Nội dung được dịch bởi AI, chỉ mang tính chất tham khảo
Sự điều hòa p73 bởi Hck thông qua các cơ chế phụ thuộc và không phụ thuộc vào kinase
Tóm tắt
p73, một thành viên của họ p53, là một yếu tố phiên mã có vai trò trong chu trình tế bào, phân hóa và quá trình apoptosis. p73 được điều chỉnh thông qua các biến đổi sau dịch mã và các tương tác protein. c-Abl là kinase tyrosine duy nhất được biết đến có khả năng phosphoryl hóa và kích hoạt p73. Ở đây, chúng tôi đã phân tích vai trò của các kinase thuộc họ Src, những kinase này tham gia vào nhiều con đường tín hiệu khác nhau, trong việc điều hòa p73. Hck được biểu hiện ngoại sinh cũng như p73 tương tác với nhau trong môi trường sống. Các thử nghiệm gắn kết trong ống nghiệm cho thấy miền SH3 của Hck tương tác với p73. Sự đồng biểu hiện của p73 với Hck hoặc c-Src trong tế bào động vật có vú dẫn đến việc phosphoryl hóa tyrosine của p73. Sử dụng phân tích đột biến có định hướng, chúng tôi xác định rằng Tyr-28 là vị trí chủ yếu bị phosphoryl hóa bởi Hck và c-Src, không giống như c-Abl, phosphoryl hóa Tyr-99. Một cách phụ thuộc vào kinase, sự đồng biểu hiện Hck dẫn đến việc ổn định protein p73 trong tế bào chất. Kích hoạt Hck trong các tế bào HL-60 dẫn đến phosphoryl hóa tyrosine của p73 nội sinh. Cả Hck ngoại sinh và nội sinh đều được định vị tại cả khu vực hạt nhân và tế bào chất, giống như p73. Hck được biểu hiện ngoài sinh ngăn chặn hoạt động phiên mã của p73 như được xác định bởi các thử nghiệm promoter và phân tích RT-PCR bán định lượng của các mục tiêu p73, Ipaf và MDM2. Chức năng phụ thuộc vào miền SH3 của Hck là cần thiết cho ảnh hưởng của nó đối với hoạt động của p73, điều này cũng được phản ánh trong khả năng ngăn chặn apoptosis do p73 trung gian. Chúng tôi cũng chỉ ra rằng Hck tương tác với protein đồng hoạt hóa Yes (YAP), một đồng hoạt hóa phiên mã của p73, và sự giảm biểu hiện protein YAP thông qua shRNA làm giảm việc kích hoạt promoter Ipaf do p73 gây ra. Chúng tôi đã xác định p73 là một chất nền mới và đối tác tương tác của Hck và cho thấy rằng nó điều hòa p73 thông qua các cơ chế phụ thuộc vào hoạt động xúc tác hoặc các miền tương tác protein. Các tương tác do miền Hck-SH3 trung gian đóng một vai trò quan trọng trong việc ức chế hoạt động phiên mã phụ thuộc p73 của một gen đích, Ipaf, cũng như apoptosis.
Từ khóa
#p73 #Hck #kinase #phosphorylation #apoptosis #cell signaling #transcription factorTài liệu tham khảo
Kaghad M, Bonnet H, Yang A, Creancier L, Biscan JC, Valent A, Minty A, Chalon P, Lelias JM, Dumont X: et al, Monoallelically expressed gene related to p53 at 1p36, a region frequently deleted in neuroblastoma and other human cancers. Cell. 1997, 90: 809-819. 10.1016/S0092-8674(00)80540-1
Ozaki T, Nakagawara A: p73, a sophisticated p53 family member in the cancer world. Cancer Sci. 2005, 96: 729-737. 10.1111/j.1349-7006.2005.00116.x
Melino G, De LV, Vousden KH: p73: Friend or foe in tumorigenesis. Nat Rev Cancer. 2002, 2: 605-615. 10.1038/nrc861
Harms K, Nozell S, Chen X: The common and distinct target genes of the p53 family transcription factors. Cell Mol Life Sci. 2004, 61: 822-842. 10.1007/s00018-003-3304-4
Jost CA, Marin MC, Kaelin WG: p73 is a simian [correction of human] p53-related protein that can induce apoptosis. Nature. 1997, 389: 191-194. 10.1038/38298
De LV, Melino G: Evolution of functions within the p53/p63/p73 family. Ann N Y Acad Sci. 2000, 926: 90-100.
