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TIAM1  -  T-cell lymphoma invasion and metastasis 1

Homo sapiens

Synonyms: T-lymphoma invasion and metastasis-inducing protein 1, TIAM-1
 
 
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Disease relevance of TIAM1

 

High impact information on TIAM1

 

Chemical compound and disease context of TIAM1

 

Biological context of TIAM1

 

Anatomical context of TIAM1

  • Sequence of the human invasion-inducing TIAM1 gene, its conservation in evolution and its expression in tumor cell lines of different tissue origin [2].
  • We have identified a gene, T-cell lymphoma invasion and metastasis 2 (HGMW-approved symbol TIAM2), with significant identity to the carboxyl-terminal region of the TIAM1 and mapped it to 6q25 [1].
  • Our results suggested that Tiam1 signaling contributed to the invasion and metastasis of the human giant-cell lung carcinoma cells [7].
  • Moreover, in 1321N1 astrocytoma cells, translocation of Tiam1 to the cytosol, following receptor-mediated stimulation of PtdIns(4,5)P(2) breakdown, correlates with decreased Rac1-GTP levels, indicating that membrane-association is required for GDP/GTP exchange on Rac1 [8].
  • Inositol phospholipids regulate the guanine-nucleotide-exchange factor Tiam1 by facilitating its binding to the plasma membrane and regulating GDP/GTP exchange on Rac1 [8].
 

Associations of TIAM1 with chemical compounds

  • Tiam1 is a member of the Dbl family of guanine nucleotide exchange factors that activate Rho family GTPases [9].
  • Certain phosphoinositides also stimulated Tiam1 activity but were less potent than ascorbyl stearate [9].
  • Finally, the data demonstrate that PtdIns(4,5)P(2) and PtdIns(3,4,5)P(3) bind to the same pleckstrin homology domain in Tiam1 and that soluble inositol phosphates appear to compete with lipids for this binding [8].
  • Finally, we demonstrate that in cells treated with ceramide, cleavage of TIAM1 coincided with the inactivation of endogenous Rac [10].
  • While the PH domains of intersectin and Dbs promiscuously bind several multiphosphorylated phosphoinositides, Tiam1 selectively interacts with phosphatidylinositol 3-phosphate (K(D) approximately 5-10 microm) [11].
 

Physical interactions of TIAM1

 

Regulatory relationships of TIAM1

  • These results suggest that nm23H1 negatively regulates Tiam1 and inhibits Rac1 activation in vivo [13].
  • The reverse transition from mesenchymal invasive to a resident epithelial-like phenotype implicates a role for Tiam1/Rac signaling in the control of cell-cell contacts through a novel ALCAM-mediated mechanism [3].
  • In contrast, Rac2 displays a slower nucleotide association and is more efficiently activated by the Rac-GEF Tiam1 [14].
  • Stable overexpression of Tiam1 or constitutively active V12-Rac1 in a human renal cell carcinoma cell line (clearCa-28) strongly inhibited cell migration by promoting E-cadherin-mediated cell-cell adhesion [15].
 

Other interactions of TIAM1

  • Tumor metastasis suppressor nm23H1 regulates Rac1 GTPase by interaction with Tiam1 [13].
  • Regulation of Tiam1 nucleotide exchange activity by pleckstrin domain binding ligands [9].
  • Blocking E-cadherin-mediated adhesion by E-cadherin-specific HAV peptides allowed cells to migrate, but was not sufficient to antagonize Tiam1- and V12-Rac1-induced inhibition of Matrigel invasion, suggesting that Rac may influence invasion also through other mechanisms [15].
  • In group A tumors, Rac was positive in 10/35 (28%), cdc42 was positive in 12/35 (34%) and Tiam1 was positive in 30/35 (85%) tumors [16].
  • Here we demonstrate that the conserved PH domains of three distinct Dbl family proteins, intersectin, Dbs, and Tiam1, selectively bind lipid vesicles only when phosphoinositides are present [11].
 

