Role of the ENTH Domain in Phosphatidylinositol-4,5-Bisphosphate Binding and Endocytosis
摘要：
Endocytic proteins such as epsin, AP180, and Hip1R (Sla2p) share a conserved modular region termed the epsin NH2-terminal homology (ENTH) domain, which plays a crucial role in clathrin-mediated endocytosis through an unknown target. Here, we demonstrate a strong affinity of the ENTH domain for phosphatidylinositol-4,5-bisphosphate [Ptdlns(4,5)P2]. With nuclear magnetic resonance analysis of the epsin ENTH domain, we determined that a cleft formed with positively charged residues contributed to phosphoinositide binding. Over-expression of a mutant, epsin Lys76→ Ala76, with an ENTH domain defective in phosphoinositide binding, blocked epidermal growth factor internalization in COS-7 cells. Thus, interaction between the ENTH domain and Ptdlns(4,5)P2is essential for endocytosis mediated by clathrin-coated pits.
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关键词：
Animals Cercopithecus aethiops COS Cells Coated Pits, Cell-Membrane Neuropeptides Transcription Factors DNA-Binding Proteins Recombinant Fusion Proteins Vesicular Transport Proteins Adaptor Proteins, Vesicular Transport
DOI：
10.1126/science.291.5506.1047
被引量：
年份：
2001
万方医学
Semantic Scholar
dx.doi.org
Europe PMC
NCBI
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