Zhu J, Jiang J, Zhou W, Chen X: The potential tumor suppressor p73 differentially regulates cellular p53 target genes. Cancer Res. 1998, 58: 5061-5065.
Yang A, Walker N, Bronson R, Kaghad M, Oosterwegel M, Bonnin J, Vagner C, Bonnet H, Dikkes P, Sharpe A: et al, p73-deficient mice have neurological, pheromonal and inflammatory defects but lack spontaneous tumours. Nature. 2000, 404: 99-103. 10.1038/35003607
Jain N, Gupta S, Sudhakar C, Radha V, Swarup G: Role of p73 in regulating human caspase-1 gene transcription induced by interferon-{gamma} and cisplatin. J Biol Chem. 2005, 280: 36664-36673. 10.1074/jbc.M413261200
Irwin MS, Kaelin WG: p53 family update: p73 and p63 develop their own identities. Cell Growth Differ. 2001, 12: 337-349.
Dobbelstein M, Strano S, Roth J, Blandino G: p73-induced apoptosis: a question of compartments and cooperation. Biochem Biophys Res Commun. 2005, 331: 688-693. 10.1016/j.bbrc.2005.03.155
Gong JG, Costanzo A, Yang HQ, Melino G, Kaelin WG, Levrero M, Wang JY: The tyrosine kinase c-Abl regulates p73 in apoptotic response to cisplatin-induced DNA damage. Nature. 1999, 399: 806-809. 10.1038/21690
Miyazaki K, Ozaki T, Kato C, Hanamoto T, Fujita T, Irino S, Watanabe K, Nakagawa T, Nakagawara A: A novel HECT-type E3 ubiquitin ligase, NEDL2, stabilizes p73 and enhances its transcriptional activity. Biochem Biophys Res Commun. 2003, 308: 106-113. 10.1016/S0006-291X(03)01347-0
Kramer S, Ozaki T, Miyazaki K, Kato C, Hanamoto T, Nakagawara A: Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells. Oncogene. 2005, 24: 938-944. 10.1038/sj.onc.1208257
Stros M, Ozaki T, Bacikova A, Kageyama H, Nakagawara A: HMGB1 and HMGB2 cell-specifically down-regulate the p53- and p73-dependent sequence-specific transactivation from the human Bax gene promoter. J Biol Chem. 2002, 277: 7157-7164. 10.1074/jbc.M110233200
Ozaki T, Watanabe K, Nakagawa T, Miyazaki K, Takahashi M, Nakagawara A: Function of p73, not of p53, is inhibited by the physical interaction with RACK1 and its inhibitory effect is counteracted by pRB. Oncogene. 2003, 22: 3231-3242. 10.1038/sj.onc.1206382
Fulco M, Costanzo A, Merlo P, Mangiacasale R, Strano S, Blandino G, Balsano C, Lavia P, Levrero M: p73 is regulated by phosphorylation at the G2/M transition. J Biol Chem. 2003, 278: 49196-49202. 10.1074/jbc.M304921200
Gaiddon C, Lokshin M, Gross I, Levasseur D, Taya Y, Loeffler JP, Prives C: Cyclin-dependent kinases phosphorylate p73 at threonine 86 in a cell cycle-dependent manner and negatively regulate p73. J Biol Chem. 2003, 278: 27421-27431. 10.1074/jbc.M300251200
Aqeilan RI, Pekarsky Y, Herrero JJ, Palamarchuk A, Letofsky J, Druck T, Trapasso F, Han SY, Melino G, Huebner K: et al, Functional association between Wwox tumor suppressor protein and p73, a p53 homolog. Proc Natl Acad Sci USA. 2004, 101: 4401-4406. 10.1073/pnas.0400805101
Hanamoto T, Ozaki T, Furuya K, Hosoda M, Hayashi S, Nakanishi M, Yamamoto H, Kikuchi H, Todo S, Nakagawara A: Identification of protein kinase A catalytic subunit beta as a novel binding partner of p73 and regulation of p73 function. J Biol Chem. 2005, 280: 16665-16675. 10.1074/jbc.M414323200
Watanabe K, Ozaki T, Nakagawa T, Miyazaki K, Takahashi M, Hosoda M, Hayashi S, Todo S, Nakagawara A: Physical interaction of p73 with c-Myc and MM1, a c-Myc-binding protein, and modulation of the p73 function. J Biol Chem. 2002, 277: 15113-15123. 10.1074/jbc.M111281200
Agami R, Blandino G, Oren M, Shaul Y: Interaction of c-Abl and p73alpha and their collaboration to induce apoptosis. Nature. 1999, 399: 809-813. 10.1038/21697
Yuan ZM, Shioya H, Ishiko T, Sun X, Gu J, Huang YY, Lu H, Kharbanda S, Weichselbaum R, Kufe D: p73 is regulated by tyrosine kinase c-Abl in the apoptotic response to DNA damage. Nature. 1999, 399: 814-817. 10.1038/21704
