메뉴 건너뛰기




Volumn 5, Issue 1, 2005, Pages 51-63

Integrin-linked kinase: A cancer therapeutic target unique among its ILK

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ADAPTOR PROTEIN; CANCER GROWTH FACTOR; CELL RECEPTOR; GROWTH FACTOR; INTEGRIN; INTEGRIN LINKED KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOTRANSFERASE INHIBITOR; PROTEIN KINASE B; UVOMORULIN; VASCULOTROPIN;

EID: 11144225205     PISSN: 1474175X     EISSN: None     Source Type: Journal    
DOI: 10.1038/nrc1524     Document Type: Review
Times cited : (527)

References (133)
  • 1
    • 0030026679 scopus 로고    scopus 로고
    • Regulation of cell adhesion and anchorage-dependent growth by a new β1-integrin-linked protein kinase
    • Hannigan, G. E. et al. Regulation of cell adhesion and anchorage-dependent growth by a new β1-integrin-linked protein kinase. Nature 379, 91-96 (1996). First report of the identification of ILK. Demonstration of an interaction with β1-integrin cytoplasmic domain and function in the regulation of anchorage-dependent growth of epithelial cells.
    • (1996) Nature , vol.379 , pp. 91-96
    • Hannigan, G.E.1
  • 2
    • 0035809918 scopus 로고    scopus 로고
    • Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane
    • Zervas, C. G., Gregory, S. L. & Brown, N. H. Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane. J. Cell Biol. 152, 1007-1018 (2001).
    • (2001) J. Cell Biol. , vol.152 , pp. 1007-1018
    • Zervas, C.G.1    Gregory, S.L.2    Brown, N.H.3
  • 3
    • 0037076211 scopus 로고    scopus 로고
    • Elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes
    • Mackinnon, A. C., Qadota, H., Norman, K. R., Moerman, D. G. & Williams, B. D. C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr. Biol. 12, 787-797 (2002). References 2 and 3 provide genetic evidence in model oganisms for the integrin-ILK connection and show conserved evolutionary function of ILK.
    • (2002) Curr. Biol. , vol.12 , pp. 787-797
    • Mackinnon, A.C.1    Qadota, H.2    Norman, K.R.3    Moerman, D.G.4    Williams, B.D.C.5
  • 4
    • 0345103747 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation
    • Sakai, T. et al. Integrin-linked kinase (ILK) is required for polarizing the epiblast, cell adhesion, and controlling actin accumulation. Genes Dev. 17, 926-940 (2003).
    • (2003) Genes Dev. , vol.17 , pp. 926-940
    • Sakai, T.1
  • 5
    • 0037904987 scopus 로고    scopus 로고
    • The integrin-actin connection, an eternal love affair
    • Brakebusch, C. & Fassler, R. The integrin-actin connection, an eternal love affair. EMBO J. 22, 2324-2333 (2003).
    • (2003) EMBO J. , vol.22 , pp. 2324-2333
    • Brakebusch, C.1    Fassler, R.2
  • 6
    • 3042708179 scopus 로고    scopus 로고
    • The PINCH-ILK-parvin complexes: Assembly, functions and regulation
    • Wu, C. The PINCH-ILK-parvin complexes: assembly, functions and regulation. Biochim. Biophys. Acta 1692, 55-62 (2004).
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 55-62
    • Wu, C.1
  • 7
    • 0035969233 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) and its interactors: A new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes
    • Wu, C. & Dedhar, S. Integrin-linked kinase (ILK) and its interactors: a new paradigm for the coupling of extracellular matrix to actin cytoskeleton and signaling complexes. J. Cell Biol. 155, 505-510 (2001).
    • (2001) J. Cell Biol. , vol.155 , pp. 505-510
    • Wu, C.1    Dedhar, S.2
  • 8
    • 2542468783 scopus 로고    scopus 로고
    • Affixin interacts with α-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interaction
    • Yamaji, S. et al. Affixin interacts with α-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interaction. J. Cell Biol. 165, 539-551 (2004).
    • (2004) J. Cell Biol. , vol.165 , pp. 539-551
    • Yamaji, S.1
  • 9
    • 18644372487 scopus 로고    scopus 로고
    • Possible role of ILK-affixin complex in integrin-cytoskeleton linkage during platelet aggregation
    • Yamaji, S. et al. Possible role of ILK-affixin complex in integrin-cytoskeleton linkage during platelet aggregation. Biochem. Biophys. Res. Commun. 297, 1324-1331 (2002).
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 1324-1331
    • Yamaji, S.1
  • 10
    • 0038724824 scopus 로고    scopus 로고
    • The role of integrin-linked kinase (ILK) in cancer progression
    • Persad, S. & Dedhar, S. The role of integrin-linked kinase (ILK) in cancer progression. Cancer Metastasis Rev. 22, 375-384 (2003).
    • (2003) Cancer Metastasis Rev. , vol.22 , pp. 375-384
    • Persad, S.1    Dedhar, S.2
  • 11
    • 1642587815 scopus 로고    scopus 로고
    • Regulation of E-cadherin expression and β-catenin/Tcf transcriptional activity by the integrin-linked kinase
    • Oloumi, A., McPhee, T. & Dedhar, S. Regulation of E-cadherin expression and β-catenin/Tcf transcriptional activity by the integrin-linked kinase. Biochim. Bophys. Acta 1691, 1-15 (2004).
    • (2004) Biochim. Bophys. Acta , vol.1691 , pp. 1-15
    • Oloumi, A.1    McPhee, T.2    Dedhar, S.3
  • 12
    • 0035844257 scopus 로고    scopus 로고
    • 2+-independent smooth muscle contraction, a novel function for integrin-linked kinase
    • 2+-independent smooth muscle contraction, a novel function for integrin-linked kinase. J. Biol. Chem. 276, 16365-16373 (2001). An unbiased approach providing biochemical data demonstrating that ILK is a bona fide serine/threonine protein kinase.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16365-16373
    • Deng, J.T.1    Van Lierop, J.E.2    Sutherland, C.3    Walsh, M.P.4
  • 13
    • 4644322059 scopus 로고    scopus 로고
    • ILK is required for the assembly of matrix-forming adhesions and capillary morphogenesis in endothelial cells
    • Vouret-Craviari, V., Boulter, E., Grall, D., Matthews, C. & Van Obberghen-Schilling, E. ILK is required for the assembly of matrix-forming adhesions and capillary morphogenesis in endothelial cells. J. Cell Sci. 117, 4539-4569 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 4539-4569
    • Vouret-Craviari, V.1    Boulter, E.2    Grall, D.3    Matthews, C.4    Van Obberghen-Schilling, E.5
  • 14
    • 4444305175 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates endothelial cell survival and vascular develpment
    • Friedrich, E. B. et al. Integrin-linked kinase regulates endothelial cell survival and vascular develpment. Mol. Cell. Biol. 24, 8134-8144 (2004). Endothelial-cell-specific knockout demonstrating an essential role of ILK in vascular development and angiogenesis. Demonstrates an essential role of ILK in the control of endothelial-cell survival.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8134-8144
    • Friedrich, E.B.1
  • 15
    • 9144270454 scopus 로고    scopus 로고
    • Regulation of tumor angiogenesis by integrin-linked kinase (ILK)
    • Tan, C. et al. Regulation of tumor angiogenesis by integrin-linked kinase (ILK). Cancer Cell 5, 79-90 (2004). Shows that ILK can promote the expression and synthesis of VEGF by prostate cancer cells, and also that ILK is required for VEGF-induced angiogenic response. Also shows the efficacy of ILK inhibitors in suppressing tumour angiogenesis and growth in vivo, and provides a framework for ILK as a two-hit therapeutic target for tumour angiogenesis.
