Title : Specific
isoforms of the resident endoplasmic reticulum protein
glucosidase II associate with the
CD45 protein-
tyrosine phosphatase via a lectin-like interaction
Abstract :
- We have previously demonstrated that CD45 physically associates with the endoplasmic reticulum processing enzyme glucosidase II ( GII )
- GII consists of the catalytic alpha-chain chain and an associated beta- chain
- To gain insight into the basis of the association between CD45 and GII , we examined the biochemical requirements for the interaction
- We show that the alpha- subunit is essential for the interaction
- Interestingly, only a higher molecular weight form of GIIalpha is capable of associating with CD45 in a competitive situation where multiple GIIalpha isoforms are expressed
- Further, transfection studies demonstrate that only isoforms containing the alternatively spliced sequence Box A1 are capable of binding CD45 , although all isoforms are catalytically active
- The interaction between CD45 and GII is dependent on the active site of GII , is mediated through the carbohydrate on CD45 , and can be inhibited with mannose.
- Taken together, these results suggest that GIIalpha acts as a lectin and binds to CD45 in an exon-dependent manner
- This lectin activity of GII may be a novel mechanism for the regulation of CD45 biology and play a role in immune function, possibly by regulating CD45 glycosylation