Luminal/extracellular domains of chimeric CI-M6PR-C proteins interfere with their retrograde endosome-to-TGN trafficking in the transient expression system.

ABSTRACT: The membrane trafficking of cation-independent mannose 6-phosphate receptor (CI-M6PR) between the trans-Golgi network (TGN) and endosomal compartments is not only critical for maintaining lysosomal function but also a well-known event for understanding molecular and cellular mechanisms in retrograde endosome-to-TGN trafficking. Although it has been well established in literature that the C-terminus of bovine CI-M6PR determines its retrograde trafficking, it remains unclear whether the luminal domain of the protein plays a role on these sorting events. In this study, we found that partial deletion of luminal domain of human CI-M6PR mistargeted the mutant protein to non-TGN compartments. Moreover, replacing the luminal domain of both bovine and human CI-M6PR with that from irrelevant membran

SUBMITTER: Chang F 

PROVIDER: S-EPMC6117607 | biostudies-literature | 2018 Jul

REPOSITORIES: biostudies-literature