id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-329515-ra20actc	nan	Retention of p63 in an ER-Golgi intermediate compartment depends on the presence of all three of its domains and on its ability to form oligomers	1994-07-01		.txt	text/plain	9067	464	54	Recently, oligomerization of a chimeric protein containing the first membrane-spanning domain of the M glycoprotein of avian coronavirus has been correlated to its retention in the Golgi apparatus (Weisz et al., 1993) . When COS cells transfected with this mutant were permeabilized, the predominant staining pattern was characteristic for the ER and the Golgi apparatus indicating that/,16-101,6-12A had lost p63wt localization (Fig. 6 c) . To further analyze the role of the cytoplasmic tail of p63 in retention and to determine whether the transmembrane and lumenal domains of this protein contribute to proper intracellular localization, we substituted each of these domains with the corresponding domains of the cell surface protein human DPPIV (Fig. 9) . A similar result was obtained with a construct that only contained the lumenal domain of p63 (DDP; DPPIV cytoplasmic; DPPIV transmembrane, p63 lumenal; Fig. 9 ) except that most of the ER staining was now replaced by cell surface expression (data not shown).	./cache/cord-329515-ra20actc.txt	./txt/cord-329515-ra20actc.txt