메뉴 건너뛰기




Volumn 68, Issue 21, 2008, Pages 8761-8769

c-Cbl interacts with CD38 and promotes retinoic acid-induced differentiation and G0 arrest of human myeloblastic leukemia cells

Author keywords

[No Author keywords available]

Indexed keywords

CBL PROTEIN; CD38 ANTIGEN; MITOGEN ACTIVATED PROTEIN KINASE 1; RETINOIC ACID;

EID: 55349137357     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-08-1058     Document Type: Article
Times cited : (37)

References (45)
  • 1
    • 0023245020 scopus 로고
    • Vitamin A in human nutrition
    • Sklan D. Vitamin A in human nutrition. Prog Food Nut Sci 1987;11:39-55.
    • (1987) Prog Food Nut Sci , vol.11 , pp. 39-55
    • Sklan, D.1
  • 2
    • 0034906769 scopus 로고    scopus 로고
    • Treatment with all-trans retinoic acid in acute promyelocytic leukemia reduces early death in children
    • Mann G, Reinhardt D, Ritter J, et al. Treatment with all-trans retinoic acid in acute promyelocytic leukemia reduces early death in children. Ann Hematol 2001;80:417-22.
    • (2001) Ann Hematol , vol.80 , pp. 417-422
    • Mann, G.1    Reinhardt, D.2    Ritter, J.3
  • 3
    • 0017782474 scopus 로고
    • Continuous growth and differentiation of human myeloid leukaemic cells in suspension culture
    • Collins SJ, Gallo RC, Gallagher RE. Continuous growth and differentiation of human myeloid leukaemic cells in suspension culture. Nature 1977;270:347-9.
    • (1977) Nature , vol.270 , pp. 347-349
    • Collins, S.J.1    Gallo, R.C.2    Gallagher, R.E.3
  • 4
    • 0001679798 scopus 로고
    • Induction of differentiation of the human promyelocytic leukemia cell line (HL-60) by retinoic acid
    • Bretiman TR, Selonick SE, Collins SJ. Induction of differentiation of the human promyelocytic leukemia cell line (HL-60) by retinoic acid. Proc Natl Acad Sci U S A 1980;77:2926-40.
    • (1980) Proc Natl Acad Sci U S A , vol.77 , pp. 2926-2940
    • Bretiman, T.R.1    Selonick, S.E.2    Collins, S.J.3
  • 5
    • 0025353817 scopus 로고
    • HL-60 cells as a model of growth control and differentiation: The significance of variant cells
    • Yen A. HL-60 cells as a model of growth control and differentiation: the significance of variant cells. Hematol Rev 1990;4:5-46.
    • (1990) Hematol Rev , vol.4 , pp. 5-46
    • Yen, A.1
  • 6
    • 0032528172 scopus 로고    scopus 로고
    • Retinoic acid induces mitogen-activated protein (MAP)/extracellular signal-regulated kinase (ERK) kinase-dependent MAP kinase activation needed to elicit HL-60 cell differentiation and growth arrest
    • Yen A, Roberson MS, Varvayanis S, Lee AT. Retinoic acid induces mitogen-activated protein (MAP)/extracellular signal-regulated kinase (ERK) kinase-dependent MAP kinase activation needed to elicit HL-60 cell differentiation and growth arrest. Cancer Res 1998;58:3163-72.
    • (1998) Cancer Res , vol.58 , pp. 3163-3172
    • Yen, A.1    Roberson, M.S.2    Varvayanis, S.3    Lee, A.T.4
  • 7
    • 0032733965 scopus 로고    scopus 로고
    • Retinoic acid selectively activates the ERK2 but not JNK/SAPK or p38 MAP kinases when inducing myeloid differentiation
    • Yen A, Roberson MS, Varvayanis S. Retinoic acid selectively activates the ERK2 but not JNK/SAPK or p38 MAP kinases when inducing myeloid differentiation. In Vitro Cell Dev Biol Anim 1999;35:527-32.
    • (1999) In Vitro Cell Dev Biol Anim , vol.35 , pp. 527-532
    • Yen, A.1    Roberson, M.S.2    Varvayanis, S.3
  • 8
    • 33748196233 scopus 로고    scopus 로고
    • The Cbl family proteins: Ring leaders in regulation of cell signaling
    • Swaminathan G, Tsygankov A. The Cbl family proteins: ring leaders in regulation of cell signaling. J Cell Physiol 2006;209:21-43.