    • (2004) Cancer Cell , vol.5 , pp. 79-90
    • Tan, C.1
  • 16
    • 0842280613 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates vascular morphogenesis induced by vascular endothelial growth factor
    • Kaneko, Y., Kitazato, K., & Basaki, Y. Integrin-linked kinase regulates vascular morphogenesis induced by vascular endothelial growth factor. J. Cell Sci. 117, 407-415 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 407-415
    • Kaneko, Y.1    Kitazato, K.2    Basaki, Y.3
  • 17
    • 0035920145 scopus 로고    scopus 로고
    • Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: Critical roles for kinase activity and amino adds arginine 211 and serine 343
    • Persad, S. et al. Regulation of protein kinase B/Akt-serine 473 phosphorylation by integrin-linked kinase: critical roles for kinase activity and amino adds arginine 211 and serine 343. J. Biol. Chem. 276, 27462-27469 (2001). In depth biochemical analysis of ILK as a Ser473 kinase for AKT. Characterization of critical amino acids involved in the regulation of ILK activity, and characterization of small-molecule ILK inhibitors.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27462-27469
    • Persad, S.1
  • 18
    • 0035804215 scopus 로고    scopus 로고
    • -/- human colon carcinoma cells
    • -/- human colon carcinoma cells. Oncogene 20, 133-140 (2001).
    • (2001) Oncogene , vol.20 , pp. 133-140
    • Tan, C.1
  • 20
    • 0015266211 scopus 로고
    • Cytochalasin B: Effects on cell morphology, cell adhesion, and mucopolysaccharide synthesis (cultured cells-contractile microfilaments- glycoproteins-embryonic cells-sorting-out)
    • Sanger, J. W. & Holtzer, H. Cytochalasin B: effects on cell morphology, cell adhesion, and mucopolysaccharide synthesis (cultured cells-contractile microfilaments-glycoproteins-embryonic cells-sorting-out). Proc. Natl Acad. Sci. USA 69, 253-257 (1972).
    • (1972) Proc. Natl. Acad. Sci. USA , vol.69 , pp. 253-257
    • Sanger, J.W.1    Holtzer, H.2
  • 21
    • 0027454485 scopus 로고
    • Mapping of the α-actinin binding site within the β1 integrin cytoplasmic domain
    • Otey, C. A., Vasquez, G. B., Burridge, K. & Erickson, B. W. Mapping of the α-actinin binding site within the β1 integrin cytoplasmic domain. J. Biol. Chem. 268, 21193-21197 (1993).
    • (1993) J. Biol. Chem. , vol.268 , pp. 21193-21197
    • Otey, C.A.1    Vasquez, G.B.2    Burridge, K.3    Erickson, B.W.4
  • 22
    • 0027172919 scopus 로고
    • Mechanotransduction across the cell surface and through the cytoskeleton
    • Wang, N., Butler, J. P. & Ingber, D. E. Mechanotransduction across the cell surface and through the cytoskeleton. Science 260, 1124-1127 (1993).
    • (1993) Science , vol.260 , pp. 1124-1127
    • Wang, N.1    Butler, J.P.2    Ingber, D.E.3
  • 23
    • 0343576503 scopus 로고
    • Dual control of cell growth by somatomedins and platelet-derived growth factor
    • Stiles, C. D. et al. Dual control of cell growth by somatomedins and platelet-derived growth factor. Proc. Natl Acad Sci. USA 76, 1279-1283 (1979).
    • (1979) Proc. Natl. Acad Sci. USA , vol.76 , pp. 1279-1283
    • Stiles, C.D.1
  • 24
    • 0027176804 scopus 로고
    • Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown
    • McNamee, H. P., Ingber, D. E. & Schwartz, M. A. Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown. J. Cell Biol. 121, 673-678 (1993).
    • (1993) J. Cell Biol. , vol.121 , pp. 673-678
    • McNamee, H.P.1    Ingber, D.E.2    Schwartz, M.A.3
  • 25
    • 0025946283 scopus 로고
    • Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by clustering of β1 integrins
    • Kornberg, L. J., Earp, H. S., Turner, C. E., Prockop, C. & Juliano, R. L. Signal transduction by integrins: increased protein tyrosine phosphorylation caused by clustering of β1 integrins. Proc. Natl Acad Sci. USA 88, 8392-8396 (1991).
    • (1991) Proc. Natl. Acad Sci. USA , vol.88 , pp. 8392-8396
    • Kornberg, L.J.1    Earp, H.S.2    Turner, C.E.3    Prockop, C.4    Juliano, R.L.5
  • 26
    • 0027055575 scopus 로고
    • Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
    • Kornberg, L., Earp, H. S., Parsons, J. T., Schaller, M. & Juliano, R. L. Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J. Biol. Chem. 267, 23439-23442 (1992).
    • (1992) J. Biol. Chem. , vol.267 , pp. 23439-23442
    • Kornberg, L.1    Earp, H.S.2    Parsons, J.T.3    Schaller, M.4    Juliano, R.L.5
  • 27
    • 0028238346 scopus 로고
    • Disruption of integrin function and induction of tyrosine phosphorylation by the autonomously expressed β1 integrin cytoplasmic domain
    • Lukashev, M. E., Sheppard, D. & Pytela, R. Disruption of integrin function and induction of tyrosine phosphorylation by the autonomously expressed β1 integrin cytoplasmic domain. J. Biol. Chem. 269, 18311-18314 (1994).
    • (1994) J. Biol. Chem. , vol.269 , pp. 18311-18314
    • Lukashev, M.E.1    Sheppard, D.2    Pytela, R.3
  • 28
    • 0008584962 scopus 로고    scopus 로고
    • Mapping of the gene encoding the integrin-linked kinase, ILK, to human chromosome 11p15. 5-p15.4
    • Hannigan, G. E. et al. Mapping of the gene encoding the integrin-linked kinase, ILK, to human chromosome 11p15. 5-p15.4. Genomes 42, 177-179 (1997).
    • (1997) Genomes , vol.42 , pp. 177-179
    • Hannigan, G.E.1
  • 29
    • 0033020670 scopus 로고    scopus 로고
    • The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells
    • Tu, Y., Li, F., Goicoechea, S. & Wu, C. The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells. Mol. Cell. Biol. 19, 2425-2434 (1999). First identification of the interaction of ILK with PINCH, an evolutionary conserved protein required for various ILK functions.
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 2425-2434
    • Tu, Y.1    Li, F.2    Goicoechea, S.3    Wu, C.4
  • 30
    • 0035341207 scopus 로고    scopus 로고
    • Modulation of integrin signa transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1
    • Leung-Hagestejn, C., Mahendra, A., Naruszewicz, I. & Hannigan, G. E. Modulation of integrin signa transduction by ILKAP, a protein phosphatase 2C associating with the integrin-linked kinase, ILK1. EMBO J. 20, 2160-2170 (2001). Important finding identifying a negative regulator of ILK activity.
    • (2001) EMBO J. , vol.20 , pp. 2160-2170
    • Leung-Hagestejn, C.1    Mahendra, A.2    Naruszewicz, I.3    Hannigan, G.E.4
  • 31
    • 0035844879 scopus 로고    scopus 로고
    • A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction
    • Yamaji, S. et al. A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction. J. Cell Biol. 153, 1251-1264 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 1251-1264
    • Yamaji, S.1
  • 32
    • 0035972170 scopus 로고    scopus 로고
    • A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading
    • Tu, Y., Huang, Y., Zhang, Y., Hua, Y. & Wu, C. A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading, J. Cell Biol. 153, 585-598 (2001). References 31 and 32 describe the identification and interactions with ILK of β-parvin and α-parvin, respectively, and the roles of their interactions with ILK on cell spreading.
    • (2001) J. Cell Biol. , vol.153 , pp. 585-598
    • Tu, Y.1    Huang, Y.2    Zhang, Y.3    Hua, Y.4    Wu, C.5
  • 33
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks, S. K. & Hunter, T. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9, 576-596 (1995).
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 34
    • 0026345394 scopus 로고
    • Protein kinase catalytic domain sequence database: Identification of conserved features of primary structure and classification of family members
    • Hanks, S. K. & Quinn, A. M. Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members. Methods Enzymol. 200, 38-62 (1991).
