메뉴 건너뛰기




Volumn 11, Issue 1, 2013, Pages

C3G forms complexes with Bcr-Abl and p38α MAPK at the focal adhesions in chronic myeloid leukemia cells: Implication in the regulation of leukemic cell adhesion

Author keywords

Abi1; Bcr Abl; C3G; Cbl; Cell adhesion; CML; p130Cas; p38 MAPK

Indexed keywords

ALPHA5 INTEGRIN; BCR ABL PROTEIN; CBL PROTEIN; CELL PROTEIN; CRK ASSOCIATED SUBSTRATE PROTEIN; CRK LIKE PROTEIN; FIBRONECTIN; FOCAL ADHESION KINASE; MITOGEN ACTIVATED PROTEIN KINASE 14; PAXILLIN; PROTEIN ABI1; PROTEIN C3G; PROTEIN SH3; TUMOR PROTEIN; UNCLASSIFIED DRUG;

EID: 84874922971     PISSN: None     EISSN: 1478811X     Source Type: Journal    
DOI: 10.1186/1478-811X-11-9     Document Type: Article
Times cited : (24)

References (71)
  • 1
    • 77949828806 scopus 로고    scopus 로고
    • Crk and CrkL adaptor proteins: Networks for physiological and pathological signaling
    • 10.1186/1478-811X-7-13 19426560
    • Crk and CrkL adaptor proteins: networks for physiological and pathological signaling. Birge RB, Kalodimos C, Inagaki F, Tanaka S, Cell Commun Signal 2009 7 13 10.1186/1478-811X-7-13 19426560
    • (2009) Cell Commun Signal , vol.7 , pp. 13
    • Birge, R.B.1    Kalodimos, C.2    Inagaki, F.3    Tanaka, S.4
  • 2
    • 0346101792 scopus 로고    scopus 로고
    • Physical and Functional Interaction between Hck Tyrosine Kinase and Guanine Nucleotide Exchange Factor C3G Results in Apoptosis, Which Is Independent of C3G Catalytic Domain
    • DOI 10.1074/jbc.M310656200
    • Physical and functional interaction between Hck tyrosine kinase and guanine nucleotide exchange factor C3G results in apoptosis, which is independent of C3G catalytic domain. Shivakrupa R, Radha V, Sudhakar C, Swarup G, J Biol Chem 2003 278 52188 52194 10.1074/jbc.M310656200 14551197 (Pubitemid 38035806)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 52188-52194
    • Shivakrupa, R.1    Radha, V.2    Sudhakar, Ch.3    Swarup, G.4
  • 3
    • 34250012883 scopus 로고    scopus 로고
    • C3G is required for c-Abl-induced filopodia and its overexpression promotes filopodia formation
    • DOI 10.1016/j.yexcr.2007.03.019, PII S0014482707001395
    • C3G is required for c-Abl-induced filopodia and its overexpression promotes filopodia formation. Radha V, Rajanna A, Mitra A, Rangaraj N, Swarup G, Exp Cell Res 2007 313 2476 2492 10.1016/j.yexcr.2007.03.019 17475248 (Pubitemid 46891471)
    • (2007) Experimental Cell Research , vol.313 , Issue.11 , pp. 2476-2492
    • Radha, V.1    Rajanna, A.2    Mitra, A.3    Rangaraj, N.4    Swarup, G.5
  • 5
    • 79960113049 scopus 로고    scopus 로고
    • Signalling to actin: Role of C3G, a multitasking guanine-nucleotide- exchange factor
    • 10.1042/BSR20100094 21366540
    • Signalling to actin: role of C3G, a multitasking guanine-nucleotide- exchange factor. Radha V, Mitra A, Dayma K, Sasikumar K, Biosci Rep 2011 31 231 244 10.1042/BSR20100094 21366540
    • (2011) Biosci Rep , vol.31 , pp. 231-244
    • Radha, V.1    Mitra, A.2    Dayma, K.3    Sasikumar, K.4
  • 6
    • 0033152359 scopus 로고    scopus 로고
    • CrkL activates integrin-mediated hematopoietic cell adhesion through the guanine nucleotide exchange factor C3G
    • CrkL activates integrin-mediated hematopoietic cell adhesion through the guanine nucleotide exchange factor C3G. Arai A, Nosaka Y, Kohsaka H, Miyasaka N, Miura O, Blood 1999 93 3713 3722 10339478 (Pubitemid 29249818)
    • (1999) Blood , vol.93 , Issue.11 , pp. 3713-3722
    • Arai, A.1    Nosaka, Y.2    Kohsaka, H.3    Miyasaka, N.4    Miura, O.5
  • 7
    • 0032569839 scopus 로고    scopus 로고
    • C3G is tyrosine-phosphorylated after integrin-mediated cell adhesion in normal but not in Bcr/Ab1 expressing cells
    • C3G is tyrosine-phosphorylated after integrin-mediated cell adhesion in normal but not in Bcr/Abl expressing cells. de Jong R, van Wijk A, Heisterkamp N, Groffen J, Oncogene 1998 17 2805 2810 10.1038/sj.onc.1202207 9840945 (Pubitemid 28554240)
    • (1998) Oncogene , vol.17 , Issue.21 , pp. 2805-2810
    • De Jong, R.1    Van Wijk, A.2    Heisterkamp, N.3    Groffen, J.4
  • 8
    • 33644924043 scopus 로고    scopus 로고
    • Characterization of p87C3G, a novel, truncated C3G isoform that is overexpressed in chronic myeloid leukemia and interacts with Bcr-Abl
    • 10.1016/j.yexcr.2005.12.007 16443220
