Src uses Cas to suppress Fhl1 in order to promote nonanchored growth and migration of tumor cells

Cancer Research

Volumn 66, Issue 3, 2006, Pages 1543-1552

  Shen, Yongquan ^a   Jia, Zhenyu ^a   Nagele, Robert G ^a   Ichikawa, Hitoshi ^b   Goldberg, Gary S ^a  

^a UNIVERSITY OF MEDICINE AND DENTISTRY OF NEW JERSEY   (United States)

^b NATIONAL CANCER CENTER RESEARCH INSTITUTE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN; STEROID RECEPTOR COACTIVATOR 1;

ANCHORAGE INDEPENDENT GROWTH; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CELL JUNCTION; CELL MIGRATION; CELL TRANSFORMATION; CONTROLLED STUDY; FHL1 GENE; GENE EXPRESSION; GENE IDENTIFICATION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; TUMOR CELL; TUMOR GROWTH; TUMOR SUPPRESSOR GENE;

AMINO ACID SEQUENCE; ANIMALS; CELL ADHESION; CELL GROWTH PROCESSES; CELL LINE, TUMOR; CELL MOVEMENT; CELLULAR APOPTOSIS SUSCEPTIBILITY PROTEIN; GENE EXPRESSION REGULATION, NEOPLASTIC; GENES, TUMOR SUPPRESSOR; HUMANS; MICE; MICE, KNOCKOUT; MOLECULAR SEQUENCE DATA; MUSCLE PROTEINS; NEOPLASMS, EXPERIMENTAL; PHOSPHORYLATION; SRC-FAMILY KINASES;

EID: 32944468266     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-05-3152     Document Type: Article

References (39)