    • (1991) Methods Enzymol. , vol.200 , pp. 38-62
    • Hanks, S.K.1    Quinn, A.M.2
  • 36
    • 0031974516 scopus 로고    scopus 로고
    • Peutz-Jeghers syndrome is caused by mutations in a novel serine threonine kinase
    • Jenne, D. E. et al. Peutz-Jeghers syndrome is caused by mutations in a novel serine threonine kinase. Nature Genet. 18, 38-43 (1998).
    • (1998) Nature Genet. , vol.18 , pp. 38-43
    • Jenne, D.E.1
  • 37
    • 0032471851 scopus 로고    scopus 로고
    • Loss of LKB1 kinase activity in Peutz-Jeghers syndrome, and evidence for allelic and locus heterogeneity
    • Mehenni, H. et al. Loss of LKB1 kinase activity in Peutz-Jeghers syndrome, and evidence for allelic and locus heterogeneity. Am. J. Hum. Genet. 63, 1641-1650 (1998).
    • (1998) Am. J. Hum. Genet. , vol.63 , pp. 1641-1650
    • Mehenni, H.1
  • 38
    • 18344405643 scopus 로고    scopus 로고
    • Functional analysis of LKB1/STK11 mutants and two aberrant isoforms found in Peutz-Jeghers Syndrome patients
    • Boudeau, J. et al. Functional analysis of LKB1/STK11 mutants and two aberrant isoforms found in Peutz-Jeghers Syndrome patients. Hum. Mutat. 21, 172 (2003).
    • (2003) Hum. Mutat. , vol.21 , pp. 172
    • Boudeau, J.1
  • 39
    • 0037076484 scopus 로고    scopus 로고
    • Integrin adhesion: When is a kinase a kinase?
    • Zervas, C. G. & Brown, N. H. Integrin adhesion: when is a kinase a kinase? Curr. Biol. 12, R350-R351 (2002).
    • (2002) Curr. Biol. , vol.12
    • Zervas, C.G.1    Brown, N.H.2
  • 40
    • 0034601436 scopus 로고    scopus 로고
    • The integrin-linked kinase (ILK) suppresses anoikis
    • Attwel, S., Roskelley, C. & Dedhar, S. The integrin-linked kinase (ILK) suppresses anoikis. Oncogene 19, 3811-3815 (2000).
    • (2000) Oncogene , vol.19 , pp. 3811-3815
    • Attwel, S.1    Roskelley, C.2    Dedhar, S.3
  • 41
    • 0030999580 scopus 로고    scopus 로고
    • Overexpression of the integrin-linked kinase promotes anchorage-independent cell cycle progression
    • Radeva, G. et al. Overexpression of the integrin-linked kinase promotes anchorage-independent cell cycle progression. J. Biol. Chem. 272, 13937-13944 (1997). This study showed that ILK can coordinate adhesion-dependent cell-cycle regulation.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13937-13944
    • Radeva, G.1
  • 43
    • 0344012484 scopus 로고    scopus 로고
    • Integration of cell attachment, cytoskeletal localization, and signaling by integrin-linked kinase (ILK), CH-ILKBP, and the tumor suppressor PTEN
    • Attwel, S., Mills, J., Troussard, A., Wu, C. & Dedhar, S. Integration of cell attachment, cytoskeletal localization, and signaling by integrin-linked kinase (ILK), CH-ILKBP, and the tumor suppressor PTEN. Mol. Biol. Cell 14, 4813-4825 (2003). This work shows the integrated function of ILK as a kinase and an adaptor in focal adhesions.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4813-4825
    • Attwel, S.1    Mills, J.2    Troussard, A.3    Wu, C.4    Dedhar, S.5
  • 44
    • 0030913673 scopus 로고    scopus 로고
    • Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway
    • Khwaja, A., Rodriguez-Viciana, P., Wennstrom, S., Warne, P.H. & Downward, J. Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway. EMBO J. 16, 2783-2793 (1997).
    • (1997) EMBO J. , vol.16 , pp. 2783-2793
    • Khwaja, A.1    Rodriguez-Viciana, P.2    Wennstrom, S.3    Warne, P.H.4    Downward, J.5
  • 45
    • 0032530482 scopus 로고    scopus 로고
    • Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase
    • Delcommenne, M. et al. Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc. Natl Acad. Sci. USA 95, 11211-11216 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11211-11216
    • Delcommenne, M.1
  • 46
    • 0033599029 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates phosphorylation of serine 473 of protein kinase B by an indirect mechanism
    • Lynch, D. K., Ellis, C. A., Edwards, P. A. & Hiles, I. D. Integrin-linked kinase regulates phosphorylation of serine 473 of protein kinase B by an indirect mechanism. Oncogene 18, 8024-8032 (1999). References 45 and 46 showed that ILK activity is regulated in a PI3K-dependent manner, and that ILK regulates AKT Ser473 phosphorylation in a PI3K-dependent manner.
    • (1999) Oncogene , vol.18 , pp. 8024-8032
    • Lynch, D.K.1    Ellis, C.A.2    Edwards, P.A.3    Hiles, I.D.4
  • 47
    • 0034724443 scopus 로고    scopus 로고
    • Inhibition of integrin-linked kinase (ILK) suppresses activation of protein kinase B/Akt and induces cell cycle arrest and apoptosis of PTEN-mutant prostate cancer cells
    • Persad, S. et al. Inhibition of integrin-linked kinase (ILK) suppresses activation of protein kinase B/Akt and induces cell cycle arrest and apoptosis of PTEN-mutant prostate cancer cells. Proc. Natl Acad. Sci. USA 97, 3207-3212 (2000). References 47 and 56 show that PTEN negatively regulates ILK activity and that loss of PTEN results in constitutively activated ILK. Inhibition of ILK in PTEN-negative cells inhibits tumour-cell growth and inhibits AKT activation.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 3207-3212
    • Persad, S.1
  • 48
    • 0037457047 scopus 로고    scopus 로고
    • α integrins regulate cell proliferation through integrin-linked kinase (ILK) in ovarian cancer cells
    • Cruet-Hennequart, S. et al. α integrins regulate cell proliferation through integrin-linked kinase (ILK) in ovarian cancer cells. Oncogene 22, 1688-1702 (2003).
    • (2003) Oncogene , vol.22 , pp. 1688-1702
    • Cruet-Hennequart, S.1
  • 49
    • 0032577699 scopus 로고    scopus 로고
    • The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate
    • Maehama, T. & Dixon, J. E. The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. J. Biol. Chem. 273, 13375-13378 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 13375-13378
    • Maehama, T.1    Dixon, J.E.2
  • 50
    • 0036181869 scopus 로고    scopus 로고
    • PTEN: The down side of PI 3-kinase signaling
    • Leslie, N. R. & Downes, C. P. PTEN: The down side of PI 3-kinase signaling. Cell Signal. 14, 285-295 (2002).
    • (2002) Cell Signal. , vol.14 , pp. 285-295
    • Leslie, N.R.1    Downes, C.P.2
  • 51
    • 0030936323 scopus 로고    scopus 로고
    • PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer
    • Li, J. et al. PTEN, a putative protein tyrosine phosphatase gene mutated in human brain, breast, and prostate cancer. Science 275, 1943-1947 (1997).
    • (1997) Science , vol.275 , pp. 1943-1947
    • Li, J.1
  • 52
    • 15444349266 scopus 로고    scopus 로고
    • Frequent inactivation of PTEN/MMAC1 in primary prostate cancer
    • Cairns, P. et al. Frequent inactivation of PTEN/MMAC1 in primary prostate cancer. Cancer Res. 57, 4997-5000 (1997).
