Role of the ENTH Domain in Phosphatidylinositol-4,5-Bisphosphate Binding and Endocytosis-Reference-Cited by-同舟云学术

Role of the ENTH Domain in Phosphatidylinositol-4,5-Bisphosphate Binding and Endocytosis

Published:2001-02-09 Issue:5506 Volume:291 Page:1047-1051
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Itoh Toshiki¹,Koshiba Seizo²,Kigawa Takanori²³,Kikuchi Akira⁴,Yokoyama Shigeyuki²³⁵,Takenawa Tadaomi¹

Affiliation:

1. Department of Biochemistry, Institute of Medical Science, University of Tokyo, 4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.

2. RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama-shi, Kanagawa 230-0045, Japan.

3. Cellular Signaling Laboratory, RIKEN Harima Institute at SPring-8, 1-1-1 Kouto, Mikazuki-cho, Sayo, Hyogo 679-5148, Japan.

4. Department of Biochemistry, Hiroshima University School of Medicine, 1-2-3 Kasumi, Minami-ku, Hiroshima 734–8551, Japan.

5. Department of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan.

Abstract

Endocytic proteins such as epsin, AP180, and Hip1R (Sla2p) share a conserved modular region termed the epsin NH 2 -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 [PtdIns(4,5)P 2 ]. With nuclear magnetic resonance analysis of the epsin ENTH domain, we determined that a cleft formed with positively charged residues contributed to phosphoinositide binding. Overexpression of a mutant, epsin Lys 76 → Ala 76 , with an ENTH domain defective in phosphoinositide binding, blocked epidermal growth factor internalization in COS-7 cells. Thus, interaction between the ENTH domain and PtdIns(4,5)P 2 is essential for endocytosis mediated by clathrin-coated pits.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

Reference38 articles.

1. Identification of a novel domain shared by putative components of the endocytic and cytoskeletal machinery

2. Chen H., et al., Nature 394, 793 (1998).

3. Yeast epsins contain an essential N-terminal ENTH domain, bind clathrin and are required for endocytosis

4. Engqvist-Goldstein A. E., Kessels M. M., Chopra V. S., Hayden M. R., Drubin D. G., J. Cell Biol. 147, 1503 (1999).

5. O. Cremona

Cited by 415 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Linking phosphoinositide function to mitosis;Cell Reports;2024-06

2. Subtleties in Clathrin Heavy Chain Binding Boxes provide selectivity among Adaptor Proteins of Budding Yeast;2024-05-31

3. PMIpred: a physics-informed web server for quantitative protein–membrane interaction prediction;Bioinformatics;2024-02-01

4. PRL1 and PRL3 promote macropinocytosis via its lipid phosphatase activity;Theranostics;2024

5. Nuclear Phosphoinositides as Key Determinants of Nuclear Functions;Biomolecules;2023-06-28