92
Views
135
CrossRef citations to date
0
Altmetric
Cell Growth and Development

Structure-Function Analysis of Lyn Kinase Association with Lipid Rafts and Initiation of Early Signaling Events after Fcɛ Receptor I Aggregation

, , , , &
Pages 8318-8328 | Received 23 Jul 2001, Accepted 14 Sep 2001, Published online: 27 Mar 2023

REFERENCES

  • Alber, G. L., L. Miller, C. L. Jelsema, N. Varin-Blank, and H. Metzger. 1991. Structure-function relationships in the mast cell high affinity receptor for IgE. J. Biol. Chem. 266:22613–22620.
  • Amoui, M., L. Dráberová, P. Tolar, and P. Dráber. 1997. Direct interaction of Syk and Lyn protein tyrosine kinases in rat basophilic leukemia cells activated via type I Fcɛ receptor. Eur. J. Immunol. 27:321–328.
  • Amoui, M., P. Dráber, and L. Dráberová. 1997. Src family-selective tyrosine kinase inhibitor, PP1, inhibits both FcɛRI- and Thy-1-mediated activation of rat basophilic leukemia cells. Eur. J. Immunol. 27:1881–1886.
  • Arudchandran, R., M. J. Brown, J. S. Song, S. A. Wank, H. Haleem-Smith, and J. Rivera. 1999. Polyethylene glycol-mediated infection of non-permissive mammalian cells with Semliki Forest virus: application to signal transduction studies. J. Immunol. Methods 222:197–208.
  • Arudchandran, R., M. J. Brown, M. J. Peirce, J. S. Song, J. Zhang, R. P. Siraganian, U. Blank, and J. Rivera. 2000. The Src homology 2 domain of Vav is required for its compartmentation to the plasma membrane and activation of c-Jun NH2-terminal kinase 1. J. Exp. Med. 191:47–59.
  • Benhamou, M., N. J. P. Ryba, H. Kihara, H. Nishikata, and R. P. Siraganian. 1993. Protein-tyrosine kinase p72syk in high affinity IgE receptor signaling. J. Biol. Chem. 268:23318–233324.
  • Bijlmakers, M. J., M. Isobe-Nakamura, L. J. Ruddock, and M. Marsh. 1997. Intrinsic signals in the unique domain target p56lck to the plasma membrane independently of CD4. J. Cell Biol. 137:1029–1040.
  • Brdic̆ka, T., D. Pavlis̆tová, A. Leo, E. Bruyns, V. Kor̆ı́nek, P. Angelisová, J. Scherer, A. Shevchenko, I. Hilgert, J. C̆erný, K. Drbal, Y. Kuramitsu, B. Kornacker, V. Hor̆ejs̆ı́, and B. Schraven. 2000. Phosphoprotein associated with glycosphingolipid-enriched microdomains (PAG), a novel ubiquitously expressed transmembrane adaptor protein, binds the protein tyrosine kinase csk and is involved in regulation of T cell activation. J. Exp. Med. 191:1591–1604.
  • Brown, D. A., and E. London. 1998. Functions of lipid rafts in biological membranes. Annu. Rev. Cell Dev. Biol. 14:111–136.
  • Cheng, P. C., M. L. Dykstra, R. N. Mitchell, and S. K. Pierce. 1999. A role for lipid rafts in B cell antigen receptor signaling and antigen targeting. J. Exp. Med. 190:1549–1560.
  • Dráberová, L., and P. Dráber. 1991. Functional expression of the endogenous Thy-1 gene and the transfected murine Thy-1.2 gene in rat basophilic leukemia cells. Eur. J. Immunol. 21:1583–1590.
  • Dráberová, L., E. Dráberová, Z. Surviladze, P. Dráber, and Pa. Dráber. 1999. Protein tyrosine kinase p53/p56lyn forms complexes with γ-tubulin in rat basophilic leukemia cells. Int. Immunol. 11:1829–1839.
  • Dráberová, L., M. Amoui, and P. Dráber. 1996. Thy-1-mediated activation of rat mast cells: the role of Thy-1 membrane microdomains. Immunology 87:141–148.
  • Eiseman, E., and J. B. Bolen. 1992. Engagement of the high-affinity IgE receptor activates src protein-related tyrosine kinases. Nature 355:78–80.
  • Field, K. A., D. Holowka, and B. Baird. 1995. FcɛRI-mediated recruitment of p53/56lyn to detergent-resistant membrane domains accompanies cellular signaling. Proc. Natl. Acad. Sci. USA 92:9201–9205.
  • Field, K. A., D. Holowka, and B. Baird. 1997. Compartmentalized activation of the high affinity immunoglobulin E receptor within membrane domains. J. Biol. Chem. 272:4276–4280.
  • Field, K. A., D. Holowka, and B. Baird. 1999. Structural aspects of the association of FcɛRI with detergent-resistant membranes. J. Biol. Chem. 274:1753–1758.