    • (1997) Cancer Res. , vol.57 , pp. 4997-5000
    • Cairns, P.1
  • 53
    • 0032574718 scopus 로고    scopus 로고
    • Inactivation of the tumor suppressor PTEN/MMAC1 in advanced human prostate cancer through loss of expression
    • Whang, Y. E. et al. Inactivation of the tumor suppressor PTEN/MMAC1 in advanced human prostate cancer through loss of expression. Proc. Natl Acad. Sci. USA 95, 5246-5250 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5246-5250
    • Whang, Y.E.1
  • 54
    • 0032506011 scopus 로고    scopus 로고
    • The lipid phosphatase activity of PTEN is critical for its tumor supressor function
    • Myers, M. P. et al. The lipid phosphatase activity of PTEN is critical for its tumor supressor function. Proc. Natl Acad. Sci. USA 95, 13513-13518 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 13513-13518
    • Myers, M.P.1
  • 55
    • 0032475861 scopus 로고    scopus 로고
    • Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN
    • Stambolic, V. et al. Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN. Cell 95, 29-39 (1998).
    • (1998) Cell , vol.95 , pp. 29-39
    • Stambolic, V.1
  • 56
    • 0034642547 scopus 로고    scopus 로고
    • The MMAC1 tumor suppressor phosphatase inhibits phospholipase C and integrin-linked kinase activity
    • Morimoto, A. M. et al. The MMAC1 tumor suppressor phosphatase inhibits phospholipase C and integrin-linked kinase activity. Oncogene 19, 200-209 (2000).
    • (2000) Oncogene , vol.19 , pp. 200-209
    • Morimoto, A.M.1
  • 57
    • 0035844886 scopus 로고    scopus 로고
    • Tumor suppressor PTEN inhibits nuclear accumulation of β-catenin and T cell/lymphoid enhancer factor 1-mediated transcriptional activation
    • Persad, S., Troussard, A. A., McPhee, T. R., Mulholland, D. J. & Dedhar, S. Tumor suppressor PTEN inhibits nuclear accumulation of β-catenin and T cell/lymphoid enhancer factor 1-mediated transcriptional activation. J. Cell Biol. 153, 1161-1174 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 1161-1174
    • Persad, S.1    Troussard, A.A.2    McPhee, T.R.3    Mulholland, D.J.4    Dedhar, S.5
  • 58
    • 11144227278 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) regulation of the cell viability in PTEN mutant glioblastoma and in vitro inhibition by the specific COX-2 inhibitor NS-398
    • Obara, S. et al. Integrin-linked kinase (ILK) regulation of the cell viability in PTEN mutant glioblastoma and in vitro inhibition by the specific COX-2 inhibitor NS-398. Cancer Lett. 208, 115-122 (2004).
    • (2004) Cancer Lett. , vol.208 , pp. 115-122
    • Obara, S.1
  • 59
    • 7144261716 scopus 로고    scopus 로고
    • DOC-2, a candidate tumor suppressor gene in human epithelial ovarian cancer
    • Mok, S. C. et al. DOC-2, a candidate tumor suppressor gene in human epithelial ovarian cancer. Oncogene 16, 2381-2387 (1998).
    • (1998) Oncogene , vol.16 , pp. 2381-2387
    • Mok, S.C.1
  • 60
    • 0036734416 scopus 로고    scopus 로고
    • Down-regulation of DOC-2 in colorectal cancer points to is role as a tumor suppressor in this malignancy
    • Kleeff, J. et al. Down-regulation of DOC-2 in colorectal cancer points to is role as a tumor suppressor in this malignancy. Dis. Colon Rectum 45, 1242-1248 (2002).
    • (2002) Dis. Colon Rectum , vol.45 , pp. 1242-1248
    • Kleeff, J.1
  • 61
    • 3442894137 scopus 로고    scopus 로고
    • Expression profiling reveals novel pathways in the transformation of melanocytes to melanomas
    • Hoek, K. et al. Expression profiling reveals novel pathways in the transformation of melanocytes to melanomas. Cancer Res. 64, 5270-5282 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 5270-5282
    • Hoek, K.1
  • 62
    • 0141891463 scopus 로고    scopus 로고
    • Increased expression of integrin-linked kinase is correlated with melanoma progression and poor patient survival
    • Dai, D. L. et al. Increased expression of integrin-linked kinase is correlated with melanoma progression and poor patient survival. Clin. Cancer Res. 9, 4409-4414 (2003).
    • (2003) Clin. Cancer Res. , vol.9 , pp. 4409-4414
    • Dai, D.L.1
  • 63
    • 0037072821 scopus 로고    scopus 로고
    • Induction of apoptosis by stomach cancer-associated protein-tyrosine phosphatase-1
    • Takada, T. et al. Induction of apoptosis by stomach cancer-associated protein-tyrosine phosphatase-1. J. Biol. Chem. 277, 34359-34366 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 34359-34366
    • Takada, T.1
  • 64
    • 0037338529 scopus 로고    scopus 로고
    • Phosphorylation of myosin II regulatory light chain is necessary for migration of HeLa cells but not for localization of myosin II at the leading edge
    • Fumoto, K., Uchimura, T., Iwasaki, T., Ueda, K. & Hosoya, H. Phosphorylation of myosin II regulatory light chain is necessary for migration of HeLa cells but not for localization of myosin II at the leading edge. Biochem. J. 370, 551-556 (2003).
    • (2003) Biochem. J. , vol.370 , pp. 551-556
    • Fumoto, K.1    Uchimura, T.2    Iwasaki, T.3    Ueda, K.4    Hosoya, H.5
  • 65
    • 0037004888 scopus 로고    scopus 로고
    • Spatial localization of mono-and diphosphorylated myosin II regulatory light chain at the leading edge of motile HeLa cells
    • Uchimura, T., Fumoto, K., Yamamoto, Y., Ueda, K. & Hosoya, H. Spatial localization of mono-and diphosphorylated myosin II regulatory light chain at the leading edge of motile HeLa cells. Cell Struct. Funct. 27, 479-486 (2002).
    • (2002) Cell Struct. Funct. , vol.27 , pp. 479-486
    • Uchimura, T.1    Fumoto, K.2    Yamamoto, Y.3    Ueda, K.4    Hosoya, H.5
  • 66
    • 0031917782 scopus 로고    scopus 로고
    • Specific localization of serine 19 phosphorated myosin II during cell locomotion and mitosis of cultured cells
    • Matsumura, F., Ono, S., Yamakita, Y., Totsukawa, G. & Yamashino, S. Specific localization of serine 19 phosphorated myosin II during cell locomotion and mitosis of cultured cells. J. Cell Biol. 140, 119-129 (1998).
    • (1998) J. Cell Biol. , vol.140 , pp. 119-129
    • Matsumura, F.1    Ono, S.2    Yamakita, Y.3    Totsukawa, G.4    Yamashino, S.5
  • 67
    • 0037109063 scopus 로고    scopus 로고
    • Phosphorylation of the myosin phosphatase inhibitors, CPI-17 and PHI-1, by integrin-linked kinase
    • Deng, J. T., Sutherland, C., Brautigan, D. L., Eto, M. & Walsh, M. P. Phosphorylation of the myosin phosphatase inhibitors, CPI-17 and PHI-1, by integrin-linked kinase. Biochem. J. 367, 517-524 (2002).
    • (2002) Biochem. J. , vol.367 , pp. 517-524
    • Deng, J.T.1    Sutherland, C.2    Brautigan, D.L.3    Eto, M.4    Walsh, M.P.5
  • 68
    • 0037532608 scopus 로고    scopus 로고
    • Phosphorylation of protein phosphatase type-1 inhibitory proteins by integrin-linked kinase and cyclic nucleotide-dependent protein kinases
    • Erdodi, F. et al. Phosphorylation of protein phosphatase type-1 inhibitory proteins by integrin-linked kinase and cyclic nucleotide-dependent protein kinases. Biochem. Biophys. Res. Commun. 306, 382-387 (2003).
