,"href":"https:\/\/www.bu.edu\/nf-kb\/wp-json\/wp\/v2\/pages\/588\/revisions\/590"}],"up":[{"embeddable":true,"href":"https:\/\/www.bu.edu\/nf-kb\/wp-json\/wp\/v2\/pages\/337"}],"wp:attachment":[{"href":"https:\/\/www.bu.edu\/nf-kb\/wp-json\/wp\/v2\/media?parent=588"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}