  • Haleem-Smith, H., E. Y. Chang, Z. Szallasi, P. M. Blumberg, and J. Rivera. 1995. Tyrosine phosphorylation of protein kinase C-δ in response to the activation of the high-affinity receptor for immunoglobulin E modifies its substrate recognition. Proc. Natl. Acad. Sci. USA 92:9112–9116.
  • Hibbs, M. L., D. M. Tarlinton, J. Armes, D. Grail, G. Hodgson, R. Maglitto, S. A. Stacker, and A. R. Dunn. 1995. Multiple defects in the immune system of Lyn-deficient mice, culminating in autoimmune disease. Cell 83:301–311.
  • Holowka, D., E. D. Sheets, and B. Baird. 2000. Interactions between FcɛRI and lipid raft components are regulated by the actin cytoskeleton. J. Cell Sci. 113:1009–1019.
  • Honda, Z., T. Suzuki, H. Kono, M. Okada, T. Yamamoto, C. Ra, Y. Morita, and K. Yamamoto. 2000. Sequential requirements of the N-terminal palmitoylation site and SH2 domain of Src family kinases in the initiation and progression of FcɛRI signaling. Mol. Cell. Biol. 20:1759–1771.
  • Hutchcroft, J. E., R. L. Geahlen, G. G. Deanin, and J. M. Oliver. 1992. FcɛRI-mediated tyrosine phosphorylation and activation of the 72-kD protein-tyrosine kinase, PTK72, in RBL-2H3 rat tumor mast cells. Proc. Natl. Acad. Sci. USA 89:9107–9111.
  • Janes, P. W., S. C. Ley, and A. I. Magee. 1999. Aggregation of lipid rafts accompanies signaling via the T cell antigen receptor. J. Cell Biol. 147:447–461.
  • Kawabuchi, M., Y. Satomi, T. Takao, Y. Shimonishi, S. Nada, K. Nagai, A. Tarakhovsky, and M. Okada. 2000. Transmembrane phosphoprotein Cbp regulates the activities of Src-family tyrosine kinases. Nature 404:999–1003.
  • Kihara, H., and R. P. Siraganian. 1994. Src homology 2 domains of Syk and Lyn bind to tyrosine-phosphorylated subunit of the high affinity IgE receptor. J. Biol. Chem. 269:22427–22432.
  • Li, W., G. G. Deanin, B. Margolis, J. Schlessinger, and J. M. Oliver. 1992. FcɛRI-mediated tyrosine phosphorylation of multiple proteins, including phospholipase Cγ1 and the receptor βγ2 complex, in RBL-2H3 rat basophilic leukemia cells. Mol. Cell. Biol. 12:3176–3182.
  • Lin, S., C. Cicala, A. M. Scharenberg, and J. P. Kinet. 1996. The FcɛRIβ subunit functions as an amplifier of FcɛRIγ-mediated cell activation signals. Cell 85:985–995.
  • Minoguchi, K., M. Benhamou, W. D. Swaim, Y. Kawakami, T. Kawakami, and R. P. Siraganian. 1994. Activation of protein tyrosine kinase p72syk by FcɛRI aggregation in rat basophilic leukemia cells. J. Biol. Chem. 269:16902–16908.
  • Montixi, C., C. Langlet, A. M. Bernard, J. Thimonier, C. Dubois, M. A. Wurbel, J. P. Chauvin, M. Pierres, and H. T. He. 1998. Engagement of T cell receptor triggers its recruitment to low-density detergent-insoluble membrane domains. EMBO J. 17:5334–5348.
  • Ortega, E., M. Lara, I. Lee, C. Santana, A. M. Martinez, J. R. Pfeiffer, R. J. Lee, B. S. Wilson, and J. M. Oliver. 1999. Lyn dissociation from phosphorylated FcɛRI subunits: A new regulatory step in the FcɛRI signaling cascade revealed by studies of FcɛRI dimer signaling activity. J. Immunol. 162:176–185.
  • Paolini, R., M. H. Jouvin, and J. P. Kinet. 1991. Phosphorylation and dephosphorylation of the high-affinity receptor for immunoglobulin E immediately after receptor engagement and disengagement. Nature 353:855–858.
  • Perez-Montfort, R., J. P. Kinet, and H. Metzger. 1983. A previously unrecognized subunit of the receptor for immunoglobulin E. Biochemistry 22:5722–5728.
  • Pribluda, V. S., C. Pribluda, and H. Metzger. 1994. Transphosphorylation as the mechanism by which the high-affinity receptor for IgE is phosphorylated upon aggregation. Proc. Natl. Acad. Sci. USA 91:11246–11250.