    • (2003) Biochem. Biophys. Res. Commun. , vol.306 , pp. 382-387
    • Erdodi, F.1
  • 69
    • 0037016703 scopus 로고    scopus 로고
    • A critical role of the PINCH-integrin-tinked kinase interaction in the regulation of cell shape change and migration
    • Zhang, Y., Guo, L., Chen, K. & Wu, C. A critical role of the PINCH-integrin-tinked kinase interaction in the regulation of cell shape change and migration. J. Biol. Chem. 277, 318-326 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 318-326
    • Zhang, Y.1    Guo, L.2    Chen, K.3    Wu, C.4
  • 70
    • 0035895898 scopus 로고    scopus 로고
    • Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain
    • Velyvis, A., Yang, Y., Wu, C. & Qin, J. Solution structure of the focal adhesion adaptor PINCH LIM1 domain and characterization of its interaction with the integrin-linked kinase ankyrin repeat domain. J. Biol. Chem. 276, 4932-4939 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 4932-4939
    • Velyvis, A.1    Yang, Y.2    Wu, C.3    Qin, J.4
  • 71
    • 0033378656 scopus 로고    scopus 로고
    • Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats
    • Li, F., Zhang, Y. & Wu, C. Integrin-linked kinase is localized to cell-matrix focal adhesions but not cell-cell adhesion sites and the focal adhesion localization of integrin-linked kinase is regulated by the PINCH-binding ANK repeats. J. Cell Sci. 112, 4589-4599 (1999).
    • (1999) J. Cell Sci. , vol.112 , pp. 4589-4599
    • Li, F.1    Zhang, Y.2    Wu, C.3
  • 72
    • 0345803932 scopus 로고    scopus 로고
    • PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival
    • Fukuda, T., Chen, K., Shi, X. & Wu, C. PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival. J. Biol. Chem. 278, 51324-51333 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 51324-51333
    • Fukuda, T.1    Chen, K.2    Shi, X.3    Wu, C.4
  • 73
    • 0037064063 scopus 로고    scopus 로고
    • Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration
    • Zhang, Y., Chen, K., Guo, L. & Wu, C. Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration. J. Biol. Chem. 277, 38328-38338 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 38328-38338
    • Zhang, Y.1    Chen, K.2    Guo, L.3    Wu, C.4
  • 74
    • 0037377167 scopus 로고    scopus 로고
    • PINCH2 is a new five LIM domain protein, homologous to PINCHand localized to focal adhesions
    • Braun, A. et al. PINCH2 is a new five LIM domain protein, homologous to PINCHand localized to focal adhesions. Exp. Cell Res. 284, 239-250 (2003).
    • (2003) Exp. Cell Res. , vol.284 , pp. 239-250
    • Braun, A.1
  • 75
    • 0035126590 scopus 로고    scopus 로고
    • Parvin, a 42 kDa focal adhesion protein, related to the α-actinin superfamily
    • Olski, T. M., Noegel, A. A. & Korenbaum, E. Parvin, a 42 kDa focal adhesion protein, related to the α-actinin superfamily. J. Cell Sci. 114, 525-538 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 525-538
    • Olski, T.M.1    Noegel, A.A.2    Korenbaum, E.3
  • 76
    • 0037059789 scopus 로고    scopus 로고
    • Molecular dissection of actopaxin-integrin-linked kinase-paxillin interactions and their role in subcellular localization
    • Nikolopoulos, S. N. & Turner, C. E. Molecular dissection of actopaxin-integrin-linked kinase-paxillin interactions and their role in subcellular localization. J. Biol. Chem. 277, 1568-1575 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 1568-1575
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 77
    • 10644244400 scopus 로고    scopus 로고
    • β-parvin inhibits integrin linked kinase signaling and is down-regulated in breast cancer
    • Mongroo, P. et al. β-parvin inhibits integrin linked kinase signaling and is down-regulated in breast cancer. Oncogene 23, 8959-8970 (2004).
    • (2004) Oncogene , vol.23 , pp. 8959-8970
    • Mongroo, P.1
  • 78
    • 0037417416 scopus 로고    scopus 로고
    • CH-ILKBP regulates cell survival by facilitating the membrane translocation of protein kinase B/Akt
    • Fukuda, T., Guo, L., Shi, X. & Wu, C. CH-ILKBP regulates cell survival by facilitating the membrane translocation of protein kinase B/Akt. J. Cell Biol. 160, 1001-1008 (2003).
    • (2003) J. Cell Biol. , vol.160 , pp. 1001-1008
    • Fukuda, T.1    Guo, L.2    Shi, X.3    Wu, C.4
  • 79
    • 4744340477 scopus 로고    scopus 로고
    • Distinct roles of two structurally closely related focal adhesion proteins, α-parvins and β-parvins, in regulation of cell morphology and survival
    • Zhang, Y., Chen, K., Tu, Y. & Wu, C. Distinct roles of two structurally closely related focal adhesion proteins, α-parvins and β-parvins, in regulation of cell morphology and survival. J. Biol. Chem. 279, 41695-41705 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 41695-41705
    • Zhang, Y.1    Chen, K.2    Tu, Y.3    Wu, C.4
  • 80
    • 0037115611 scopus 로고    scopus 로고
    • Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites
    • Zhang, Y. et al. Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites. J. Cell Sci. 115, 4777-4786 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 4777-4786
    • Zhang, Y.1
  • 81
    • 0036673109 scopus 로고    scopus 로고
    • Regulation of fibronectin matrix deposition and cell proliferation by the PINCH-ILK-CH-ILKBP complex
    • Guo, L. & Wu, C. Regulation of fibronectin matrix deposition and cell proliferation by the PINCH-ILK-CH-ILKBP complex. FASEB J. 16, 1298-1300 (2002).
    • (2002) FASEB J. , vol.16 , pp. 1298-1300
    • Guo, L.1    Wu, C.2
  • 82
    • 0035968234 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions
    • Nikolopoulos, S. N. & Turner, C. E. Integrin-linked kinase (ILK) binding to paxillin LD1 motif regulates ILK localization to focal adhesions. J. Biol. Chem. 276, 23499-23505 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 23499-23505
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 83
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frish, S. M. & Francis, H. Disruption of epithelial cell-matrix interactions induces apoptosis. J. Cell Biol. 124, 619-626 (1984).
    • (1984) J. Cell Biol. , vol.124 , pp. 619-626
    • Frish, S.M.1    Francis, H.2
  • 84
    • 0027752979 scopus 로고
    • A link between cyclin A expression and adhesion-dependent cell cycle progression
    • Guadagno, T. M., Ohtsubo, M., Roberts, J. M. & Assoian, R. K. A link between cyclin A expression and adhesion-dependent cell cycle progression. Science 262, 1572-1575 (1993).
    • (1993) Science , vol.262 , pp. 1572-1575
    • Guadagno, T.M.1    Ohtsubo, M.2    Roberts, J.M.3    Assoian, R.K.4
  • 85
    • 0029876639 scopus 로고    scopus 로고
    • Adhesion-dependent cell cycle progression linked to the expression of cyclin D1, activation of cyclin E-cdk2, and phosphorylation of the retinoblastoma protein
    • Zhu, X., Ohtsubo, M., Bohmer, R. M., Roberts, J. M. & Assoian, R. K. Adhesion-dependent cell cycle progression linked to the expression of cyclin D1, activation of cyclin E-cdk2, and phosphorylation of the retinoblastoma protein. J.Cell Biol. 133, 391-403 (1996).
    • (1996) J.Cell Biol. , vol.133 , pp. 391-403
    • Zhu, X.1    Ohtsubo, M.2    Bohmer, R.M.3    Roberts, J.M.4    Assoian, R.K.5
  • 86
    • 0034692686 scopus 로고    scopus 로고
    • The integrin-linked kinase regulates the cyclin D1 gene through glycogen synthase kinase 3β and cAMP-responsive element-binding protein-dependent pathways
    • D'Amico, M. et al. The integrin-linked kinase regulates the cyclin D1 gene through glycogen synthase kinase 3β and cAMP-responsive element-binding protein-dependent pathways. J. Biol. Chem. 275, 32649-32657 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 32649-32657
    • D'Amico, M.1
  • 87
    • 0030786162 scopus 로고    scopus 로고
    • Identification and characterization of a mouse protein kinase that is highly homologous to human integrin-linked kinase
    • Li, F., Liu, J., Mayne, R. & Wu, C. Identification and characterization of a mouse protein kinase that is highly homologous to human integrin-linked kinase. Biochim. Biophys. Acta 1358, 215-220 (1997).