    • (2006) J Cell Physiol , vol.209 , pp. 21-43
    • Swaminathan, G.1    Tsygankov, A.2
  • 9
    • 0035825121 scopus 로고    scopus 로고
    • Cbl associates with Pyk2 and Src to regulate Src kinase activity, avh3 integrin-mediated signaling, cell adhesion, and osteoclast motility
    • Sanjay A, Houghton A, Neff L, et al. Cbl associates with Pyk2 and Src to regulate Src kinase activity, avh3 integrin-mediated signaling, cell adhesion, and osteoclast motility. J Cell Biol 2001;152:181-95.
    • (2001) J Cell Biol , vol.152 , pp. 181-195
    • Sanjay, A.1    Houghton, A.2    Neff, L.3
  • 10
    • 0033615732 scopus 로고    scopus 로고
    • Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7
    • Yokouchi M, Kondo T, Houghton A, et al. Ligand-induced ubiquitination of the epidermal growth factor receptor involves the interaction of the c-Cbl RING finger and UbcH7. J Biol Chem 1999;274:31707-12.
    • (1999) J Biol Chem , vol.274 , pp. 31707-31712
    • Yokouchi, M.1    Kondo, T.2    Houghton, A.3
  • 11
    • 0034614386 scopus 로고    scopus 로고
    • The RING finger domain of Cbl is essential for negative regulation of the Syk tyrosine kinase
    • Ota S, Hazeki K, Rao N, et al. The RING finger domain of Cbl is essential for negative regulation of the Syk tyrosine kinase. J Biol Chem 2000;275:414-22.
    • (2000) J Biol Chem , vol.275 , pp. 414-422
    • Ota, S.1    Hazeki, K.2    Rao, N.3
  • 12
    • 27444445613 scopus 로고    scopus 로고
    • c-Cbl and Cbl-b ubiquitin ligases: Substrate diversity and the negative regulation of signaling responses
    • Thien CBF, Langdon WY. c-Cbl and Cbl-b ubiquitin ligases: substrate diversity and the negative regulation of signaling responses. Biochem J 2005;391:153-66.
    • (2005) Biochem J , vol.391 , pp. 153-166
    • Thien, C.B.F.1    Langdon, W.Y.2
  • 13
    • 0030872395 scopus 로고    scopus 로고
    • Phosphotyrosine binding domain-dependent upregulation of the platelet-derived growth factor receptor α signaling cascade by transforming mutants of Cbl: Implications for Cbl's function and oncogenicity
    • Bonita DP, Miyake S, Lupher ML, Langdon WY, Band H. Phosphotyrosine binding domain-dependent upregulation of the platelet-derived growth factor receptor α signaling cascade by transforming mutants of Cbl: implications for Cbl's function and oncogenicity. Mol Cell Biol 1997;17:4597-610.
    • (1997) Mol Cell Biol , vol.17 , pp. 4597-4610
    • Bonita, D.P.1    Miyake, S.2    Lupher, M.L.3    Langdon, W.Y.4    Band, H.5
  • 14
    • 0033522219 scopus 로고    scopus 로고
    • Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70ki nase
    • Meng W, Sawasdikosol S, Burakoff SJ, Eck MJ. Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70ki nase. Nature 1999;398:84-90.
    • (1999) Nature , vol.398 , pp. 84-90
    • Meng, W.1    Sawasdikosol, S.2    Burakoff, S.J.3    Eck, M.J.4
  • 15
    • 0033536637 scopus 로고    scopus 로고
    • The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase
    • Joazeiro CA, Wing SS, Huang H, Leverson JD, Hunter T, Liu YC. The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. Science 1999;286:309-12.
    • (1999) Science , vol.286 , pp. 309-312
    • Joazeiro, C.A.1    Wing, S.S.2    Huang, H.3    Leverson, J.D.4    Hunter, T.5    Liu, Y.C.6
  • 16
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligase
    • Zheng N, Wang P, Jeffrey PD, Pavletich NP. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligase. Cell 2000;102:533-9.
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 17
    • 0033392493 scopus 로고    scopus 로고
    • Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1
    • Levkowitz G, Waterman H, Ettenberg SA, et al. Ubiquitin ligase activity and tyrosine phosphorylation underlie suppression of growth factor signaling by c-Cbl/Sli-1. Mol Cell 1999;4:1029-40.
