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We examined possible contributions of GPI\u2010PLC to the response of <jats:italic>T.\u2003brucei<\/jats:italic> to hypo\u2010osmotic or mildly alkaline conditions. GPIs were detected at the endoplasmic reticulum (ER). They were cleaved after exposure of <jats:italic>T.\u2003brucei<\/jats:italic> to hypo\u2010osmolarity or mild alkalinity, which also, strikingly, caused translocation of GPI\u2010PLC from glycosomes (peroxisomes) to the ER. A catalytically inactive Gln81Leu mutant of GPI\u2010PLC failed to cleave GPIs despite being transported from glycosomes to the ER after hypo\u2010osmotic or mild alkaline treatment of the parasites. In contrast, a Cys347Ser mutant of the enzyme could not exit glycosomes after treatment of cells expressing the protein with mild base or hypo\u2010osmotic buffer. We conclude that: (a) GPI\u2010PLC contributes to loss of GPIs in <jats:italic>T.\u2003brucei<\/jats:italic> treated with hypo\u2010osmotic or mildly alkaline buffer; (b) access of GPI\u2010PLC to its substrate <jats:italic>in vivo<\/jats:italic> can be regulated post\u2010translationally; (c) translocation of GPI\u2010PLC from glycosomes to the ER is important for <jats:italic>in vivo<\/jats:italic> cleavage of GPIs; (d) Cys347 is part of a peptide motif required for post\u2010translational targeting of GPI\u2010PLC to the ER. Glycosome\u2010to\u2010ER movement of GPI\u2010PLC reveals a novel pathway for intracellular protein traffic. The physiological significance of GPI digestion in cells exposed to mildly alkalinity or hypo\u2010osmolarity is discussed.<\/jats:p>","DOI":"10.1111\/j.1742-4658.2006.05225.x","type":"journal-article","created":{"date-parts":[[2006,4,29]],"date-time":"2006-04-29T22:45:10Z","timestamp":1146350710000},"page":"2110-2126","source":"Crossref","is-referenced-by-count":13,"title":["Regulated cleavage of intracellular glycosylphosphatidylinositol in a 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