Selected article for: "cell surface and secretory pathway"

Title: Yeast Kex1p is a Golgi-associated membrane protein: deletions in a cytoplasmic targeting domain result in mislocalization to the vacuolar membrane
  • Document date: 1992_12_2
  • ID: ucguzgdm_2
    Snippet: Proteins that enter the secretory pathway are thought to be transported to the cell surface by default via a "bulk flow" mechanism unless they contain additional targeting information (Pfeffer and Rothman, 1987; Rothman, 1987; Wieland et al., 1987; Karrenbauer et al., 1990) . Such targeting information is found in soluble proteins resident in the ER which maintain their localization by containing a retention signal at their carboxy termini (Munro.....
    Document: Proteins that enter the secretory pathway are thought to be transported to the cell surface by default via a "bulk flow" mechanism unless they contain additional targeting information (Pfeffer and Rothman, 1987; Rothman, 1987; Wieland et al., 1987; Karrenbauer et al., 1990) . Such targeting information is found in soluble proteins resident in the ER which maintain their localization by containing a retention signal at their carboxy termini (Munro and Pelham, 1987; Pelham et al., 1988) . Deletion of the retention signal results in secretion of the soluble ER resident proteins to the cell surface. Soluble proteins destined for the mammalian lysosome re-A. Cooper's present address is the Institute of Molecular Biology, University of Oregon, Eugene, OR 97403.

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