    • Characterization of p87C3G, a novel, truncated C3G isoform that is overexpressed in chronic myeloid leukemia and interacts with Bcr-Abl. Gutierrez-Berzal J, Castellano E, Martin-Encabo S, Gutierrez-Cianca N, Hernandez JM, Santos E, Guerrero C, Exp Cell Res 2006 312 938 948 10.1016/j.yexcr.2005. 12.007 16443220
    • (2006) Exp Cell Res , vol.312 , pp. 938-948
    • Gutierrez-Berzal, J.1    Castellano, E.2    Martin-Encabo, S.3    Gutierrez-Cianca, N.4    Hernandez, J.M.5    Santos, E.6    Guerrero, C.7
  • 9
    • 77955662809 scopus 로고    scopus 로고
    • F-actin-binding domain of c-Abl regulates localized phosphorylation of C3G: Role of C3G in c-Abl-mediated cell death
    • 10.1038/onc.2010.113 20581864
    • F-actin-binding domain of c-Abl regulates localized phosphorylation of C3G: role of C3G in c-Abl-mediated cell death. Mitra A, Radha V, Oncogene 2010 29 4528 4542 10.1038/onc.2010.113 20581864
    • (2010) Oncogene , vol.29 , pp. 4528-4542
    • Mitra, A.1    Radha, V.2
  • 10
    • 21344443036 scopus 로고    scopus 로고
    • Interaction of Bcr/Abl with C3G, an exchange factor for the small GTPase Rap1, through the adapter protein Crkl
    • DOI 10.1016/j.bbrc.2005.06.030, PII S0006291X05012465
    • Interaction of Bcr/Abl with C3G, an exchange factor for the small GTPase Rap1, through the adapter protein Crkl. Cho YJ, Hemmeryckx B, Groffen J, Heisterkamp N, Biochem Biophys Res Commun 2005 333 1276 1283 10.1016/j.bbrc.2005.06.030 15982636 (Pubitemid 40910140)
    • (2005) Biochemical and Biophysical Research Communications , vol.333 , Issue.4 , pp. 1276-1283
    • Young, J.C.1    Hemmeryckx, B.2    Groffen, J.3    Heisterkamp, N.4
  • 11
    • 27644475483 scopus 로고    scopus 로고
    • Multiple roles of Rap1 in hematopoietic cells: Complementary versus antagonistic functions
    • DOI 10.1182/blood-2005-03-1062
    • Multiple roles of Rap1 in hematopoietic cells: complementary versus antagonistic functions. Stork PJ, Dillon TJ, Blood 2005 106 2952 2961 10.1182/blood-2005-03-1062 16076873 (Pubitemid 41565885)
    • (2005) Blood , vol.106 , Issue.9 , pp. 2952-2961
    • Stork, P.J.S.1    Dillon, T.J.2
  • 14
    • 0026441040 scopus 로고
    • Mechanisms underlying abnormal trafficking of malignant progenitors in chronic myelogenous leukemia. Decreased adhesion to stroma and fibronectin but increased adhesion to the basement membrane components laminin and collagen type IV
    • 10.1172/JCI115985 1383271
    • Mechanisms underlying abnormal trafficking of malignant progenitors in chronic myelogenous leukemia. Decreased adhesion to stroma and fibronectin but increased adhesion to the basement membrane components laminin and collagen type IV. Verfaillie CM, McCarthy JB, McGlave PB, J Clin Invest 1992 90 1232 1241 10.1172/JCI115985 1383271
    • (1992) J Clin Invest , vol.90 , pp. 1232-1241
    • Verfaillie, C.M.1    McCarthy, J.B.2    McGlave, P.B.3
  • 16
    • 64849092800 scopus 로고    scopus 로고
    • C3G silencing enhances STI-571-induced apoptosis in CML cells through p38 MAPK activation, but it antagonizes STI-571 inhibitory effect on survival
    • 10.1016/j.cellsig.2009.03.015 19324082
    • C3G silencing enhances STI-571-induced apoptosis in CML cells through p38 MAPK activation, but it antagonizes STI-571 inhibitory effect on survival. Maia V, Sanz M, Gutierrez-Berzal J, de Luis A, Gutierrez-Uzquiza A, Porras A, Guerrero C, Cell Signal 2009 21 1229 1235 10.1016/j.cellsig.2009.03.015 19324082
    • (2009) Cell Signal , vol.21 , pp. 1229-1235
    • Maia, V.1    Sanz, M.2    Gutierrez-Berzal, J.3    De Luis, A.4    Gutierrez-Uzquiza, A.5    Porras, A.6    Guerrero, C.7
  • 17
    • 71449126669 scopus 로고    scopus 로고
    • C3G down-regulates p38 MAPK activity in response to stress by Rap-1 independent mechanisms: Involvement in cell death
    • 10.1016/j.cellsig.2009.11.008 19925863
    • C3G down-regulates p38 MAPK activity in response to stress by Rap-1 independent mechanisms: Involvement in cell death. Gutiérrez-Uzquiza A, Arechederra M, Molina I, Baños R, Maia V, Benito M, Guerrero C, Porras A, Cell Signal 2010 22 533 542 10.1016/j.cellsig.2009.11.008 19925863
    • (2010) Cell Signal , vol.22 , pp. 533-542
    • Gutiérrez-Uzquiza, A.1    Arechederra, M.2    Molina, I.3    Baños, R.4    Maia, V.5    Benito, M.6    Guerrero, C.7    Porras, A.8
  • 18
