IndraLab

Statements


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sparser
"In the present study, it was found that CD63 and its mutant efficiently interact with CXCR4 in live cells and that CD63-induced downregulation and interaction are significantly abrogated by the N-linked glycosylation inhibitor, TM."

sparser
"Either CD63 or CD63DeltaN formed a complex with CXCR4 at the Golgi apparatus and the late endosomes, while CD63 GD mutants lost the ability to form a complex with CXCR4 exclusively at the Golgi apparatus."

sparser
"These findings suggest that CD63 interacts with CXCR4 through the N-linked glycans-portion of the CD63 protein and that the complex induces direction of CXCR4 trafficking to the endosomes/lysosomes, rather than to the plasma membrane."

sparser
"Several studies have evidenced that CXCR4 interacts with CD63, and that N-terminal deletion mutations occurring in CD63 blocks virus entry by inducing a reduction in CXCR4 expression [ 19 , 52 ]."

reach
"Indeed, Yoshida et al. showed that CD63 had three N linked glycosylation sites [XREF_BIBR], that CD63 interacts with CXCR4 through the N linked glycans-portion of the CD63 protein and that the complex induces the direction of CXCR4 trafficking to the endosomes and lysosomes, rather than to the plasma membrane."

sparser
"To our knowledge, inhibition of tetraspanin-partner interactions by glycosylation has not been reported before, as other studies either found no effect, like RDS-ROM1 ( xref ), or increased binding upon glycosylation, like CD63-CXCR4 ( xref ) and CD82-integrin α5β1 ( xref )."

sparser
"For instance, the tetraspanin CD63 interacts with CXCR4 on activated B cells and downregulates this receptor ( xref )."

sparser
"Indeed, Yoshida et al. showed that CD63 had three N-linked glycosylation sites [ xref ], that CD63 interacts with CXCR4 through the N-linked glycans-portion of the CD63 protein and that the complex induces the direction of CXCR4 trafficking to the endosomes/lysosomes, rather than to the plasma membrane."

reach
"Either CD63 or CD63DeltaN formed a complex with CXCR4 at the Golgi apparatus and the late endosomes, while CD63 GD mutants lost the ability to form a complex with CXCR4 exclusively at the Golgi apparatus."

reach
"These findings suggest that CD63 interacts with CXCR4 through the N linked glycans-portion of the CD63 protein and that the complex induces direction of CXCR4 trafficking to the endosomes and lysosomes, rather than to the plasma membrane."