Analytical, diagnostic and therapeutic context of TIAM1

References

  1. Cloning and characterization of T-cell lymphoma invasion and metastasis 2 (TIAM2), a novel guanine nucleotide exchange factor related to TIAM1. Chiu, C.Y., Leng, S., Martin, K.A., Kim, E., Gorman, S., Duhl, D.M. Genomics (1999) [Pubmed]
  2. Sequence of the human invasion-inducing TIAM1 gene, its conservation in evolution and its expression in tumor cell lines of different tissue origin. Habets, G.G., van der Kammen, R.A., Stam, J.C., Michiels, F., Collard, J.G. Oncogene (1995) [Pubmed]
  3. The RacGEF Tiam1 inhibits migration and invasion of metastatic melanoma via a novel adhesive mechanism. Uhlenbrock, K., Eberth, A., Herbrand, U., Daryab, N., Stege, P., Meier, F., Friedl, P., Collard, J.G., Ahmadian, M.R. J. Cell. Sci. (2004) [Pubmed]
  4. Tiam1 gene expression and its significance in colorectal carcinoma. Liu, L., Wu, D.H., Ding, Y.Q. World J. Gastroenterol. (2005) [Pubmed]
  5. Inhibition of invasion of epithelial cells by Tiam1-Rac signaling. Hordijk, P.L., ten Klooster, J.P., van der Kammen, R.A., Michiels, F., Oomen, L.C., Collard, J.G. Science (1997) [Pubmed]
  6. Withdrawal phenomena in subjects with essential hypertension on clonidine or tiamenidine. Hamilton, B.P., Mersey, J.H., Hamilton, J., Kuzbida, G., Pavlis, R., Levinson, P. Clin. Pharmacol. Ther. (1984) [Pubmed]
  7. Antisense Tiam1 down-regulates the invasiveness of 95D cells in vitro. Hou, M., Tan, L., Wang, X., Zhu, Y.S. Acta Biochim. Biophys. Sin. (Shanghai) (2004) [Pubmed]
  8. Inositol phospholipids regulate the guanine-nucleotide-exchange factor Tiam1 by facilitating its binding to the plasma membrane and regulating GDP/GTP exchange on Rac1. Fleming, I.N., Batty, I.H., Prescott, A.R., Gray, A., Kular, G.S., Stewart, H., Downes, C.P. Biochem. J. (2004) [Pubmed]
  9. Regulation of Tiam1 nucleotide exchange activity by pleckstrin domain binding ligands. Crompton, A.M., Foley, L.H., Wood, A., Roscoe, W., Stokoe, D., McCormick, F., Symons, M., Bollag, G. J. Biol. Chem. (2000) [Pubmed]
  10. Caspase-mediated cleavage of the TIAM1 guanine nucleotide exchange factor during apoptosis. Qi, H., Juo, P., Masuda-Robens, J., Caloca, M.J., Zhou, H., Stone, N., Kazanietz, M.G., Chou, M.M. Cell Growth Differ. (2001) [Pubmed]
  11. Quantitative analysis of the effect of phosphoinositide interactions on the function of Dbl family proteins. Snyder, J.T., Rossman, K.L., Baumeister, M.A., Pruitt, W.M., Siderovski, D.P., Der, C.J., Lemmon, M.A., Sondek, J. J. Biol. Chem. (2001) [Pubmed]
  12. The Rac1-GEF Tiam1 couples the NMDA receptor to the activity-dependent development of dendritic arbors and spines. Tolias, K.F., Bikoff, J.B., Burette, A., Paradis, S., Harrar, D., Tavazoie, S., Weinberg, R.J., Greenberg, M.E. Neuron (2005) [Pubmed]
  13. Tumor metastasis suppressor nm23H1 regulates Rac1 GTPase by interaction with Tiam1. Otsuki, Y., Tanaka, M., Yoshii, S., Kawazoe, N., Nakaya, K., Sugimura, H. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  14. Comparative functional analysis of the Rac GTPases. Haeusler, L.C., Blumenstein, L., Stege, P., Dvorsky, R., Ahmadian, M.R. FEBS Lett. (2003) [Pubmed]
  15. Rac affects invasion of human renal cell carcinomas by up-regulating tissue inhibitor of metalloproteinases (TIMP)-1 and TIMP-2 expression. Engers, R., Springer, E., Michiels, F., Collard, J.G., Gabbert, H.E. J. Biol. Chem. (2001) [Pubmed]
  16. Expressions of Rac1, Tiam1 and Cdc42 in retinoblastoma. Adithi, M., Venkatesan, N., Kandalam, M., Biswas, J., Krishnakumar, S. Exp. Eye Res. (2006) [Pubmed]
  17. Tiam1 is involved in the regulation of bufalin-induced apoptosis in human leukemia cells. Kawazoe, N., Watabe, M., Masuda, Y., Nakajo, S., Nakaya, K. Oncogene (1999) [Pubmed]
  18. Prognostic relevance of Tiam1 protein expression in prostate carcinomas. Engers, R., Mueller, M., Walter, A., Collard, J.G., Willers, R., Gabbert, H.E. Br. J. Cancer (2006) [Pubmed]
 
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