    • 33751004130 scopus 로고    scopus 로고
    • Altered cell adhesion and cell viability in a p38α mitogen-activated protein kinase-deficient mouse embryonic stem cell line
    • DOI 10.1089/scd.2006.15.655
    • Altered Cell Adhesion and Cell Viability in a p38alpha Mitogen-Activated Protein Kinase-Deficient Mouse Embryonic Stem Cell Line. Guo YL, Yang B, Stem Cells Dev 2006 15 655 664 10.1089/scd.2006.15.655 17105401 (Pubitemid 44748601)
    • (2006) Stem Cells and Development , vol.15 , Issue.5 , pp. 655-664
    • Guo, Y.-L.1    Yang, B.2
  • 19
    • 34547154349 scopus 로고    scopus 로고
    • P38 MAP-Kinases pathway regulation, function and role in human diseases
    • DOI 10.1016/j.bbamcr.2007.03.010, PII S0167488907000705
    • p38 MAP-kinases pathway regulation, function and role in human diseases. Cuenda A, Rousseau S, Biochim Biophys Acta 2007 1773 1358 1375 10.1016/j.bbamcr.2007.03.010 17481747 (Pubitemid 47125981)
    • (2007) Biochimica et Biophysica Acta - Molecular Cell Research , vol.1773 , Issue.8 , pp. 1358-1375
    • Cuenda, A.1    Rousseau, S.2
  • 20
    • 33744544424 scopus 로고    scopus 로고
    • P38 and a p38-Interacting Protein Are Critical for Downregulation of E-Cadherin during Mouse Gastrulation
    • DOI 10.1016/j.cell.2006.03.048, PII S0092867406005630
    • p38 and a p38-interacting protein are critical for downregulation of E-cadherin during mouse gastrulation. Zohn IE, Li Y, Skolnik EY, Anderson KV, Han J, Niswander L, Cell 2006 125 957 969 10.1016/j.cell.2006.03.048 16751104 (Pubitemid 43810156)
    • (2006) Cell , vol.125 , Issue.5 , pp. 957-969
    • Zohn, I.E.1    Li, Y.2    Skolnik, E.Y.3    Anderson, K.V.4    Han, J.5    Niswander, L.6
  • 21
    • 17644367566 scopus 로고    scopus 로고
    • H-Ras-specific activation of Rac-MKK3/6-p38 pathway: Its critical role in invasion and migration of breast epithelial cells
    • DOI 10.1074/jbc.M411625200
    • H-Ras-specific activation of Rac-MKK3/6-p38 pathway: its critical role in invasion and migration of breast epithelial cells. Shin I, Kim S, Song H, Kim HR, Moon A, J Biol Chem 2005 280 14675 14683 10.1074/jbc.M411625200 15677464 (Pubitemid 40562814)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.15 , pp. 14675-14683
    • Shin, I.1    Kim, S.2    Song, H.3    Kim, H.-R.C.4    Moon, A.5
  • 23
    • 0031946385 scopus 로고    scopus 로고
    • Role of the adapter protein CRKL in signal transduction of normal hematopoietic and BCR/ABL-transformed cells
    • Role of the adapter protein CRKL in signal transduction of normal hematopoietic and BCR/ABL-transformed cells. Sattler M, Salgia R, Leukemia 1998 12 637 644 10.1038/sj.leu.2401010 9593259 (Pubitemid 28220814)
    • (1998) Leukemia , vol.12 , Issue.5 , pp. 637-644
    • Sattler, M.1    Salgia, R.2
  • 24
    • 0030917924 scopus 로고    scopus 로고
    • Interactions of CBL with BCR-ABL and CRKL in BCR-ABL-transformed myeloid cells
    • DOI 10.1074/jbc.272.26.16170
    • Interactions of CBL with BCR-ABL and CRKL in BCR-ABL-transformed myeloid cells. Bhat A, Kolibaba K, Oda T, Ohno-Jones S, Heaney C, Druker BJ, J Biol Chem 1997 272 16170 16175 10.1074/jbc.272.26.16170 9195915 (Pubitemid 27276433)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.26 , pp. 16170-16175
    • Bhat, A.1    Kolibaba, K.2    Oda, T.3    Ohno-Jones, S.4    Heaney, C.5    Druker, B.J.6
  • 25
    • 0033519691 scopus 로고    scopus 로고
    • Involvement of the adapter protein CRKL in integrin-mediated adhesion
    • DOI 10.1038/sj.onc.1202689
    • Involvement of the adapter protein CRKL in integrin-mediated adhesion. Uemura N, Salgia R, Ewaniuk DS, Little MT, Griffin JD, Oncogene 1999 18 3343 3353 10.1038/sj.onc.1202689 10362355 (Pubitemid 29286980)
    • (1999) Oncogene , vol.18 , Issue.22 , pp. 3343-3353
    • Uemura, N.1    Salgia, R.2    Ewaniuk, D.S.3    Little, M.-T.4    Griffin, J.D.5
  • 26
    • 0036161707 scopus 로고    scopus 로고
    • PKA phosphorylation of Src mediates cAMP's inhibition of cell growth via Rap1
    • DOI 10.1016/S1097-2765(01)00432-4
    • PKA phosphorylation of Src mediates cAMP's inhibition of cell growth via Rap1. Schmitt JM, Stork PJ, Mol Cell 2002 9 85 94 10.1016/S1097-2765(01)00432-4 11804588 (Pubitemid 34127773)
    • (2002) Molecular Cell , vol.9 , Issue.1 , pp. 85-94
    • Schmitt, J.M.1    Stork, P.J.S.2
  • 27
