The role of glycosylphosphatidylinositol phospholipase C in membrane trafficking in Trypanosoma brucei

被引:0
|
作者
Garrison, Paige [1 ,2 ]
Umaer, Khan [1 ,3 ]
Bangs, James D. [1 ]
机构
[1] Univ Buffalo, Jacobs Sch Med & Biomed Sci, Dept Microbiol & Immunol, Buffalo, NY 14214 USA
[2] Pharmaceut Prod Dev, Wilmington, NC USA
[3] Eurofins, Spring House, PA USA
关键词
Trypanosome; Variant surface glycoprotein; Glycosylphosphatidylinositol; Glycosylphosphatidylinositol-specific; phospholipase C; Transferrin receptor; VARIANT SURFACE GLYCOPROTEINS; BLOOD-STREAM; ESCRT MACHINERY; EXPRESSION; FORM; DIFFERENTIATION; PURIFICATION; RECEPTOR; RELEASE; COMPLEX;
D O I
10.1016/j.molbiopara.2021.111409
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Glycosylphosphatidylinositol-phospholipase C (GPI-PLC) is an enzyme that has been implicated in GPIdependent protein trafficking and phosphoinositide metabolism in the bloodstream stage of African trypanosomes. However, despite the fact that it is associated with the cytoplasmic face of internal organellar compartments, its role in general membrane trafficking has not been investigated. Using a GPI-PLC null cell line, we determine the effect of GPI-PLC deficiency on these processes. Biosynthetic trafficking of lysosomal cargo, soluble cathepsin L and membrane bound p67, are unaffected. Likewise, secretory transport, recycling and ultimate lysosomal turnover of the GPI-anchored and transmembrane glycoproteins, transferrin receptor and invariant surface glycoprotein 65, respectively, were unaffected. A significant decrease in the endocytic uptake of transferrin was observed, confirming a prior report, but ultimate delivery to the lysosome was unimpacted. These results contribute to our understanding of the roles of this enigmatic enzyme in trypanosome cell biology.
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页数:4
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