    • (1999) Mol Cell , vol.4 , pp. 1029-1040
    • Levkowitz, G.1    Waterman, H.2    Ettenberg, S.A.3
  • 18
    • 0141637441 scopus 로고    scopus 로고
    • Cbl signaling networks in the regulation of cell function
    • Szymkiswicz DI, Soubeyran P. Cbl signaling networks in the regulation of cell function. Cell Mol Life Sci 2003;60:1805-27.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1805-1827
    • Szymkiswicz, D.I.1    Soubeyran, P.2
  • 19
    • 28844490931 scopus 로고    scopus 로고
    • The Cbl interactome and its functions
    • Schmidt MH, Dikic I. The Cbl interactome and its functions. Nat Rev Mol Cell Biol 2005;6:907-19.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 907-919
    • Schmidt, M.H.1    Dikic, I.2
  • 20
    • 0030070331 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the c-Cbl proto-oncogene product mediated by cell surface antigen CD38 in HL-60 cells
    • Kontani K, Kikimoto I, Nishina H, et al. Tyrosine phosphorylation of the c-Cbl proto-oncogene product mediated by cell surface antigen CD38 in HL-60 cells. J Biol Chem 1996;271:1534-7.
    • (1996) J Biol Chem , vol.271 , pp. 1534-1537
    • Kontani, K.1    Kikimoto, I.2    Nishina, H.3
  • 21
    • 0025265030 scopus 로고
    • Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation
    • Jackson DG, Bell JI. Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation. J Immunol 1990;144:2811-5.
    • (1990) J Immunol , vol.144 , pp. 2811-2815
    • Jackson, D.G.1    Bell, J.I.2
  • 23
    • 36148992239 scopus 로고    scopus 로고
    • CD38 expression labels an activated subset within chronic lymphocytic leukemia clones enriched in proliferating B cells
    • Damle RN, Temburni S, Calissano C, et al. CD38 expression labels an activated subset within chronic lymphocytic leukemia clones enriched in proliferating B cells. Blood 2007;110:3352-9.
    • (2007) Blood , vol.110 , pp. 3352-3359
    • Damle, R.N.1    Temburni, S.2    Calissano, C.3
  • 24
    • 33847056763 scopus 로고    scopus 로고
    • Identification and functional characterization of the hepatic stellate cell CD38 cell surface molecule
    • March S, Graupera M, Rosa Sarrias M, et al. Identification and functional characterization of the hepatic stellate cell CD38 cell surface molecule. Am J Pathol 2007;170:176-87.
    • (2007) Am J Pathol , vol.170 , pp. 176-187
    • March, S.1    Graupera, M.2    Rosa Sarrias, M.3
  • 25
    • 0035177850 scopus 로고    scopus 로고
    • Human CD38: A (r)evolutionary story of enzymes and receptors
    • Deaglio S, Mehta K, Malavasi F. Human CD38: a (r)evolutionary story of enzymes and receptors. Leukemia Res 2001;25:1-12.
    • (2001) Leukemia Res , vol.25 , pp. 1-12
    • Deaglio, S.1    Mehta, K.2    Malavasi, F.3
  • 26
    • 0037016731 scopus 로고    scopus 로고
    • CD38 is associated with lipid rafts and upon receptor stimulation leads to Akt/Protein kinase B and Erk activation in the absence of the CD3. Immune receptor tyrosine-based activation motifs
    • Zubiaur M, Fernandez O, Ferrero E, et al. CD38 is associated with lipid rafts and upon receptor stimulation leads to Akt/Protein kinase B and Erk activation in the absence of the CD3. Immune receptor tyrosine-based activation motifs. J Biol Chem 2002;277:13-22.
    • (2002) J Biol Chem , vol.277 , pp. 13-22
    • Zubiaur, M.1    Fernandez, O.2    Ferrero, E.3
  • 27
    • 33645696402 scopus 로고    scopus 로고
    • Retinoic acid-induced CD38 expression in HL-60 myeloblastic leukemia cells regulates cell differentiation or viability depending on expression levels
    • Lamkin TJ, Chin V, Varvayanis S, et al. Retinoic acid-induced CD38 expression in HL-60 myeloblastic leukemia cells regulates cell differentiation or viability depending on expression levels. J Cell Biochem 2006;97:1328-38.
    • (2006) J Cell Biochem , vol.97 , pp. 1328-1338
    • Lamkin, T.J.1    Chin, V.2    Varvayanis, S.3
  • 28
    • 0034917928 scopus 로고    scopus 로고
    • CD38 expression correlates with adverse biological features and predicts poor clinical outcome in B-cell chronic lymphocytic leukemia
    • D'Arena G, Musto P, Cascavilla N, et al. CD38 expression correlates with adverse biological features and predicts poor clinical outcome in B-cell chronic lymphocytic leukemia. Leuk Lymphoma 2001;42:109-14.