Sanchez-Prieto R, Sanchez-Arevalo VJ, Servitja JM, Gutkind JS: Regulation of p73 by c-Abl through the p38 MAP kinase pathway. Oncogene. 2002, 21: 974-979. 10.1038/sj.onc.1205134
Thomas SM, Brugge JS: Cellular functions regulated by Src family kinases. Annu Rev Cell Dev Biol. 1997, 13: 513-609. 10.1146/annurev.cellbio.13.1.513
Briggs SD, Sharkey M, Stevenson M, Smithgall TE: SH3-mediated Hck tyrosine kinase activation and fibroblast transformation by theNef protein of HIV-1. J Biol Chem. 1997, 272: 17899-17902. 10.1074/jbc.272.29.17899
Liu X, Pawson T: Biochemistry of the Src protein-tyrosine kinase: regulation by SH2 and SH3 domains. Recent Prog Horm Res. 1994, 49: 149-60.
Ernst M, Gearing DP, Dunn AR: Functional and biochemical association of Hck with the LIF/IL-6 receptor signal transducing subunit gp130 in embryonic stem cells. EMBO J. 1994, 13: 1574-1584.
Quintrell N, Lebo R, Varmus H, Bishop JM, Pettenati MJ, Le Beau MM, Diaz MO, Rowley JD: Identification of a human gene (HCK) that encodes a protein-tyrosine kinase and is expressed in hemopoietic cells. Mol Cell Biol. 1987, 7: 2267-2275.
Ziegler SF, Marth JD, Lewis DB, Perlmutter RM: Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic origin. Mol Cell Biol. 1987, 7: 2276-2285.
Lock P, Ralph S, Stanley E, Boulet I, Ramsay R, Dunn AR: Two isoforms of murine hck, generated by utilization of alternative translational initiation codons, exhibit different patterns of subcellular localization. Mol Cell Biol. 1991, 11: 4363-4370.
Bosco MC, Curiel RE, Zea AH, Malabarba MG, Ortaldo JR, Espinoza-Delgado I: IL-2 signaling in human monocytes involves the phosphorylation and activation of p59hck. J Immunol. 2000, 164: 4575-4585.
Ward AC, Monkhouse JL, Csar XF, Touw IP, Bello PA: The Src-like tyrosine kinase Hck is activated by granulocyte colony-stimulating factor (G-CSF) and docks to the activated G-CSF receptor. Biochem Biophys Res Commun. 1998, 251: 117-123. 10.1006/bbrc.1998.9441
English BK, Ihle JN, Myracle A, Yi T: Hck tyrosine kinase activity modulates tumor necrosis factor production by murine macrophages. J Exp Med. 1993, 178: 1017-1022. 10.1084/jem.178.3.1017
Boulet I, Ralph S, Stanley E, Lock P, Dunn AR, Green SP, Phillips WA: Lipopolysaccharide- and interferon-gamma-induced expression of hck and lyn tyrosine kinases in murine bone marrow-derived macrophages. Oncogene. 1992, 7: 703-710.
Shivakrupa R, Radha V, Sudhakar C, Swarup G: Physical and functional interaction between Hck tyrosine kinase and guanine nucleotide exchange factor C3G results in apoptosis, which is independent of C3G catalytic domain. J Biol Chem. 2003, 278: 52188-52194. 10.1074/jbc.M310656200
Scholz G, Cartledge K, Dunn AR: Hck enhances the adherence of lipopolysaccharide-stimulated macrophages via Cbl and phosphatidylinositol 3-kinase. J Biol Chem. 2000, 275: 14615-14623. 10.1074/jbc.275.19.14615
Scott MP, Zappacosta F, Kim EY, Annan RS, Miller WT: Identification of novel SH3 domain ligands for the Src family kinase Hck. Wiskott-Aldrich syndrome protein (WASP), WASP-interacting protein (WIP), and ELMO1. J Biol Chem. 2002, 277: 28238-28246. 10.1074/jbc.M202783200
Schreiner SJ, Schiavone AP, Smithgall TE: Activation of STAT3 by the Src family kinase Hck requires a functional SH3 domain. J Biol Chem. 2002, 277: 45680-45687. 10.1074/jbc.M204255200
Yokoyama N, Miller WT: Biochemical properties of the Cdc42-associated tyrosine kinase ACK1. Substrate specificity, authphosphorylation, and interaction with Hck. J Biol Chem. 2003, 278: 47713-47723. 10.1074/jbc.M306716200
Tsai KK, Yuan ZM: c-Abl stabilizes p73 by a phosphorylation-augmented interaction. Cancer Res. 2003, 63: 3418-3424.