    • 53349164086 scopus 로고    scopus 로고
    • Inhibitory Receptor Signaling via Tyrosine Phosphorylation of the Adaptor Crk
    • 10.1016/j.immuni.2008.07.014 18835194
    • Inhibitory Receptor Signaling via Tyrosine Phosphorylation of the Adaptor Crk. Peterson ME, Long EO, Immunity 2008 29 578 588 10.1016/j.immuni.2008.07. 014 18835194
    • (2008) Immunity , vol.29 , pp. 578-588
    • Peterson, M.E.1    Long, E.O.2
  • 28
    • 0029876948 scopus 로고    scopus 로고
    • Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G
    • DOI 10.1074/jbc.271.14.8435
    • Stimulation through the T cell receptor induces Cbl association with Crk proteins and the guanine nucleotide exchange protein C3G. Reedquist KA, Fukazawa T, Panchamoorthy G, Langdon WY, Shoelson SE, Druker BJ, Band H, J Biol Chem 1996 271 8435 8442 10.1074/jbc.271.14.8435 8626543 (Pubitemid 26108681)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.14 , pp. 8435-8442
    • Reedquist, K.A.1    Fukazawa, T.2    Panchamoorthy, G.3    Langdon, W.Y.4    Shoelson, S.E.5    Druker, B.J.6    Band, H.7
  • 29
    • 0032475982 scopus 로고    scopus 로고
    • Direct binding of p130(Cas) to the guanine nucleotide exchange factor C3G
    • DOI 10.1074/jbc.273.40.25673
    • Direct binding of p130(Cas) to the guanine nucleotide exchange factor C3G. Kirsch KH, Georgescu MM, Hanafusa H, J Biol Chem 1998 273 25673 25679 10.1074/jbc.273.40.25673 9748234 (Pubitemid 28475789)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.40 , pp. 25673-25679
    • Kirsch, K.H.1    Georgescu, M.-M.2    Hanafusa, H.3
  • 30
    • 0026743906 scopus 로고
    • Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho
    • 10.1126/science.1379745 1379745
    • Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho. Cicchetti P, Mayer BJ, Thiel G, Baltimore D, Science 1992 257 803 806 10.1126/science.1379745 1379745
    • (1992) Science , vol.257 , pp. 803-806
    • Cicchetti, P.1    Mayer, B.J.2    Thiel, G.3    Baltimore, D.4
  • 31
    • 0028844631 scopus 로고
    • Abl-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the Abl protein, suppresses v-abl transforming activity
    • 10.1101/gad.9.21.2583 7590237
    • Abl-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the Abl protein, suppresses v-abl transforming activity. Shi Y, Alin K, Goff SP, Genes Dev 1995 9 2583 2597 10.1101/gad.9.21.2583 7590237
    • (1995) Genes Dev , vol.9 , pp. 2583-2597
    • Shi, Y.1    Alin, K.2    Goff, S.P.3
  • 32
    • 11944275667 scopus 로고
    • Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity
    • 10.1101/gad.9.21.2569 7590236
    • Abi-2, a novel SH3-containing protein interacts with the c-Abl tyrosine kinase and modulates c-Abl transforming activity. Dai Z, Pendergast AM, Genes Dev 1995 9 2569 2582 10.1101/gad.9.21.2569 7590236
    • (1995) Genes Dev , vol.9 , pp. 2569-2582
    • Dai, Z.1    Pendergast, A.M.2
  • 33
    • 0029956391 scopus 로고    scopus 로고
    • C-ABL tyrosine kinase activity is regulated by association with a novel SH3-domain-binding protein
    • c-ABL tyrosine kinase activity is regulated by association with a novel SH3-domain-binding protein. Zhu J, Shore SK, Mol Cell Biol 1996 16 7054 7062 8943360 (Pubitemid 26389764)
    • (1996) Molecular and Cellular Biology , vol.16 , Issue.12 , pp. 7054-7062
    • Zhu, J.1    Shore, S.K.2
  • 34
    • 0342762061 scopus 로고    scopus 로고
    • Regulation of the oncogenic activity of BCR-ABL by a tightly bound substrate protein RIN1
    • DOI 10.1016/S1074-7613(00)80452-5
    • Regulation of the oncogenic activity of BCR-ABL by a tightly bound substrate protein RIN1. Afar DE, Han L, McLaughlin J, Wong S, Dhaka A, Parmar K, Rosenberg N, Witte ON, Colicelli J, Immunity 1997 6 773 782 10.1016/S1074-7613(00)80452-5 9208849 (Pubitemid 27305739)
    • (1997) Immunity , vol.6 , Issue.6 , pp. 773-782
    • Afar, D.E.H.1    Limin, H.2    McLaughlin, J.3    Wong, S.4    Dhaka, A.5    Parmar, K.6    Rosenberg, N.7    Witte, O.N.8    Colicelli, J.9
  • 35
    • 0030803669 scopus 로고    scopus 로고
    • The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c- Abl tyrosine kinase activity
    • The PAG gene product, a stress-induced protein with antioxidant properties, is an Abl SH3-binding protein and a physiological inhibitor of c-Abl tyrosine kinase activity. Wen ST, Van Etten RA, Genes Dev 1997 11 2456 2467 10.1101/gad.11.19.2456 9334312 (Pubitemid 27438828)