    • (1997) Biochim. Biophys. Acta , vol.1358 , pp. 215-220
    • Li, F.1    Liu, J.2    Mayne, R.3    Wu, C.4
  • 88
    • 0038148536 scopus 로고    scopus 로고
    • Reduced chondrocyte proliferation and chondrodysplasia in mice lacking the integrin-linked kinase in chondrocytes
    • Terpstra, L. et al. Reduced chondrocyte proliferation and chondrodysplasia in mice lacking the integrin-linked kinase in chondrocytes. J. Cell Biol. 162, 139-148 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 139-148
    • Terpstra, L.1
  • 89
    • 0038323946 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates chondrocyte shape and proliferation
    • Grashoff, C., Aszodi, A., Sakai, T., Hunziker, E. B. & Fassler, R. Integrin-linked kinase regulates chondrocyte shape and proliferation. EMBO Rep. 4, 432-138 (2003).
    • (2003) EMBO Rep. , vol.4 , pp. 432-1138
    • Grashoff, C.1    Aszodi, A.2    Sakai, T.3    Hunziker, E.B.4    Fassler, R.5
  • 90
    • 0032746701 scopus 로고    scopus 로고
    • Cell-extracellular matrix interactions stimulate the AP-1 transcription factor in an integrin-linked kinase- and glycogen synthase kinase 3-dependent manner
    • Troussard, A. A., Tan, C., Yoganathan, T. N. & Dedhar, S. Cell-extracellular matrix interactions stimulate the AP-1 transcription factor in an integrin-linked kinase- and glycogen synthase kinase 3-dependent manner. Mol. Cell. Biol. 19, 7420-7427 (1999).
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 7420-7427
    • Troussard, A.A.1    Tan, C.2    Yoganathan, T.N.3    Dedhar, S.4
  • 91
  • 92
    • 6344280968 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) regulates the nuclear entry of the c-JUN coactivator αNAC and its coactivation potency
    • Quelo, I., Gauthier, C., Hannigan, G. E., Dedhar, S. & St-Arnaud, R. Integrin-linked kinase (ILK) regulates the nuclear entry of the c-JUN coactivator αNAC and its coactivation potency. J. Biol. Chem. 279, 43893-43899 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 43893-43899
    • Quelo, I.1    Gauthier, C.2    Hannigan, G.E.3    Dedhar, S.4    St-Arnaud, R.5
  • 93
    • 0037666792 scopus 로고    scopus 로고
    • Conditional knock-out of integrin-linked kinase demonstrates an essential role in protein kinase B/Akt activation
    • Troussard, A. A. et al. Conditional knock-out of integrin-linked kinase demonstrates an essential role in protein kinase B/Akt activation. J. Biol. Chem. 278, 22374-22378 (2003). Genetic approach showing that ILK is essential for promoting phosphorylation of AKT on Ser473.
    • (2003) J. Biol. Chem. , vol.278 , pp. 22374-22378
    • Troussard, A.A.1
  • 94
    • 0037315101 scopus 로고    scopus 로고
    • Essential role for integrin linked kinase in Akt-mediated integrin survival signaling in hippocampal neurons
    • Gary, D. S., Milhavet, O., Camandola, S. & Mattson, M. P. Essential role for integrin linked kinase in Akt-mediated integrin survival signaling in hippocampal neurons. J. Neurochem. 84, 878-890 (2003).
    • (2003) J. Neurochem. , vol.84 , pp. 878-890
    • Gary, D.S.1    Milhavet, O.2    Camandola, S.3    Mattson, M.P.4
  • 95
    • 0036185848 scopus 로고    scopus 로고
    • The protein kinase B/Akt signalling pathway in human malignancy
    • Nicholson, K. M. & Anderson, N. G. The protein kinase B/Akt signalling pathway in human malignancy. Cell Signal. 14, 381-395 (2002).
    • (2002) Cell Signal. , vol.14 , pp. 381-395
    • Nicholson, K.M.1    Anderson, N.G.2
  • 96
    • 0036479113 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates inducible nitric oxide synthase and cyclooxygenase-2 expression in an NF-κS-dependent manner
    • Tan, C., Mui, A. & Dedhar, S. Integrin-linked kinase regulates inducible nitric oxide synthase and cyclooxygenase-2 expression in an NF-κS-dependent manner. J. Biol. Chem. 277, 3109-3116 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 3109-3116
    • Tan, C.1    Mui, A.2    Dedhar, S.3
  • 97
    • 2342641439 scopus 로고    scopus 로고
    • Upregulation of IKKα/IKKβ by integrin-linked kinase is required for HER2/neu-induced NF-κB antiapoptotic pathway
    • Makino, K., Day, C. P., Wang, S. C., Li, Y. M. & Hung, M. C. Upregulation of IKKα/IKKβ by integrin-linked kinase is required for HER2/neu-induced NF-κB antiapoptotic pathway. Oncogene 23, 3883-3887 (2004).
    • (2004) Oncogene , vol.23 , pp. 3883-3887
    • Makino, K.1    Day, C.P.2    Wang, S.C.3    Li, Y.M.4    Hung, M.C.5
  • 98
    • 0035977036 scopus 로고    scopus 로고
    • Inhibition of integrin-linked kinase/protein kinase B/Akt signaling: Mechanism for ganglioside-induced apoptosis
    • Wang, X. Q., Sun, P. & Paller, A. S. Inhibition of integrin-linked kinase/protein kinase B/Akt signaling: mechanism for ganglioside-induced apoptosis. J. Biol. Chem. 276, 44504-44511 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 44504-44511
    • Wang, X.Q.1    Sun, P.2    Paller, A.S.3
  • 99
    • 0037162291 scopus 로고    scopus 로고
    • Identification of a plasma membrane Raft-associated PKB Ser473 kinase activity that is distinct from ILK and PDK1
    • Hill, M. M., Feng, J. & Hemmings, B. A. Identification of a plasma membrane Raft-associated PKB Ser473 kinase activity that is distinct from ILK and PDK1. Curr. Biol. 12, 1251-1255 (2002).
    • (2002) Curr. Biol. , vol.12 , pp. 1251-1255
    • Hill, M.M.1    Feng, J.2    Hemmings, B.A.3
  • 100
    • 4644359805 scopus 로고    scopus 로고
    • Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase
    • Feng, J., Park, J., Cron, P., Hess, D. & Hemmings, B. A. Identification of a PKB/Akt hydrophobic motif Ser-473 kinase as DNA-dependent protein kinase. J. Biol. Chem. 279, 41189-41196 (2004).
    • (2004) J. Biol. Chem. , vol.279 , pp. 41189-41196
    • Feng, J.1    Park, J.2    Cron, P.3    Hess, D.4    Hemmings, B.A.5
  • 101
    • 0242266910 scopus 로고    scopus 로고
    • Integrin-linked kinase is required for laminin-2-induced oligodendrocyte cell spreading and CNS myelination
    • Chun, S. J., Rasband, M. N., Sidman, R. L., Habib, A. A. & Vartanian, T. Integrin-linked kinase is required for laminin-2-induced oligodendrocyte cell spreading and CNS myelination. J. Cell Biol. 163, 397-408 (2003).
