Title: Membrane protein retention in the yeast Golgi apparatus: dipeptidyl aminopeptidase A is retained by a cytoplasmic signal containing aromatic residues Document date: 1993_6_2
ID: 0pz80zbg_5
Snippet: In this study, we have sought to test further the vacuolar default model and to analyze the Golgi retention signal of DPAP A in detail. An alternative model, in which the DPAP A transmembrane contained a cryptic vacuolar targeting signal, can be ruled out since its replacement with a synthetic hydrophobic sequence still resulted in transport of Golgi retention-defective DPAP A to the vacuole. An 8-amino acid peptide sequence within the DPAP A cyt.....
Document: In this study, we have sought to test further the vacuolar default model and to analyze the Golgi retention signal of DPAP A in detail. An alternative model, in which the DPAP A transmembrane contained a cryptic vacuolar targeting signal, can be ruled out since its replacement with a synthetic hydrophobic sequence still resulted in transport of Golgi retention-defective DPAP A to the vacuole. An 8-amino acid peptide sequence within the DPAP A cytoplasmic domain containing a Phe-X-Phe-X-Asp motif was absolutely required for efficient Golgi retention. A 10-amino acid sequence containing the Phe and Asp residues was found to be sufficient for retention of a vacuolar membrane protein in the yeast Golgi.
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