    • (1997) Genes and Development , vol.11 , Issue.19 , pp. 2456-2467
    • Wen, S.-T.1    Van Etten, R.A.2
  • 36
    • 0028181873 scopus 로고
    • Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites
    • 10.1101/gad.8.7.783 7926767
    • Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites. Ren R, Ye ZS, Baltimore D, Genes Dev 1994 8 783 795 10.1101/gad.8.7.783 7926767
    • (1994) Genes Dev , vol.8 , pp. 783-795
    • Ren, R.1    Ye, Z.S.2    Baltimore, D.3
  • 37
    • 0028142490 scopus 로고
    • Crkl is the major tyrosine-phosphorylated protein in neutrophils from patients with chronic myelogenous leukemia
    • Crkl is the major tyrosine-phosphorylated protein in neutrophils from patients with chronic myelogenous leukemia. Oda T, Heaney C, Hagopian JR, Okuda K, Griffin JD, Druker BJ, J Biol Chem 1994 269 22925 22928 8083188 (Pubitemid 24283264)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.37 , pp. 22925-22928
    • Oda, T.1    Heaney, C.2    Hagopian, J.R.3    Okuda, K.4    Griffin, J.D.5    Druker, B.J.6
  • 38
    • 0029813117 scopus 로고    scopus 로고
    • A potential SH3 domain-binding site in the Crk SH2 domain
    • DOI 10.1074/jbc.271.35.21365
    • A potential SH3 domain-binding site in the Crk SH2 domain. Anafi M, Rosen MK, Gish GD, Kay LE, Pawson T, J Biol Chem 1996 271 21365 21374 10.1074/jbc.271.35.21365 8702917 (Pubitemid 26292999)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.35 , pp. 21365-21374
    • Anafi, M.1    Rosen, M.K.2    Gish, G.D.3    Kay, L.E.4    Pawson, T.5
  • 39
    • 0031038399 scopus 로고    scopus 로고
    • Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation
    • Direct binding of CRKL to BCR-ABL is not required for BCR-ABL transformation. Heaney C, Kolibaba K, Bhat A, Oda T, Ohno S, Fanning S, Druker BJ, Blood 1997 89 297 306 8978305 (Pubitemid 26428206)
    • (1997) Blood , vol.89 , Issue.1 , pp. 297-306
    • Heaney, C.1    Kolibaba, K.2    Bhat, A.3    Oda, T.4    Ohno, S.5    Fanning, S.6    Druker, B.J.7
  • 41
    • 0029006745 scopus 로고
    • Cloning and characterization of cbl-b: A SH3 binding protein with homology to the c-cbl proto-oncogene
    • 7784085
    • Cloning and characterization of cbl-b: a SH3 binding protein with homology to the c-cbl proto-oncogene. Keane MM, Rivero-Lezcano OM, Mitchell JA, Robbins KC, Lipkowitz S, Oncogene 1995 10 2367 2377 7784085
    • (1995) Oncogene , vol.10 , pp. 2367-2377
    • Keane, M.M.1    Rivero-Lezcano, O.M.2    Mitchell, J.A.3    Robbins, K.C.4    Lipkowitz, S.5
  • 42
    • 0029034440 scopus 로고
    • Interactions of Cbl with Grb2 and phosphatidylinositol 3'-kinase in activated Jurkat cells
    • 7791764
    • Interactions of Cbl with Grb2 and phosphatidylinositol 3'-kinase in activated Jurkat cells. Meisner H, Conway BR, Hartley D, Czech MP, Mol Cell Biol 1995 15 3571 3578 7791764
    • (1995) Mol Cell Biol , vol.15 , pp. 3571-3578
    • Meisner, H.1    Conway, B.R.2    Hartley, D.3    Czech, M.P.4
  • 43
    • 77949862490 scopus 로고    scopus 로고
    • The final steps of integrin activation: The end game
    • 10.1038/nrm2871 20308986
    • The final steps of integrin activation: the end game. Shattil SJ, Kim C, Ginsberg M, Nat Rev Mol Cell Biol 2010 11 288 300 10.1038/nrm2871 20308986
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 288-300
    • Shattil, S.J.1    Kim, C.2    Ginsberg, M.3
  • 44
    • 50249107474 scopus 로고    scopus 로고
    • Paxillin comes of age
    • 10.1242/jcs.018044 18650496
    • Paxillin comes of age. Deakin NO, Turner CE, J Cell Sci 2008 121 2435 2444 10.1242/jcs.018044 18650496
    • (2008) J Cell Sci , vol.121 , pp. 2435-2444
    • Deakin, N.O.1    Turner, C.E.2
  • 47
    • 0029664864 scopus 로고    scopus 로고
    • P210(BCR/ABL) induces formation of complexes containing focal adhesion proteins and the protooncogene product p120(c-Cbl)
    • p210BCR/ABL induces formation of complexes containing focal adhesion proteins and the protooncogene product p120c-Cbl. Salgia R, Sattler M, Pisick E, Li JL, Griffin JD, Exp Hematol 1996 24 310 313 8641358 (Pubitemid 26096310)
    • (1996) Experimental Hematology , vol.24 , Issue.2 , pp. 310-313
    • Salgia, R.1    Sattler, M.2    Pisick, E.3    Li, J.-L.4    Griffin, J.D.5
  • 48
    • 0035475308 scopus 로고    scopus 로고