    • (2001) Leuk Lymphoma , vol.42 , pp. 109-114
    • D'Arena, G.1    Musto, P.2    Cascavilla, N.3
  • 29
    • 0037441762 scopus 로고    scopus 로고
    • The pattern of CD38 expression defines a distinct sunset of chronic lymphocytic leukemia (CLL) patients at risk of disease progression
    • Ghia P, Guida G, Stella S, et al. The pattern of CD38 expression defines a distinct sunset of chronic lymphocytic leukemia (CLL) patients at risk of disease progression. Blood 2003;101:1262-9.
    • (2003) Blood , vol.101 , pp. 1262-1269
    • Ghia, P.1    Guida, G.2    Stella, S.3
  • 30
    • 0030031227 scopus 로고    scopus 로고
    • Myeloid differentiation and RB phosphorylation changes in HL-60 cells induced by RAR- and RXR-selective retinoic acid analogs
    • Brooks SC III, Kazmer S, Levin AA, Yen A. Myeloid differentiation and RB phosphorylation changes in HL-60 cells induced by RAR- and RXR-selective retinoic acid analogs. Blood 1996;87:227-37.
    • (1996) Blood , vol.87 , pp. 227-237
    • Brooks III, S.C.1    Kazmer, S.2    Levin, A.A.3    Yen, A.4
  • 31
    • 34548013939 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor regulates myeloid and monocytic differentiation of HL-60 cells
    • Reiterer G, Yen A. Platelet-derived growth factor receptor regulates myeloid and monocytic differentiation of HL-60 cells. Cancer Res 2007;67:7765-72.
    • (2007) Cancer Res , vol.67 , pp. 7765-7772
    • Reiterer, G.1    Yen, A.2
  • 32
    • 0036560276 scopus 로고    scopus 로고
    • Retinoic acid-induced growth arrest and differentiation: Retinoic acid up-regulates CD32 (FcγRII) RII) expression, the ectopic expression of which retards the cell cycle
    • Wightman J, Roberson MS, Lamkin TJ, Varvayanis S, Yen A. Retinoic acid-induced growth arrest and differentiation: retinoic acid up-regulates CD32 (FcγRII) RII) expression, the ectopic expression of which retards the cell cycle. Mol Cancer Ther 2002;1:493-506.
    • (2002) Mol Cancer Ther , vol.1 , pp. 493-506
    • Wightman, J.1    Roberson, M.S.2    Lamkin, T.J.3    Varvayanis, S.4    Yen, A.5
  • 33
    • 33750707926 scopus 로고    scopus 로고
    • Analysis of in vivo targets of transcriptional activators by fluorescence resonance energy transfer
    • Bhaumik SR. Analysis of in vivo targets of transcriptional activators by fluorescence resonance energy transfer. Methods 2006;40:353-9.
    • (2006) Methods , vol.40 , pp. 353-359
    • Bhaumik, S.R.1
  • 34
    • 0141637441 scopus 로고    scopus 로고
    • Cbl signaling networks in the regulation of cell function
    • Dikic I, Szymkiewicz I, Soubeyran P. Cbl signaling networks in the regulation of cell function. Cell Mol Life Sci 2003;60:1805-27.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1805-1827
    • Dikic, I.1    Szymkiewicz, I.2    Soubeyran, P.3
  • 35
    • 0035937774 scopus 로고    scopus 로고
    • Suppression of apoptosis induced by growth factor withdrawal by an oncogenic form of c-Cbl
    • Hamilton E, Miller KM, Helm KM, Langdon WY, Anderson SM. Suppression of apoptosis induced by growth factor withdrawal by an oncogenic form of c-Cbl. J Biol Chem 2001;276:9028-37.
    • (2001) J Biol Chem , vol.276 , pp. 9028-9037
    • Hamilton, E.1    Miller, K.M.2    Helm, K.M.3    Langdon, W.Y.4    Anderson, S.M.5
  • 37
    • 0035316576 scopus 로고    scopus 로고
    • Cbl: Many adaptors to regulate protein tyrosine kinase
    • Thien CB, Langdon WY. Cbl: many adaptors to regulate protein tyrosine kinase. Nat Rev Mol Cell Biol 2001;2:294-307.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 294-307
    • Thien, C.B.1    Langdon, W.Y.2
  • 38
    • 42349108970 scopus 로고    scopus 로고
    • A tale of two Cbls: Interplay of c-Cbl and Cbl-b in epidermal growth factor receptor downregulation
    • Pennock S, Wang Z. A tale of two Cbls: interplay of c-Cbl and Cbl-b in epidermal growth factor receptor downregulation. Mol Cell Biol 2008;28:3020-37.
