Title : Glycosylation of tetraspanin
Tspan-1 at four distinct
sites promotes its transition through the endoplasmic reticulum
Abstract :
- We showed that Tspan-1 , a tetraspanin overexpressed in many human cancers, harbours oligosaccharides at all four potential N-glycosylation sites
- Its most abundant form contained only mannose-rich sugar chains but two distinct glycosylation sites could also contain complex carbohydrates
- Glycosylation seemed to be required for correct folding and subsequent transition through the endoplasmic reticulum
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. Glycosylation, , Tspan-1, -, sites
- 2. contain, , -, complex carbohydrates, sites
- 2. glycosylation, , -, -, sites
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):