    • CrK family adaptors-signalling complex formation and biological roles
    • DOI 10.1038/sj.onc.1204779
    • Crk family adaptors-signalling complex formation and biological roles. Feller SM, Oncogene 2001 20 6348 6371 10.1038/sj.onc.1204779 11607838 (Pubitemid 32977844)
    • (2001) Oncogene , vol.20 , Issue.44 , pp. 6348-6371
    • Feller, S.M.1
  • 49
    • 70349509457 scopus 로고    scopus 로고
    • Adaptor protein Crk induces Src-dependent activation of p38 MAPK in regulation of synovial sarcoma cell proliferation
    • 10.1158/1541-7786.MCR-09-0064 19737974
    • Adaptor protein Crk induces Src-dependent activation of p38 MAPK in regulation of synovial sarcoma cell proliferation. Watanabe T, Tsuda M, Tanaka S, Ohba Y, Kawaguchi H, Majima T, Sawa H, Minami A, Mol Cancer Res 2009 7 1582 1592 10.1158/1541-7786.MCR-09-0064 19737974
    • (2009) Mol Cancer Res , vol.7 , pp. 1582-1592
    • Watanabe, T.1    Tsuda, M.2    Tanaka, S.3    Ohba, Y.4    Kawaguchi, H.5    Majima, T.6    Sawa, H.7    Minami, A.8
  • 50
    • 49949152321 scopus 로고    scopus 로고
    • C-Cbl facilitates cytoskeletal effects in v-Abl transformed fibroblast through Rac1- and Rap1-mediated signaling
    • 10.1016/j.biocel.2008.02.013 18403249
    • c-Cbl facilitates cytoskeletal effects in v-Abl transformed fibroblast through Rac1- and Rap1-mediated signaling. Lee H, Gaughan J, Tsygankov A, Int J Biochem Cell Biol 2008 40 1930 1943 10.1016/j.biocel.2008.02.013 18403249
    • (2008) Int J Biochem Cell Biol , vol.40 , pp. 1930-1943
    • Lee, H.1    Gaughan, J.2    Tsygankov, A.3
  • 51
    • 77949327323 scopus 로고    scopus 로고
    • A BCR-ABL mutant lacking direct binding sites for the GRB2, CBL and CRKL adapter proteins fails to induce leukemia in mice
    • 10.1371/journal.pone.0007439 19823681
    • A BCR-ABL mutant lacking direct binding sites for the GRB2, CBL and CRKL adapter proteins fails to induce leukemia in mice. Johnson K, Griswold I, O'hare T, Corbin A, Loriaux M, Deininger M, Druker BJ, PLoS ONE 2009 4 7439 10.1371/journal.pone.0007439 19823681
    • (2009) PLoS ONE , vol.4 , pp. 57439
    • Johnson, K.1    Griswold, I.2    O'Hare, T.3    Corbin, A.4    Loriaux, M.5    Deininger, M.6    Druker, B.J.7
  • 52
    • 77954240253 scopus 로고    scopus 로고
    • Dynamics and mechanism of p130Cas localization to focal adhesions
    • 10.1074/jbc.M109.091207 20430882
    • Dynamics and mechanism of p130Cas localization to focal adhesions. Donato DM, Ryzhova LM, Meenderink LM, Kaverina I, Hanks SK, J Biol Chem 2010 285 20769 20779 10.1074/jbc.M109.091207 20430882
    • (2010) J Biol Chem , vol.285 , pp. 20769-20779
    • Donato, D.M.1    Ryzhova, L.M.2    Meenderink, L.M.3    Kaverina, I.4    Hanks, S.K.5
  • 53
    • 78149441694 scopus 로고    scopus 로고
    • P130Cas Src-binding and substrate domains have distinct roles in sustaining focal adhesion disassembly and promoting cell migration
    • 10.1371/journal.pone.0013412 20976150
    • P130Cas Src-binding and substrate domains have distinct roles in sustaining focal adhesion disassembly and promoting cell migration. Meenderink LM, Ryzhova LM, Donato DM, Gochberg DF, Kaverina I, Hanks SK, PLoS One 2010 5 13412 10.1371/journal.pone.0013412 20976150
    • (2010) PLoS One , vol.5 , pp. 513412
    • Meenderink, L.M.1    Ryzhova, L.M.2    Donato, D.M.3    Gochberg, D.F.4    Kaverina, I.5    Hanks, S.K.6
  • 54
    • 0037262297 scopus 로고    scopus 로고
    • The guanine nucleotide exchange factor C3G is necessary for the formation of focal adhesions and vascular maturation
    • DOI 10.1242/dev.00217
    • The guanine nucleotide exchange factor C3G is necessary for the formation of focal adhesions and vascular maturation. Voss AK, Gruss P, Thomas T, Development 2003 130 355 367 10.1242/dev.00217 12466202 (Pubitemid 36175933)
    • (2003) Development , vol.130 , Issue.2 , pp. 355-367
    • Voss, A.K.1    Gruss, P.2    Thomas, T.3
  • 55
    • 34249110123 scopus 로고    scopus 로고
    • Bcr-Abl induces abnormal cytoskeleton remodelling, β1 integrin clustering and increased cell adhesion to fibronectin through the Abl interactor 1 pathway
    • DOI 10.1242/jcs.03430
    • Bcr-Abl induces abnormal cytoskeleton remodeling, beta1 integrin clustering and increased cell adhesion to fibronectin through the Abl interactor 1 pathway. Li Y, Clough N, Sun X, Yu W, Abbott BL, Hogan CJ, Dai Z, J Cell Sci 2007 120 1436 1446 10.1242/jcs.03430 17389688 (Pubitemid 46780036)