    • (2003) J. Cell Biol. , vol.163 , pp. 397-408
    • Chun, S.J.1    Rasband, M.N.2    Sidman, R.L.3    Habib, A.A.4    Vartanian, T.5
  • 102
    • 0032516094 scopus 로고    scopus 로고
    • Cell adhesion and the integrin-linked kinase regulate the LEF-1 and β-catenin signaling pathways
    • Novak, A. et al. Cell adhesion and the integrin-linked kinase regulate the LEF-1 and β-catenin signaling pathways. Proc. Natl Acad. Sci. USA 95, 4374-4379 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4374-4379
    • Novak, A.1
  • 103
    • 0031962084 scopus 로고    scopus 로고
    • Integrin-linked protein kinase regulates fibronectin matrix assembly, E-cadherin expression, and tumorigenicity
    • Wu, C. et al. Integrin-linked protein kinase regulates fibronectin matrix assembly, E-cadherin expression, and tumorigenicity. J. Biol. Chem. 273, 528-536 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 528-536
    • Wu, C.1
  • 104
    • 0141720342 scopus 로고    scopus 로고
    • Role for integrin-linked kinase in mediating tubular epithelial to mesenchyma transition and renal interstitial fibrogenesis
    • Li, Y., Yang, J., Dai, C., Wu, C. & Liu, Y. Role for integrin-linked kinase in mediating tubular epithelial to mesenchyma transition and renal interstitial fibrogenesis. J. Clin. Invest. 112, 503-516 (2003).
    • (2003) J. Clin. Invest. , vol.112 , pp. 503-516
    • Li, Y.1    Yang, J.2    Dai, C.3    Wu, C.4    Liu, Y.5
  • 105
    • 0035067120 scopus 로고    scopus 로고
    • Overexpression of the integrin-linked kinase mesenchymally transforms mammary epithelial cells
    • Somasiri, A., Howarth, A., Goswami, D., Dedhar, S. & Roskelley, C. D. Overexpression of the integrin-linked kinase mesenchymally transforms mammary epithelial cells. J. Cell Sci. 114, 1125-1136 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 1125-1136
    • Somasiri, A.1    Howarth, A.2    Goswami, D.3    Dedhar, S.4    Roskelley, C.D.5
  • 106
    • 0035950544 scopus 로고    scopus 로고
    • Mammary epithelial-specific expression of the integrin-linked kinase (ILK) results in the induction of mammary gland hyperplasias and tumors in transgenic mice
    • White, D. E., Cardiff, R. D., Dedhar, S. & Muller, W. J. Mammary epithelial-specific expression of the integrin-linked kinase (ILK) results in the induction of mammary gland hyperplasias and tumors in transgenic mice. Oncogene 20, 7064-7072 (2001). This study provided in vivo demonstration that increased expression of ILK in breast epithelial cells promotes hyperplasia and tumour formation.
    • (2001) Oncogene , vol.20 , pp. 7064-7072
    • White, D.E.1    Cardiff, R.D.2    Dedhar, S.3    Muller, W.J.4
  • 107
    • 6044231839 scopus 로고    scopus 로고
    • Regulation of Snail transcription during epithelial to mesenchymal transition of tumor cells
    • Barbera, M. J. et al. Regulation of Snail transcription during epithelial to mesenchymal transition of tumor cells. Oncogene 23, 7345-7354 (2004).
    • (2004) Oncogene , vol.23 , pp. 7345-7354
    • Barbera, M.J.1
  • 108
    • 1642307942 scopus 로고    scopus 로고
    • Integrin-linked kinase function is required for transforming growth factor β-mediated epithelial to mesenchymal transition
    • Lee, Y. I., Kwon, Y. J. & Joo, C. K. Integrin-linked kinase function is required for transforming growth factor β-mediated epithelial to mesenchymal transition. Biochem. Biophys. Res. Commun. 316, 997-1001 (2004).
    • (2004) Biochem. Biophys. Res. Commun. , vol.316 , pp. 997-1001
    • Lee, Y.I.1    Kwon, Y.J.2    Joo, C.K.3
  • 109
    • 0036086409 scopus 로고    scopus 로고
    • Blockade of TGF-β inhibits mammary tumor cell viability, migration, and metastases
    • Muraoka, R. S. et al. Blockade of TGF-β inhibits mammary tumor cell viability, migration, and metastases. J. Clin. Invest. 109, 1551-1559 (2002).
    • (2002) J. Clin. Invest. , vol.109 , pp. 1551-1559
    • Muraoka, R.S.1
  • 110
    • 0034676338 scopus 로고    scopus 로고
    • The integrin linked kinase (ILK) induces an invasive phenotype via AP-1 transcription factor-dependent upregulation of matrix metalloproteinase 9 (MMP-9)
    • Troussard, A. A. et al. The integrin linked kinase (ILK) induces an invasive phenotype via AP-1 transcription factor-dependent upregulation of matrix metalloproteinase 9 (MMP-9). Oncogene 19, 5444-5452 (2000).
    • (2000) Oncogene , vol.19 , pp. 5444-5452
    • Troussard, A.A.1
  • 111
    • 0037439424 scopus 로고    scopus 로고
    • Interaction of αPIX (ARHGEF6) with β-parvin (PARVB) suggests an involvement of αPIX in integrin-mediated signaling
    • Rosenberger, G., Jantke, I., Gal, A. & Kutsche, K. Interaction of αPIX (ARHGEF6) with β-parvin (PARVB) suggests an involvement of αPIX in integrin-mediated signaling. Hum. Mol. Genet. 12, 155-167 (2003).
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 155-167
    • Rosenberger, G.1    Jantke, I.2    Gal, A.3    Kutsche, K.4
  • 112
    • 0037103743 scopus 로고    scopus 로고
    • Phosphorylation of the myosin phosphatase target subunit by integrin-linked kinase
    • Muranyi, A. et al. Phosphorylation of the myosin phosphatase target subunit by integrin-linked kinase. Biochem. J. 366, 211-216 (2002).
    • (2002) Biochem. J. , vol.366 , pp. 211-216
    • Muranyi, A.1
  • 113
    • 12144286634 scopus 로고    scopus 로고
    • Cyr61 is overexpressed in gliomas and involved in integrin-linked kinase-mediated Akt and β-catenin-TCF/Lef signaling pathways
    • Xie, D. et al. Cyr61 is overexpressed in gliomas and involved in integrin-linked kinase-mediated Akt and β-catenin-TCF/Lef signaling pathways. Cancer Res. 64, 1987-1996 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 1987-1996
    • Xie, D.1
  • 114
    • 0034782943 scopus 로고    scopus 로고
    • Integrin-linked kinase expression increases with prostate tumor grade
    • Graff, J. R. et al. Integrin-linked kinase expression increases with prostate tumor grade. Clin. Cancer Res. 7, 1987-1991 (2001).
    • (2001) Clin. Cancer Res. , vol.7 , pp. 1987-1991
    • Graff, J.R.1
  • 116
    • 0038604840 scopus 로고    scopus 로고
    • Characterisation of integrin-linked kinase signailing in sporadic human colon cancer
    • Marotta, A., Parhar, K., Owen, D., Dedhar, S. & Salh, B. Characterisation of integrin-linked kinase signailing in sporadic human colon cancer. Br. J. Cancer 88, 1755-1762 (2003).
    • (2003) Br. J. Cancer , vol.88 , pp. 1755-1762
    • Marotta, A.1    Parhar, K.2    Owen, D.3    Dedhar, S.4    Salh, B.5
  • 117
    • 0035959870 scopus 로고    scopus 로고
    • Dysregulation of integrin-linked kinase (ILK) signaling in colonic polyposis
    • Marotta, A. et al. Dysregulation of integrin-linked kinase (ILK) signaling in colonic polyposis. Oncogene 20, 6250-6257 (2001).
    • (2001) Oncogene , vol.20 , pp. 6250-6257
    • Marotta, A.1
  • 118
    • 0037295608 scopus 로고    scopus 로고
    • Expression of integrin-linked kinase is closely correlated with invasion and metastasis of gastric carcinoma
    • Ito, R. et al. Expression of integrin-linked kinase is closely correlated with invasion and metastasis of gastric carcinoma. Virchows Arch. 442, 118-123 (2003).
