id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-289710-ucguzgdm	nan	Yeast Kex1p is a Golgi-associated membrane protein: deletions in a cytoplasmic targeting domain result in mislocalization to the vacuolar membrane	1992-12-02		.txt	text/plain	7986	376	51	In addition to soluble proteins, the cell surface appears to be the default destination for mammalian ER, Golgi, and lysosomal membrane proteins as removal of their respective retention/targeting signals results in their delivery to the plasma membrane (Machamer and Rose, 1987; Jackson et al., 1990; Williams and Fukuda, 1990) . Kexlp is predicted to be a type I transmembrane protein with a large amino-terminal protease domain in the lumen of the secretory pathway, a single membrane-spanning domain, and a smaller carboxy-terminai domain positioned cytoplasmicaUy. The observation that KEX/cells intracellularly retain Kexlp activity prompted an analysis to determine in which secretory compartment Kexlp resided, and how it achieved such retention. The above results indicated that Kexlp-Hpa was membrane associated, had received glycosyl modifications in the Golgi apparatus, gave wild-type levels of total activity, and was retained intracellularly; yet processed the K1 killer toxin precursor to a lesser extent than Kexlp.	./cache/cord-289710-ucguzgdm.txt	./txt/cord-289710-ucguzgdm.txt