    • (2007) Journal of Cell Science , vol.120 , Issue.8 , pp. 1436-1446
    • Li, Y.1    Clough, N.2    Sun, X.3    Yu, W.4    Abbott, B.L.5    Hogan, C.J.6    Dai, Z.7
  • 56
    • 0037592093 scopus 로고    scopus 로고
    • Negative regulation of T cell antigen receptor-mediated Crk-L-C3G signaling and cell adhesion by Cbl-b
    • DOI 10.1074/jbc.M212671200
    • Negative regulation of T cell antigen receptor-mediated Crk-L-C3G signaling and cell adhesion by Cbl-b. Zhang W, Shao Y, Fang D, Huang J, Jeon MS, Liu YC, J Biol Chem 2003 278 23978 23983 10.1074/jbc.M212671200 12697763 (Pubitemid 36830227)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.26 , pp. 23978-23983
    • Zhang, W.1    Shao, Y.2    Fang, D.3    Huang, J.4    Jeon, M.-S.5    Liu, Y.-C.6
  • 57
    • 77449137856 scopus 로고    scopus 로고
    • Roles of E3 ubiquitin ligases in cell adhesion and migration
    • 10.4161/cam.4.1.9834 20009572
    • Roles of E3 ubiquitin ligases in cell adhesion and migration. Huang C, Cell Adh Migr 2010 4 10 18 10.4161/cam.4.1.9834 20009572
    • (2010) Cell Adh Migr , vol.4 , pp. 10-18
    • Huang, C.1
  • 58
    • 0032509565 scopus 로고    scopus 로고
    • Identification of p130(Cas) as a mediator of focal adhesion kinase- promoted cell migration
    • DOI 10.1083/jcb.140.1.211
    • Identification of p130Cas as a mediator of focal adhesion kinase-promoted cell migration. Cary LA, Han DC, Polte TR, Hanks SK, Guan JL, J Cell Biol 1998 140 211 221 10.1083/jcb.140.1.211 9425168 (Pubitemid 28070908)
    • (1998) Journal of Cell Biology , vol.140 , Issue.1 , pp. 211-221
    • Cary, L.A.1    Han, D.C.2    Polte, T.R.3    Hanks, S.K.4    Guan, J.-L.5
  • 59
    • 70350453823 scopus 로고    scopus 로고
    • The role of focal adhesion kinase in tumor initiation and progression
    • 10.4161/cam.3.4.9458 19690467
    • The role of focal adhesion kinase in tumor initiation and progression. Provenzano PP, Keely PJ, Cell Adh Migr 2009 3 347 350 10.4161/cam.3.4.9458 19690467
    • (2009) Cell Adh Migr , vol.3 , pp. 347-350
    • Provenzano, P.P.1    Keely, P.J.2
  • 60
    • 68949132900 scopus 로고    scopus 로고
    • Arachidonic acid stimulates cell adhesion through a novel p38 MAPK-RhoA signaling pathway that involves heat shock protein 27
    • 10.1074/jbc.M109.020271 19506078
    • Arachidonic acid stimulates cell adhesion through a novel p38 MAPK-RhoA signaling pathway that involves heat shock protein 27. Garcia MC, Ray DM, Lackford B, Rubino M, Olden K, Roberts JD, J Biol Chem 2009 284 20936 20945 10.1074/jbc.M109.020271 19506078
    • (2009) J Biol Chem , vol.284 , pp. 20936-20945
    • Garcia, M.C.1    Ray, D.M.2    Lackford, B.3    Rubino, M.4    Olden, K.5    Roberts, J.D.6
  • 61
    • 23044510616 scopus 로고    scopus 로고
    • 1, adhesion to extracellular matrix, and tumorigenicity of T-anaplastic large cell lymphoma Karpas 299
    • DOI 10.1158/0008-5472.CAN-05-0647
    • CD26 regulates p38 mitogen-activated protein kinase-dependent phosphorylation of integrin beta1, adhesion to extracellular matrix, and tumorigenicity of T-anaplastic large cell lymphoma Karpas 299. Sato T, Yamochi T, Yamochi T, Aytac U, Ohnuma K, McKee KS, Morimoto C, Dang NH, Cancer Res 2005 65 6950 6956 10.1158/0008-5472.CAN-05-0647 16061680 (Pubitemid 41060735)
    • (2005) Cancer Research , vol.65 , Issue.15 , pp. 6950-6956
    • Sato, T.1    Yamochi, T.2    Yamochi, T.3    Aytac, U.4    Ohnuma, K.5    McKee, K.S.6    Morimoto, C.7    Dang, N.H.8
  • 62
    • 34547091942 scopus 로고    scopus 로고
    • P38α MAPK can positively or negatively regulate Rac-1 activity depending on the presence of serum
    • DOI 10.1016/j.febslet.2007.06.078, PII S0014579307007521
    • p38alpha MAPK can positively or negatively regulate Rac-1 activity depending on the presence of serum. Zuluaga S, Gutierrez-Uzquiza A, Bragado P, Alvarez-Barrientos A, Benito M, Nebreda AR, Porras A, FEBS Lett 2007 581 3819 3825 10.1016/j.febslet.2007.06.078 17658519 (Pubitemid 47102312)
    • (2007) FEBS Letters , vol.581 , Issue.20 , pp. 3819-3825
    • Zuluaga, S.1    Gutierrez-Uzquiza, A.2    Bragado, P.3    Alvarez-Barrientos, A.4    Benito, M.5    Nebreda, A.R.6    Porras, A.7
  • 63
    • 0034213138 scopus 로고    scopus 로고
