Lymphocyte-Specific Ca²⁺-Binding Protein LSP1 Is Associated with the Cytoplasmic Face of the Plasma Membrane

LITERATURE CITED

• Bell, R. M.. 1986. Protein kinase C activation by diacylglycerol second messengers. Cell 46:631–632.
   Google Scholar
• Bradford, M. M.. 1974. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248–254.
   Web of Science ®Google Scholar
• Davis, T. N., M. S. Urdea, F. R. Masiarz, and J. Thorner. 1986. Isolation of the yeast calmodulin gene: calmodulin is an essential protein. Cell 47:423–431.
   PubMed Web of Science ®Google Scholar
• Ellis, L., E. Clausner, D. O. Morgan, M. Edery, R. A. Roth, and W. J. Rutter. 1986. Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose. Cell 45:721–723.
   PubMed Web of Science ®Google Scholar
• Erickson, A. H., and G. Blobel. 1983. Cell-free translation of messenger RNA in a wheat germ system. Methods EnzymoL 96:38–50.
   PubMedGoogle Scholar
• Forni, L.. 1979. Reagents for immunofluorescence and their use for studying lymphoid cell products, p. 151–167. In I. Lefkovits, and B. Pernis (ed.). Immunological methods. Academic Press, Inc., New York.
   Google Scholar
• Gilman, A. G.. 1987. G proteins: transducers of receptor generated signals. Annu. Rev. Biochem. 56:615–649.
   PubMed Web of Science ®Google Scholar
• Hager, D. A., and R. R. Burgess. 1980. Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels, removal of sodium dodecyl sulfate, and renaturation of enzymatic activity: results with sigma subunit of Escherichia coli RNA polymerase, wheat germ DNA topoisomerase, and other enzymes. Anal. Biochem. 109:76–86.
   PubMed Web of Science ®Google Scholar
• Hilgers, J., R. C. Nowinski, G. Geering, and W. Hardy. 1972. Detection of avian and mammalian oncogenic RNA viruses (oncornaviruses) by immunofluorescence. Cancer Res. 32:98–106.
   PubMedGoogle Scholar
• Jongstra, J., and M. M. Davis. 1988. Molecular genetic analysis of mouse B lymphocyte differentiation. UCLA Symp. Mol. Cell. Biol. New Ser. 56:261–268.
   Google Scholar
• Jongstra, J., J. Jongstra-Bilen, G. F. Tidmarsh, and M. M. Davis. 1988. The in vitro translation product of the murine lambda 5 gene contains a functional signal peptide. Mol. Immunol. 25:687–693.
   PubMedGoogle Scholar
• Jongstra, J., G. F. Tidmarsh, J. Jongstra-Bilen, and M. M. Davis. 1988. A new lymphocyte-specific gene which encodes a putative Ca2+-binding protein is not expressed in transformed T lymphocyte lines. J. Immunol. 141:3999–4004.
   PubMedGoogle Scholar
• Kammer, G. M.. 1988. The adenylate cyclase-cAMP-protein kinase A pathway and regulation of the immune response. Immunol. Today 9:222–229.
   PubMedGoogle Scholar
• Kretsinger, R. H.. 1979. The informational role of calcium in the cytosol. Adv. Cyclic Nucleotide Res. 11:1–26.
   PubMedGoogle Scholar
• Kretsinger, R. H., and C. E. Nockolds. 1973. Carp muscle calcium-binding protein. II. Structure determination and general description. J. Biol. Chem. 248:3313–3326.
   PubMed Web of Science ®Google Scholar
• Laemmli, U. K.. 1970. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature (London) 227:680–685.
   PubMed Web of Science ®Google Scholar
• Maruyama, K., T. Mikawa, and S. Ebashi. 1984. Detection of calcium binding proteins by 45Ca autoradiography on nitrocellulose membrane after sodium dodecyl sulfate gel electrophoresis. J. Biochem. 95:511–519.
   PubMed Web of Science ®Google Scholar
• Means, A. R., J. S. Tash, and J. G. Chafouleas. 1982. Physiological implications of the presence, distribution, and regulation of calmodulin in eukaryotic cells. Physiol. Rev. 62:1–39.
   PubMed Web of Science ®Google Scholar
• Nishizuka, Y.. 1984. Studies and perspectives on protein kinase C. Science 233:305–312.
   Google Scholar
• Potter, J. D., and J. Gergely. 1975. The calcium and magnesium binding sites on troponin and their role in the regulation of myofibrillar adenosine triphosphatase. J. Biol. Chem. 250:4628–4633.
   PubMed Web of Science ®Google Scholar
• Pozzan, T., P. Arslan, R. Y. Tsien, and T. J. Rink. 1982. Anti-immunoglobulin. cytoplasmic free calcium, and capping in B lymphocytes. J. Cell Biol. 94:335–340.
   PubMedGoogle Scholar
• Quigley, J. P.. 1976. Association of a protease (plasminogen activator) with a specific membrane fraction isolated from transformed ceils. J. Cell Biol. 71:472–486.
   PubMed Web of Science ®Google Scholar
• Ransom, J. T., D. L. Digiusto, and J. C. Cambier. 1986. Single cell analysis of calcium mobilization in anti-immunoglobulin stimulated B lymphocytes. J. Immunol. 136:54–57.
   PubMed Web of Science ®Google Scholar
• Rosenberg, A. H., B. N. Lade, D.-S. Chui, S.-W. Lin, J. J. Dunn, and F. W. Studier. 1987. Vectors for selective expression of cloned DNAs by T7 RNA polymerase. Gene 56:125–135.
   PubMed Web of Science ®Google Scholar
• Studier, F. W., and B. A. Moffat. 1986. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:113–130.
   PubMed Web of Science ®Google Scholar
• Von Heijne, G.. 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res. 14:4683–4690.
   PubMed Web of Science ®Google Scholar
• Walter, P., and G. Blobel. 1983. Preparation of microsomal membranes for cotranslational protein translocation. Methods Enzymol. 96:84–93.
   PubMedGoogle Scholar
• Watson, M. E. E.. 1984. Compilation of published signal sequences. Nucleic Acids Res. 12:5145–5164.
   PubMed Web of Science ®Google Scholar
• Weiss, A., J. Imboden, D. Shoback, and J. Stobo. 1984. Role of T3 surface molecules in human T-cell activation: T3-dependent activation results in an increase in cytoplasmic free calcium. Proc. Natl. Acad. Sci. USA 81:4169–4173.
   PubMed Web of Science ®Google Scholar
• Weiss, M. J., J. F. Daley, J. C. Hodgdon, and E. L. Reinherz. 1984. Calcium dependency of antigen-specific (T3-Ti) and alternative (T11) pathways of human T-cell activation. Proc. Natl. Acad. Sci. USA 81:6836–6840.
   PubMed Web of Science ®Google Scholar