A broadly active fucosyltransferase LmjFUT1 whose mitochondrial localization and catalytic activity is essential in the parasitic protozoan Leishmania
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References
Modification of epidermal growth factor-like repeats with O-fucose. Molecular cloning and expression of a novel GDP-fucose protein O-fucosyltransferase.
Global distribution maps of the leishmaniases
Mitochondrial and nucleocytoplasmic isoforms of O-linked GlcNAc transferase encoded by a single mammalian gene.
The role of phosphoglycans in Leishmania–sand fly interactions
Increased enzymatic O-GlcNAcylation of mitochondrial proteins impairs mitochondrial function in cardiac myocytes exposed to high glucose.
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Frequently Asked Questions (2)
Q2. What have the authors stated for future works in "A broadly active fucosyltransferase lmjfut1 whose mitochondrial localization and catalytic activity is essential in the parasitic protozoan leishmania" ?
Future studies will address this possibility. Future studies will be necessary to resolve the nature of the GDP-Fucose and FUT1dependent product ( s ) in trypanosomatids, which genetic and biochemical data strongly predict must nonetheless exist. Potentially, trypanosomatid mitochondrial FUT1s may offer a facile system in the future for probing mitochondrial glycosylation in a setting uncomplicated by multiple isoforms targeted to diverse compartments, and its essentiality renders it an attractive target for chemotherapy of trypanosomatid parasites. L. donovani expresses a mannose-fucose conjugate whose structure has not been definitively established ( 33 ), and several L. donovani proteins exhibited MS/MS signatures suggestive of fucosylation ( 34 ).