    • P38 MAP kinases: Beyond the stress response
    • DOI 10.1016/S0968-0004(00)01595-4, PII S0968000400015954
    • p38 MAP kinases: beyond the stress response. Nebreda AR, Porras A, Trends Biochem Sci 2000 25 257 260 10.1016/S0968-0004(00)01595-4 10838561 (Pubitemid 30333380)
    • (2000) Trends in Biochemical Sciences , vol.25 , Issue.6 , pp. 257-260
    • Nebreda, A.R.1    Porras, A.2
  • 64
    • 0037049761 scopus 로고    scopus 로고
    • Mechanisms underlying abnormal trafficking and expansion of malignant progenitors in CML: BCR/ABL-induced defects in integrin function in CML
    • DOI 10.1038/sj.onc.1206088
    • Mechanisms underlying abnormal trafficking and expansion of malignant progenitors in CML: BCR/ABL-induced defects in integrin function in CML. Salesse S, Verfaillie CM, Oncogene 2002 21 8605 8611 10.1038/sj.onc.1206088 12476307 (Pubitemid 36084193)
    • (2002) Oncogene , vol.21 , Issue.56 , pp. 8605-8611
    • Salesse, S.1    Verfaillie, C.M.2
  • 65
    • 0042170248 scopus 로고    scopus 로고
    • Autoinhibition of Bcr-Abl through its SH3 domain
    • DOI 10.1016/S1097-2765(03)00274-0
    • Autoinhibition of Bcr-Abl through its SH3 domain. Smith KM, Yacobi R, Van Etten RA, Mol Cell 2003 12 27 37 10.1016/S1097-2765(03)00274-0 12887890 (Pubitemid 36945035)
    • (2003) Molecular Cell , vol.12 , Issue.1 , pp. 27-37
    • Smith, K.M.1    Yacobi, R.2    Van Etten, R.A.3
  • 66
    • 0032485067 scopus 로고    scopus 로고
    • Transformation suppressor activity of C3G is independent of its CDC25-homology domain
    • Transformation suppressor activity of C3G is independent of its CDC25-homology domain. Guerrero C, Fernandez-Medarde A, Rojas JM, Font de Mora J, Esteban LM, Santos E, Oncogene 1998 16 613 624 10.1038/sj.onc.1201569 9482107 (Pubitemid 28062341)
    • (1998) Oncogene , vol.16 , Issue.5 , pp. 613-624
    • Guerrero, C.1    Fernandez-Medarde, A.2    Rojas, J.M.3    Font De Mora, J.4    Esteban, L.M.5    Santos, E.6
  • 67
    • 0028983057 scopus 로고
    • Integrin beta 3 cytoplasmic tail is necessary and sufficient for regulation of alpha 5 beta 1 phagocytosis by alpha v beta 3 and integrin-associated protein
    • 10.1083/jcb.130.3.745 7542659
    • Integrin beta 3 cytoplasmic tail is necessary and sufficient for regulation of alpha 5 beta 1 phagocytosis by alpha v beta 3 and integrin-associated protein. Blystone SD, Lindberg FP, LaFlamme SE, Brown EJ, J Cell Biol 1995 130 745 754 10.1083/jcb.130.3.745 7542659
    • (1995) J Cell Biol , vol.130 , pp. 745-754
    • Blystone, S.D.1    Lindberg, F.P.2    LaFlamme, S.E.3    Brown, E.J.4
  • 68
    • 35248837376 scopus 로고    scopus 로고
    • C3G mediated suppression of malignant transformation involves activation of PP2A phosphatases at the subcortical actin cytoskeleton
    • DOI 10.1016/j.yexcr.2007.07.036, PII S0014482707003667
    • C3G mediated suppression of malignant transformation involves activation of PP2A phosphatases at the subcortical actin cytoskeleton. Martin-Encabo S, Santos E, Guerrero C, Exp Cell Res 2007 313 3881 3891 10.1016/j.yexcr.2007.07. 036 17825818 (Pubitemid 47561894)
    • (2007) Experimental Cell Research , vol.313 , Issue.18 , pp. 3881-3891
    • Martin-Encabo, S.1    Santos, E.2    Guerrero, C.3
  • 69
    • 67349092209 scopus 로고    scopus 로고
    • Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes
    • 10.1038/emboj.2009.48 19242489
    • Structural basis of the interaction between integrin alpha6beta4 and plectin at the hemidesmosomes. de Pereda JM, Lillo MP, Sonnenberg A, EMBO J 2009 28 1180 1190 10.1038/emboj.2009.48 19242489
    • (2009) EMBO J , vol.28 , pp. 1180-1190
    • De Pereda, J.M.1    Lillo, M.P.2    Sonnenberg, A.3
  • 70
    • 0141631492 scopus 로고    scopus 로고
    • Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin β4
    • DOI 10.1016/S0969-2126(03)00090-X
    • Structural and functional analysis of the actin binding domain of plectin suggests alternative mechanisms for binding to F-actin and integrin beta4. Garcia-Alvarez B, Bobkov A, Sonnenberg A, de Pereda JM, Structure 2003 11 615 625 10.1016/S0969-2126(03)00090-X 12791251 (Pubitemid 37281178)
    • (2003) Structure , vol.11 , Issue.6 , pp. 615-625
    • Garcia-Alvarez, B.1    Bobkov, A.2    Sonnenberg, A.3    De Pereda, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.