The transmembrane domain of TACE regulates protein ectodomain shedding
作者： Xiaojin Li , Liliana Pérez , Zui Pan , Huizhou Fan
DOI: 10.1038/CR.2007.98
关键词:
摘要: Numerous membrane proteins are cleaved by tumor necrosis factor-α converting enzyme (TACE), which causes the release of their ectodomains. An ADAM (a disintegrin and metalloprotease domain) family member, TACE contains several noncatalytic domains whose roles in ectodomain shedding have yet to be fully resolved. Here, we explored function transmembrane domain (TM) coupling molecular engineering functional analysis. A TM-free construct that is anchored plasma a glycosylphosphatidylinositol (GPI)-binding polypeptide failed restore transforming growth (TGF-α), (TNF-α) L-selectin cells lacking endogenous activity. Substitution TM with prolactin receptor or platelet-derived factor (PDGFR) also resulted severe loss TGF-α shedding, but had no effects on cleavage TNF-α L-selectin. Replacement enabled mutants carrying PDGFR. Taken together, our observations suggest anchorage lipid bilayer through required for efficient broad spectrum substrates, amino-acid sequence may play role regulatory specificity among substrates.
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