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Nucleation of COPII vesicular coat complex by endoplasmic reticulum to Golgi vesicle SNAREs.

Protein trafficking from the endoplasmic reticulum (ER) to the Golgi apparatus involves specific uptake into coat protein complex II (COPII)-coated vesicles of secretory and of vesicle targeting (v-SNARE) proteins. Here, two ER to Golgi v-SNAREs, Bet1p and Bos1p, were shown to interact specifically with Sar1p, Sec23p, and Sec24p, components of the COPII coat, in a guanine nucleotide-dependent fashion. Other v-SNAREs, Sec22p and Ykt6p, might interact more weakly with the COPII coat or interact indirectly by binding to Bet1p or Bos1p. The data suggest that transmembrane proteins can be taken up into COPII vesicles by direct interactions with the coat proteins and may play a structural role in the assembly of the COPII coat complex.

Pubmed ID: 9685263

Authors

  • Springer S
  • Schekman R

Journal

Science (New York, N.Y.)

Publication Data

July 31, 1998

Associated Grants

None

Mesh Terms

  • Binding Sites
  • COP-Coated Vesicles
  • Carrier Proteins
  • Endoplasmic Reticulum
  • Fungal Proteins
  • GTP Phosphohydrolases
  • GTP-Binding Proteins
  • GTPase-Activating Proteins
  • Golgi Apparatus
  • Guanosine Diphosphate
  • Guanosine Triphosphate
  • Guanylyl Imidodiphosphate
  • Membrane Proteins
  • Membrane Transport Proteins
  • Monomeric GTP-Binding Proteins
  • Qb-SNARE Proteins
  • Qc-SNARE Proteins
  • R-SNARE Proteins
  • Receptors, Cell Surface
  • Recombinant Fusion Proteins
  • SNARE Proteins
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Vesicular Transport Proteins