    • (2003) Virchows Arch. , vol.442 , pp. 118-123
    • Ito, R.1
  • 119
    • 0141995796 scopus 로고    scopus 로고
    • Integrin-linked kinase expression increases with ovarian tumour grade and is sustained by peritonea tumour fluid
    • Ahmed, N. et al. Integrin-linked kinase expression increases with ovarian tumour grade and is sustained by peritonea tumour fluid. J. Pathol. 201, 229-237 (2003).
    • (2003) J. Pathol. , vol.201 , pp. 229-237
    • Ahmed, N.1
  • 120
    • 1842531077 scopus 로고    scopus 로고
    • Cell-free 59 kDa immunoreactive integrin-linked kinase: A novel marker for ovarian carcinoma
    • Ahmed, N., Oliva, K., Rice, G. E. &, Quinn, M. A. Cell-free 59 kDa immunoreactive integrin-linked kinase: a novel marker for ovarian carcinoma. Clin. Cancer Res. 10, 2415-2420 (2004).
    • (2004) Clin. Cancer Res. , vol.10 , pp. 2415-2420
    • Ahmed, N.1    Oliva, K.2    Rice, G.E.3    Quinn, M.A.4
  • 121
    • 0031595969 scopus 로고    scopus 로고
    • ILK (β1-integrin-linked protein kinase): A novel immunohistochemical marker for Ewing's sarcoma and primitive neuroectodermal tumour
    • Chung, D. H. et al. ILK (β1-integrin-linked protein kinase): a novel immunohistochemical marker for Ewing's sarcoma and primitive neuroectodermal tumour. Virchows Arch. 433, 113-117 (1998).
    • (1998) Virchows Arch. , vol.433 , pp. 113-117
    • Chung, D.H.1
  • 122
    • 4143113653 scopus 로고    scopus 로고
    • Suppression of malignant growth of human breast cancer cells by ectopic expression of integrin-linked kinase
    • Chen, P., Shen, W. Z. & Karnik, P. Suppression of malignant growth of human breast cancer cells by ectopic expression of integrin-linked kinase. Int. J. Cancer 111, 881-891 (2004).
    • (2004) Int. J. Cancer , vol.111 , pp. 881-891
    • Chen, P.1    Shen, W.Z.2    Karnik, P.3
  • 123
    • 0036771764 scopus 로고    scopus 로고
    • Antiapoptotic role of PPARβ in keratinocytes via transcriptional control of the Akt1 signaling pathway
    • Di-Poi, N., Tan, N. S., Michalik, L., Wahli, W. & Desvergne, B. Antiapoptotic role of PPARβ in keratinocytes via transcriptional control of the Akt1 signaling pathway. Mol. Cell 10, 721-733 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 721-733
    • Di-Poi, N.1    Tan, N.S.2    Michalik, L.3    Wahli, W.4    Desvergne, B.5
  • 124
    • 0033615352 scopus 로고    scopus 로고
    • PPARδ is an APC-regulated target of nonsteroidal anti-inflammatory drugs
    • He, T. C., Chan, T. A., Vogelstein, B. & Kinzler, K. W. PPARδ is an APC-regulated target of nonsteroidal anti-inflammatory drugs. Cell 99, 335-345 (1999).
    • (1999) Cell , vol.99 , pp. 335-345
    • He, T.C.1    Chan, T.A.2    Vogelstein, B.3    Kinzler, K.W.4
  • 125
    • 0035956850 scopus 로고    scopus 로고
    • Genetic disruption of PPARδ decreases the tumorigenicity of human colon cancer cells
    • Park, B. H., Vogelstein, B. & Kinzler, K. W. Genetic disruption of PPARδ decreases the tumorigenicity of human colon cancer cells. Proc. Natl Acad. Sci. USA 98, 2598-2603 (2001).
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2598-2603
    • Park, B.H.1    Vogelstein, B.2    Kinzler, K.W.3
  • 126
    • 1942470331 scopus 로고    scopus 로고
    • Activation of nuclear hormone receptor peroxisome proliferator-activated receptor-δ accelerates intestinal adenoma growth
    • Gupta, R. A. et al. Activation of nuclear hormone receptor peroxisome proliferator-activated receptor-δ accelerates intestinal adenoma growth. Nature Med. 10, 245-247 (2004).
    • (2004) Nature Med. , vol.10 , pp. 245-247
    • Gupta, R.A.1
  • 127
    • 2342640982 scopus 로고    scopus 로고
    • Activation of peroxisome proliferator-activated receptor delta stimulates the proliferation of human breast and prostate cancer cell lines
    • Stephen, R. L. et al. Activation of peroxisome proliferator-activated receptor delta stimulates the proliferation of human breast and prostate cancer cell lines. Cancer Res. 64, 3162-3170 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 3162-3170
    • Stephen, R.L.1
  • 128
    • 4143127943 scopus 로고    scopus 로고
    • Overexpression of hyperactive integrin-linked kinase leads to increased ceuular radiosensitivity
    • Cordes, N. Overexpression of hyperactive integrin-linked kinase leads to increased ceuular radiosensitivity. Cancer Res. 64, 5683-5692 (2004).
    • (2004) Cancer Res. , vol.64 , pp. 5683-5692
    • Cordes, N.1
  • 129
    • 2942694338 scopus 로고    scopus 로고
    • Integrin-linked kinase (ILK) in combination molecular targeting
    • Edwards, L. A., Shabbits, J. A., Bally, M. & Dedhar, S. Integrin-linked kinase (ILK) in combination molecular targeting. Cancer Treat. Res. 119, 59-75 (2004).
    • (2004) Cancer Treat. Res. , vol.119 , pp. 59-75
    • Edwards, L.A.1    Shabbits, J.A.2    Bally, M.3    Dedhar, S.4
  • 130
    • 5144226211 scopus 로고    scopus 로고
    • PTEN activation contributes to tumor inhibition by trastuzumab, and loss of PTEN predicts trastuzumab resistance in patients
    • Nagata, Y. et al. PTEN activation contributes to tumor inhibition by trastuzumab, and loss of PTEN predicts trastuzumab resistance in patients. Cancer Cell 6, 117-127 (2004).
    • (2004) Cancer Cell , vol.6 , pp. 117-127
    • Nagata, Y.1
  • 131
    • 0037850992 scopus 로고    scopus 로고
    • C. elegans PAT-6/actopaxin plays a critical role in the assembly of integrin adhesion complexes in vivo
    • Lin, X., Qadota, H., Moerman, D. G. & Williams, B. D. C. elegans PAT-6/actopaxin plays a critical role in the assembly of integrin adhesion complexes in vivo. Curr. Biol. 13, 922-932 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 922-932
    • Lin, X.1    Qadota, H.2    Moerman, D.G.3    Williams, B.D.4
  • 132
    • 19944411156 scopus 로고    scopus 로고
    • Inhibition of ILK in PTEN-mutant human glioblastomas inhibits PKB/Akt activation, induces apoptosis, and delays tumour growth
    • in the press
    • Edwards, L. et al. Inhibition of ILK in PTEN-mutant human glioblastomas inhibits PKB/Akt activation, induces apoptosis, and delays tumour growth. Oncogene (in the press).
    • Oncogene
    • Edwards, L.1
  • 133
    • 11144230947 scopus 로고    scopus 로고
    • Inhibition of integrin-linked kinase(ILK) by a selective small molecule inhibitor, QLT054 inhibits the PI3K/PKB/mTOR, STAT-3 and FKHR pathways, tumour growth and enhances gemdtabine-induced apoptosis in human primary pancreatic cancer xenografts
    • in the press
    • Yau, C. et al. Inhibition of integrin-linked kinase(ILK) by a selective small molecule inhibitor, QLT054 inhibits the PI3K/PKB/mTOR, STAT-3 and FKHR pathways, tumour growth and enhances gemdtabine-induced apoptosis in human primary pancreatic cancer xenografts. Cancer Res. (in the press).
    • Cancer Res.
    • Yau, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.