Tanis KQ, Veach D, Duewel HS, Bornmann WG, Koleske AJ: Two distinct phosphorylation pathways have additive effects on Abl family kinase activation. Mol Cell Biol. 2003, 23: 3884-3896. 10.1128/MCB.23.11.3884-3896.2003
Tschan MP, Grob TJ, Peters UR, Laurenzi VD, Huegli B, Kreuzer KA, Schmidt CA, Melino G, Fey MF, Tobler A: et al, Enhanced p73 expression during differentiation and complex p73 isoforms in myeloid leukemia. Biochem Biophys Res Commun. 2000, 277: 62-65. 10.1006/bbrc.2000.3627
Linnekin D, Howard OM, Park L, Farrar W, Ferris D, Longo DL: Hck expression correlates with granulocyte-macrophage colony-stimulating factor-induced proliferation in HL-60 cells. Blood. 1994, 84: 94-103.
Howlett CJ, Bisson SA, Resek ME, Tigley AW, Robbins SM: The proto-oncogene p120(Cbl) is a downstream substrate of the Hck protein-tyrosine kinase. Biochem Biophys Res Commun. 1999, 257: 129-138. 10.1006/bbrc.1999.0427
Robbins SM, Quintrell NA, Bishop JM: Mercuric chloride activates the Src-family protein tyrosine kinase, Hck in myelomonocytic cells. Eur J Biochem. 2000, 267: 7201-7208. 10.1046/j.1432-1327.2000.01830.x
Mohn H, Le C V, Fischer S, Maridonneau-Parini I: The src-family protein-tyrosine kinase p59hck is located on the secretory granules in human neutrophils and translocates towards the phagosome during cell activation. Biochem J. 1995, 309: 657-665.
Robbins SM, Quintrell NA, Bishop JM: Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae. Mol Cell Biol. 1995, 15: 3507-3515.
Astarie-Dequeker C, Carreno S, Cougoule C, Maridonneau-Parini I: The protein tyrosine kinase Hck is located on lysosomal vesicles that are physically and functionally distinct from CD63-positive lysosomes in human macrophages. J Cell Sci. 2002, 115: 81-89.
Radha V, Rajanna A, Swarup G: Phosphorylated guanine nucleotide exchange factor C3G, induced by pervanadate and Src family kinases localizes to the Golgi and subcortical actin cytoskeleton. BMC Cell Biol. 2004, 20 (5): 31-10.1186/1471-2121-5-31.
Zhao Y, Sudol M, Hanafusa H, Krueger J: Increased tyrosine kinase activity of c-Src during calcium-induced keratinocyte differentiation. Proc Natl Acad Sci USA. 1992, 89: 8298-8302. 10.1073/pnas.89.17.8298
David-Pfeuty T, Bagrodia S, Shalloway D: Differential localization patterns of myristoylated and nonmyristoylated c-Src proteins in interphase and mitotic c-Src overexpresser cells. J Cell Sci. 1993, 105: 613-628.
Radha V, Nambirajan S, Swarup G: Association of Lyn tyrosine kinase with the nuclear matrix and cell-cycle-dependent changes in matrix-associated tyrosine kinase activity. Eur J Biochem. 1996, 236: 352-359. 10.1111/j.1432-1033.1996.00352.x
Ren X, Cao C, Zhu L, Yoshida K, Kharbanda S, Weichselbaum R, Kufe D: Lyn tyrosine kinase inhibits nuclear export of the p53 tumor suppressor. Cancer Biol Ther. 2002, 1: 703-708.