  • Repetto, B., G. Bandara, H. Kado Fong, J. D. Larigan, G. A. Wiggan, D. Pocius, M. Basu, A. M. Gilfillan, and J. P. Kochan. 1996. Functional contributions of the FcɛRIα and FcɛRIγ subunit domains in FcɛRI-mediated signaling in mast cells. J. Immunol. 156:4876–4883.
  • Rivera, J., J. P. Kinet, J. Kim, C. Pucillo, and H. Metzger. 1988. Studies with a monoclonal antibody to the β subunit of the receptor with high affinity for immunoglobulin E. Mol. Immunol. 25:647–661.
  • Rudolph, A. K., P. D. Burrows, and M. R. Wabl. 1981. Thirteen hybridomas secreting hapten-specific immunoglobulin E from mice with Iga or Igb heavy chain haplotype. Eur. J. Immunol. 11:527–529.
  • Saitoh, S., R. Arudchandran, T. S. Manetz, W. Zhang, C. L. Sommers, P. E. Love, J. Rivera, and L. E. Samelson. 2000. LAT is essential for FcɛRI-mediated mast cell activation. Immunity 12:525–535.
  • Sheets, E. D., D. Holowka, and B. Baird. 1999. Critical role for cholesterol in Lyn-mediated tyrosine phosphorylation of FcɛRI and their association with detergent-resistant membranes. J. Cell Biol. 145:877–887.
  • Shenoy-Scaria, A. M., L. K. Gauen, J. Kwong, A. S. Shaw, and D. M. Lublin. 1993. Palmitylation of an amino-terminal cysteine motif of protein tyrosine kinases p56lck and p59fyn mediates interaction with glycosyl-phosphatidylinositol-anchored proteins. Mol. Cell. Biol. 13:6385–6392.
  • Simons, K., and E. Ikonen. 1997. Functional rafts in cell membranes. Nature 387:569–572.
  • Song, J. S., J. Gomez, L. F. Stancato, and J. Rivera. 1996. Association of a p95 Vav-containing signaling complex with the FcɛRI γ chain in the RBL-2H3 mast cell line. Evidence for a constitutive in vivo association of Vav with Grb2, Raf-1, and ERK2 in an active complex. J. Biol. Chem. 271:26962–26970.
  • Stauffer, T. P., and T. Meyer. 1997. Compartmentalized IgE receptor-mediated signal transduction in living cells. J. Cell Biol. 139:1447–1454.
  • Surviladze, Z., L. Dráberová, L. Kubı́nová, and P. Dráber. 1998. Functional heterogeneity of Thy-1 membrane microdomains in rat basophilic leukemia cells. Eur. J. Immunol. 28:1847–1858.
  • Surviladze, Z., L. Dráberová, M. Kovár̆ová, M. Boubelı́k, and P. Dráber. 2001. Differential sensitivity to acute cholesterol lowering of activation mediated via the high-affinity IgE receptor and Thy-1 glycoprotein. Eur. J. Immunol. 31:1–10.
  • Swann, P. G., S. Odom, Y.-J. Zhou, Z. Szallasi, P. M. Blumberg, P. Draber, and J. Rivera. 1999. Requirement for a negative charge at threonine 60 of the FcRγ for complete activation of Syk. J. Biol. Chem. 274:23068–23077.
  • Tolar, P., L. Dráberová, and P. Dráber. 1997. Protein tyrosine kinase Syk is involved in Thy-1 signaling in rat basophilic leukemia cells. Eur. J. Immunol. 27:3389–3397.
  • Turner, H., K. Reif, J. Rivera, and D. A. Cantrell. 1995. Regulation of the adapter molecule Grb2 by FcɛR1 in the mast cell line RBL2H3. J. Biol. Chem. 270:9500–9506.
  • Vonakis, B. M., H. Chen, H. Haleem-Smith, and H. Metzger. 1997. The unique domain as the site on Lyn kinase for its constitutive association with the high affinity receptor for IgE. J. Biol. Chem. 272:24072–24080.
  • Vonakis, B. M., H. Haleem-Smith, P. Benjamin, and H. Metzger. 2001. Interaction between the unphosphorylated receptor with high affinity for IgE and Lyn kinase. J. Biol. Chem. 276:1041–1050.
  • Wilson, B. S., J. R. Pfeiffer, and J. M. Oliver. 2000. Observing FcɛRI signaling from the inside of the mast cell membrane. J. Cell Biol. 149:1131–1142.
  • Xavier, R., T. Brennan, Q. Li, C. McCormack, and B. Seed. 1998. Membrane compartmentation is required for efficient T cell activation. Immunity 8:723–732.
  • Zhang, W., J. Sloan-Lancaster, J. Kitchen, R. P. Trible, and L. E. Samelson. 1998. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation. Cell 92:83–92.
  • Zhang, W., R. P. Trible, and L. E. Samelson. 1998. LAT palmitoylation: its essential role in membrane microdomain targeting and tyrosine phosphorylation during T cell activation. Immunity 9:239–246.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.