1. Frisch SM, Screaton RA. Anoikis mechanisms. Curr Opin Cell Biol 2001;13:555-62.
2. Giancotti FG, Ruoslahti E. Integrin signaling. Science 1999;285:1028-32.
3. Honda H, Oda H, Nakamoto T, et al. Cardiovascular anomaly, impaired actin bundling and resistance to Src-induced transformation in mice lacking p130Cas. Nat Genet 1998;19:361-5.
4. Huang J, Hamasaki H, Nakamoto T, et al. Differential regulation of cell migration, actin stress fiber organization, and cell transformation by functional domains of Crk-associated substrate. J Biol Chem 2002;277:27265-72.
5. Cho SY, Klemke RL. Extracellular-regulated kinase activation and CAS/Crk coupling regulate cell migration and suppress apoptosis during invasion of the extracellular matrix. J Cell Biol 2000;149:223-36.
6. Klemke RL, Leng J, Molander R, et al. CAS/Crk coupling serves as a "molecular switch" for induction of cell migration. J Cell Biol 1998;140:961-72.
7. Brabek J, Constancio SS, Shin NY, et al. CAS promotes invasiveness of Src-transformed cells. Oncogene 2004;23:7406-15.
8. Shin NY, Dise RS, Schneider-Mergener J, et al. Subsets of the major tyrosine phosphorylation sites in Crk-associated substrate (CAS) are sufficient to promote cell migration. J Biol Chem 2004;279:38331-7.
9. Goldberg GS, Alexander DB, Pellicena P, et al. Src phosphorylates Cas on tyrosine 253 to promote migration of transformed cells. J Biol Chem 2003;278:46533-40.
10. Bouton AH, Riggins RB, Bruce-Staskal PJ. Functions of the adapter protein Cas: signal convergence and the determination of cellular responses. Oncogene 2001;20:6448-58.
11. Schlaepfer DD, Hauck CR, Sieg DJ. Signaling through focal adhesion kinase. Prog Biophys Mol Biol 1999;71:435-78.
12. Sieg DJ, Hauck CR, Schlaepfer DD. Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration. J Cell Sci 1999;112:2677-91.
13. Sakai R, Iwamatsu A, Hirano N, et al. A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J 1994;13:3748-56.
14. Burnham MR, Harte MT, Richardson A, et al. The identification of p130cas-binding proteins and their role in cellular transformation. Oncogene 1996;12:2467-72.
15. Vuori K, Hirai H, Aizawa S, et al. Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases. Mol Cell Biol 1996;16:2606-13.
16. Bignami M, Rosa S, La Rocca SA, et al. Differential influence of adjacent normal cells on the proliferation of mammalian cells transformed by the viral oncogenes myc, ras and src. Oncogene 1988;2:309-14.
17. Martin W, Zempel G, Hulser D, et al. Growth inhibition of oncogene-transformed rat fibroblasts by cocultured normal cells: relevance of metabolic cooperation mediated by gap junctions. Cancer Res 1991;51:5348-51.
18. Alexander DB, Ichikawa H, Bechberger JF, et al. Normal cells control the growth of neighboring transformed cells independent of gap junctional communication and SRC activity. Cancer Res 2004;64:1347-58.
19. Taniguchi Y, Furukawa T, Tun T, et al. LIM protein KyoT2 negatively regulates transcription by association with the RBP-J DNA-binding protein. Mol Cell Biol 1998;18:644-54.
20. Qin H, Du D, Zhu Y, et al. The PcG protein HPC2 inhibits RBP-J-mediated transcription by interacting with LIM protein KyoT2. FEBS Lett 2005;579:1220-6.
21. Brown S, McGrath MJ, Ooms LM, et al. Characterization of two isoforms of the skeletal muscle LIM protein 1, SLIM1. Localization of SLIM1 at focal adhesions and the isoform slimmer in the nucleus of myoblasts and cytoplasm of myotubes suggests distinct roles in the cytoskeleton and in nuclear-cytoplasmic communication. J Biol Chem 1999;274:27083-91.
22. Huang HY, Li R. Sun Q, et al. LIM protein KyoT2 interacts with human tight junction protein ZO-2-i3. Yi Chuan Xue Bao 2002;29:953-8.
23. Goldberg GS, Jin Z, Ichikawa H, et al. Global effects of anchorage on gene expression during mammary carcinoma cell growth reveal role of tumor necrosis factor-related apoptosis-inducing ligand in anoikis. Cancer Res 2001;61:1334-7.
24. Goldberg GS, Bechberger JF, Tajima Y, et al. Connexin43 suppresses MFG-E8 while inducing contact growth inhibition of glioma cells. Cancer Res 2000;60:6018-26.
25. Nagele RG, D'Andrea MR, Anderson WJ, et al. Intracellular accumulation of β-amyloid(1-42) in neurons is facilitated by the α7 nicotinic acetylcholine receptor in Alzheimer's disease. Neuroscience 2002;110:199-211.
26. Schmeichel KL, Beckerle MC. The LIM domain is a modular protein-binding interface. Cell 1994;79:211-9.
27. Durbec P, Marcos-Gutierrez CV, Kilkenny C, et al. GDNF signalling through the Ret receptor tyrosine kinase. Nature 1996;381:789-93.
28. Jing S, Wen D, Yu Y, et al. GDNF-induced activation of the ret protein tyrosine kinase is mediated by GDNFR-α, a novel receptor for GDNF. Cell 1996;85:1113-24.
29. Trupp M, Arenas E, Fainzilber M, et al. Functional receptor for GDNF encoded by the c-ret proto-oncogene. Nature 1996;381:785-9.
30. Hishiki T, Nimura Y, Isogai E, et al. Glial cell line-derived neurotrophic factor/neurturin-induced differentiation and its enhancement by retinoic acid in primary human neuroblastomas expressing c-Ret, GFR α-1, and GFR α-2. Cancer Res 1998;58:2158-65.
31. Playford MP, Schaller MD. The interplay between Src and integrins in normal and tumor biology. Oncogene 2004;23:7928-46.
32. Brabek J, Constancio SS, Siesser PF, et al. Crk-associated substrate tyrosine phosphorylation sites are critical for invasion and metastasis of SRC-transformed cells. Mol Cancer Res 2005;3:307-15.
33. Sanders MA, Basson MD. p130cas but not paxillin is essential for Caco-2 intestinal epithelial cell spreading and migration on collagen IV. J Biol Chem 2005;280:23516-22.
34. Jaggi R, Hock W, Ziemiecki A, et al. Oncogene mediated repression of glucocorticoid hormone response elements and glucocorticoid receptor levels. Cancer Res 1989;49:2266-74s.
35. Ramalho-Santos M, Yoon S, Matsuzaki Y, et al. "Stemness": transcriptional profiling of embryonic and adult stem cells. Science 2002;298:597-600.
36. Morgan MJ, Whawell SA The structure of the human LIM protein ACT gene and its expression in tumor cell lines. Biochem Biophys Res Commun 2000;273:776-83.
37. Grossi M, Hiou-Feige A, Di Vignano AT, et al. Negative control of keratinocyte differentiation by Rho/CRIK signaling coupled with up-regulation of KyoT1/2 (FHL1) expression. Proc Natl Acad Sci U S A 2005;102:11313-8.
38. Brinkman A, Van der FS, Kok EM, et al. BCAR1, a human homologue of the adapter protein p130Cas, and antiestrogen resistance in breast cancer cells. J Natl Cancer Inst 2000;92:112-20.
39. Dorssers LC, Grebenchtchikov N, Brinkman A, et al. The prognostic value of BCAR1 in patients with primary breast cancer. Clin Cancer Res 2004;10:6194-202.