He Z, Cho YY, Ma WY, Choi HS, Bode AM, Dong Z: Regulation of ultraviolet B-induced phosphorylation of histone H3 at serine 10 by Fyn kinase. J Biol Chem. 2005, 280: 2446-2454. 10.1074/jbc.M402053200
Sadasivam S, Gupta S, Radha V, Batta K, Kundu TK, Swarup G: Caspase-1 activator Ipaf is a p53-inducible gene involved in apoptosis. Oncogene. 2005, 24 (4): 627-636. 10.1038/sj.onc.1208201
Fontemaggi G, Kela I, Amariglio N, Rechavi G, Krishnamurthy J, Strano S, Sacchi A, Givol D, Blandino G: Identification of direct p73 target genes combining DNA microarray and chromatin immunoprecipitation analyses. J Biol Chem. 2002, 277: 43359-43368. 10.1074/jbc.M205573200
Strano S, Munarriz E, Rossi M, Castagnoli L, Shaul Y, Sacchi A, Oren M, Sudol M, Cesareni G, Blandino G: Physical interaction with Yes-associated protein enhances p73 transcriptional activity. J Biol Chem. 2001, 276: 15164-15173. 10.1074/jbc.M010484200
Strano S, Monti O, Pediconi N, Baccarini A, Fontemaggi G, Lapi E, Mantovani F, Damalas A, Citro G, Sacchi A: et al, The transcriptional coactivator Yes-associated protein drives p73 gene-target specificity in response to DNA Damage. Mol Cell. 2005, 18: 447-459. 10.1016/j.molcel.2005.04.008
Sudol M: Yes-associated protein (YAP65) is a proline-rich phosphoprotein that binds to the SH3 domain of the Yes proto-oncogene product. Oncogene. 1994, 9: 2145-2152.
Nilsson J, Bjursell G, Kannius-Janson M: Nuclear Jak2 and transcription factor NF1-C2: a novel mechanism of prolactin signaling in mammary epithelial cells. Mol Cell Biol. 2006, 26: 5663-5674. 10.1128/MCB.02095-05
Strano S, Munarriz E, Rossi M, Castagnoli L, Shaul Y, Sacchi A, Oren M, Sudol M, Cesareni G, Blandino G: Physical interaction with Yes-associated protein enhances p73 transcriptional activity. J Biol Chem. 2001, 276: 15164-15173. 10.1074/jbc.M010484200
Zeng X, Chen L, Jost CA, Maya R, Keller D, Wang X, Kaelin WG, Oren M, Chen J, Lu H: MDM2 suppresses p73 function without promoting p73 degradation. Mol Cell Biol. 1999, 19: 3257-3266.
Mihara M, Erster S, Zaika A, Petrenko O, Chittenden T, Pancoska P, Moll UM: p53 has a direct apoptogenic role at the mitochondria. Mol Cell. 2003, 11: 577-590. 10.1016/S1097-2765(03)00050-9
Chipuk JE, Green DR: Cytoplasmic p53: bax and forward. Cell Cycle. 2004, 3: 429-431.
Marchenko ND, Wolff S, Erster S, Becker K, Moll UM: Monoubiquitylation promotes mitochondrial p53 translocation. EMBO J. 2007, 26: 923-934. 10.1038/sj.emboj.7601560
Yang C, Zhou W, Jeon MS, Demydenko D, Harada Y, Zhou H, Liu YC: Negative regulation of the E3 ubiquitin ligase itch via Fyn-mediated tyrosine phosphorylation. Mol Cell. 2006, 21: 135-141. 10.1016/j.molcel.2005.11.014
Rossi M, De LV, Munarriz E, Green DR, Liu YC, Vousden KH, Cesareni G, Melino G: The ubiquitin-protein ligase Itch regulates p73 stability. EMBO J. 2005, 24: 836-848. 10.1038/sj.emboj.7600444
Radha V, Sudhakar C, Swarup G: Induction of p53 dependent apoptosis upon overexpression of a nuclear protein tyrosine phosphatase. FEBS Lett. 1999, 453: 308-312. 10.1016/S0014-5793(99)00734-6
Gupta S, Radha V, Furukawa Y, Swarup G: Direct transcriptional activation of human caspase-1 by tumor suppressor p53. J Biol Chem. 2001, 276: 10585-10588. 10.1074/jbc.C100025200
Yu JY, DeRuiter SL, Turner DL: RNA interference by expression of short-interfering RNAs and hairpin RNAs in mammalian cells. Proc Natl Acad Sci USA. 2002, 99: 6047-6052. 10.1073/pnas.092143499