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Molecular and Cellular Biology Volume 12, 1992 - Issue 8
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Letter to the Editor

SEC22 and SLY2 Are Identical

Anna P. Newmana Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut06510;b Department of Molecular Genetics, Max Planck Institute for Biophysical Chemistry, PO Box 2841, D-3400Göttingen, Germany
,
Jennifer Grafa Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut06510;b Department of Molecular Genetics, Max Planck Institute for Biophysical Chemistry, PO Box 2841, D-3400Göttingen, Germany
,
Patrizia Mancinia Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut06510;b Department of Molecular Genetics, Max Planck Institute for Biophysical Chemistry, PO Box 2841, D-3400Göttingen, Germany
,
Guendalina Rossia Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut06510;b Department of Molecular Genetics, Max Planck Institute for Biophysical Chemistry, PO Box 2841, D-3400Göttingen, Germany
,
Jian P. Liana Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut06510;b Department of Molecular Genetics, Max Planck Institute for Biophysical Chemistry, PO Box 2841, D-3400Göttingen, Germany
,
Susan Ferro-Novicka Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut06510;b Department of Molecular Genetics, Max Planck Institute for Biophysical Chemistry, PO Box 2841, D-3400Göttingen, Germany
,
Rainer Ossiga Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut06510;b Department of Molecular Genetics, Max Planck Institute for Biophysical Chemistry, PO Box 2841, D-3400Göttingen, Germany
,
Christiane Daschera Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut06510;b Department of Molecular Genetics, Max Planck Institute for Biophysical Chemistry, PO Box 2841, D-3400Göttingen, Germany
,
Hans Dieter Schmitta Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut06510;b Department of Molecular Genetics, Max Planck Institute for Biophysical Chemistry, PO Box 2841, D-3400Göttingen, Germany
&
Dieter Galiwitza Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut06510;b Department of Molecular Genetics, Max Planck Institute for Biophysical Chemistry, PO Box 2841, D-3400Göttingen, Germany
 show all
Pages 3663-3664 | Published online: 01 Apr 2023

REFERENCES

  • Bacon, R. A., A. Salminen, H. Ruohola, P. Novick, and S. Ferro-Novick. 1989. The GTP-binding protein, Yptl, is required for transport in vitro: the Golgi apparatus is defective in ypt1 mutants. J. Cell Biol. 109:1015–1022.
  • Carlson, M., and D. Botstein. 1982. Two differentially regulated mRNAs with different 5′ ends encode secreted and intracellular forms of yeast invertase. Cell 28:145–154.
  • Dascher, C., R. Ossig, D. Gallwitz, and H. D. Schmitt. 1991. Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily. Mol. Cell. Biol. 11:872–885.
  • Gallwitz, D., C. Donath, and C. Sander. 1983. A yeast gene encoding a protein homologous to the human c-has/bas protooncogene product. Nature (London) 306:704–707.
  • Newman, A. P. 1991. The role of the yeast BET and BOS genes in transport between the ER and the Golgi complex. Ph.D. thesis, Yale University, New Haven, Conn.
  • Newman, A. P., and S. Ferro-Novick. 1987. Characterization of new mutants in the early part of the yeast secretory pathway isolated by a 3H-mannose suicide selection. J. Cell Biol. 105:1587–1594.
  • Newman, A. P., J. Shim, and S. Ferro-Novick. 1990. BET1, BOS1, and SEC22 are members of a group of interacting yeast genes required for transport from the endoplasmic reticulum to the Golgi complex. Mol. Cell. Biol. 10:3405–3414.
  • Novick, P., C. Fields, and R. Schekman. 1980. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway. Cell 21:205–215.
  • Ossig, R., C. Dascher, H.-H. Trepte, H. D. Schmitt, and D. Gallwitz. 1991. The yeast SLY gene products, suppressors of defects in the essential GTP-binding Yptl protein, may act in endoplasmic reticulum-to-Golgi transport. Mol. Cell. Biol. 11:2980–2993.
  • Schmitt, H. D., M. Puzicha, and D. Gallwitz. 1988. Study of a temperature-sensitive mutant of the ras-related YPT1 gene product in yeast suggests a role in the regulation of intracellular calcium. Cell 53:635–647.
  • Segev, N., J. Mulholland, and D. Botstein. 1988. The yeast GTP-binding Ypt1 protein and a mammalian counterpart are associated with the secretion machinery. Cell 52:915–924.
  • Struhl, K., D. Stinchcomb, S. Scherer, and R. Davis. 1979. High frequency transformation of yeast: autonomous replication of hybrid DNA molecules. Proc. Natl. Acad. Sci. USA 76:1035–1039.

REFERENCES

  • Dascher, C., R. Ossig, D. Galiwitz, and H. D. Schmitt. 1991. Identification and structure of four yeast genes (SLY) that are able to suppress the functional loss of YPT1, a member of the RAS superfamily. Mol. Cell. Biol. 11:872–885.
  • Ossig, R., C. Dascher, H.-H. Trepte, H. D. Schmitt, and D. Galiwitz. 1991. The yeast SLY gene products, suppressors of defects in the essential GTP-binding Ypt1 protein, may act in endoplasmic reticulum-to-Golgi transport. Mol. Cell. Biol. 11:2980–2993.

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