    • (2008) Mol Cell Biol , vol.28 , pp. 3020-3037
    • Pennock, S.1    Wang, Z.2
  • 39
    • 38049063071 scopus 로고    scopus 로고
    • Up-regulation of the Cbl family of ubiquitin ligase is involved in ATRA and bufalin-induced cell adhesion but not cell differentiation
    • Qu X, Liu Y, Ma Y, Zhang Y, Li Y, Hou K. Up-regulation of the Cbl family of ubiquitin ligase is involved in ATRA and bufalin-induced cell adhesion but not cell differentiation. Biochem Biophys Res Commun 2008;267:183-9.
    • (2008) Biochem Biophys Res Commun , vol.267 , pp. 183-189
    • Qu, X.1    Liu, Y.2    Ma, Y.3    Zhang, Y.4    Li, Y.5    Hou, K.6
  • 40
    • 0029006745 scopus 로고
    • Cloning and characterization of cbl-b: A SH3 binding protein with homology to the c-cbl proto-oncogene
    • Kenae MM, Revero-Lezcano OM, Mitchell JA, Robbins KC, Lipkowitz S. Cloning and characterization of cbl-b: a SH3 binding protein with homology to the c-cbl proto-oncogene. Oncogene 1995;10:2367-77.
    • (1995) Oncogene , vol.10 , pp. 2367-2377
    • Kenae, M.M.1    Revero-Lezcano, O.M.2    Mitchell, J.A.3    Robbins, K.C.4    Lipkowitz, S.5
  • 41
    • 18144412332 scopus 로고    scopus 로고
    • c-Cbl mediates ubiquitination, degradation, and down-regulation of human protease-activated receptor 2
    • Jacob C, Cottrell GS, Gehringer D, Schmidlin F, Grady EF, Bunnett NW. c-Cbl mediates ubiquitination, degradation, and down-regulation of human protease-activated receptor 2. J Biol Chem 2005;280:16076-87.
    • (2005) J Biol Chem , vol.280 , pp. 16076-16087
    • Jacob, C.1    Cottrell, G.S.2    Gehringer, D.3    Schmidlin, F.4    Grady, E.F.5    Bunnett, N.W.6
  • 42
    • 0032478805 scopus 로고    scopus 로고
    • Fyn, Yes, and Syk phosphorylation sites in c-Cbl map to the same tyrosine residues that become phosphorylated in activated T cells
    • Feshchenko EA, Langdon WY, Tsygankov AY. Fyn, Yes, and Syk phosphorylation sites in c-Cbl map to the same tyrosine residues that become phosphorylated in activated T cells. J Biol Chem 1998;273:8323-31.
    • (1998) J Biol Chem , vol.273 , pp. 8323-8331
    • Feshchenko, E.A.1    Langdon, W.Y.2    Tsygankov, A.Y.3
  • 43
    • 0028027169 scopus 로고
    • The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor
    • Donovan JA, Wange RL, Langdon WY, Samelson LE. The protein product of the c-cbl protooncogene is the 120-kDa tyrosine-phosphorylated protein in Jurkat cells activated via the T cell antigen receptor. J Biol Chem 1994;260:22921-4.
    • (1994) J Biol Chem , vol.260 , pp. 22921-22924
    • Donovan, J.A.1    Wange, R.L.2    Langdon, W.Y.3    Samelson, L.E.4
  • 44
    • 27744568732 scopus 로고    scopus 로고
    • The Cbl RING finger C-terminal flank controls epidermal growth factor receptor fate downstream of receptor ubiquitination
    • Visser GD, Lill NL. The Cbl RING finger C-terminal flank controls epidermal growth factor receptor fate downstream of receptor ubiquitination. Exp Cell Res 2005;311:281-93.
    • (2005) Exp Cell Res , vol.311 , pp. 281-293
    • Visser, G.D.1    Lill, N.L.2
  • 45
    • 0035106341 scopus 로고    scopus 로고
    • Ring finger mutations that abolish c-Cbl-directed polyubiquitination and downregulation of the EGF receptor are insufficient for cell transformation
    • Thien CB, Walker F, Langdon W. Ring finger mutations that abolish c-Cbl-directed polyubiquitination and downregulation of the EGF receptor are insufficient for cell transformation. Mol Cell 2001;7:355-65.
    • (2001) Mol Cell , vol.7 , pp. 355-365
    • Thien, C.B.1    Walker, F.2    Langdon, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.