Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and endocytosis

被引：383
作者：
Itoh, T
Koshiba, S
Kigawa, T
Kikuchi, A
Yokoyama, S
Takenawa, T
机构：
[1] Univ Tokyo, Inst Med Sci, Dept Biochem, Minato Ku, Tokyo 1088639, Japan
[2] RIKEN, Genom Sci Ctr, Tsurumi Ku, Yokohama, Kanagawa 2300045, Japan
[3] RIKEN, Harima Inst SPring 8, Cellular Signaling Lab, Sayo, Hyogo 6795148, Japan
[4] Hiroshima Univ, Sch Med, Dept Biochem, Minami Ku, Hiroshima 7348551, Japan
[5] Univ Tokyo, Grad Sch Sci, Dept Biophys & Biochem, Bunkyo Ku, Tokyo 1130033, Japan
来源：
SCIENCE | 2001年 / 291卷 / 5506期
关键词：
D O I：
10.1126/science.291.5506.1047
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
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)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 Ptdlns(4,5)P-2 is essential for endocytosis mediated by clathrin-coated pits.
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页码：1047 / 1051
页数：5
相关论文
共 28 条
[1]  
BRUNGER AT, 1993, XPLOR VERSION 3 1 SY
[2]   Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis [J].
Chen, H ;
Fre, S ;
Slepnev, VI ;
Capua, MR ;
Takei, K ;
Butler, MH ;
Di Fiore, PP ;
De Camilli, P .
NATURE, 1998, 394 (6695) :793-797
[3]   Essential role of phosphoinositide metabolism in synaptic vesicle recycling [J].
Cremona, O ;
Di Paolo, G ;
Wenk, MR ;
Lüthi, A ;
Kim, WT ;
Takei, K ;
Daniell, L ;
Nemoto, Y ;
Shears, SB ;
Flavell, RA ;
McCormick, DA ;
De Camilli, P .
CELL, 1999, 99 (02) :179-188
[4]   Synaptic vesicle endocytosis [J].
Cremona, O ;
DeCamilli, P .
CURRENT OPINION IN NEUROBIOLOGY, 1997, 7 (03) :323-330
[5]   Phosphoinositides as regulators in membrane traffic [J].
DeCamilli, P ;
Emr, SD ;
McPherson, PS ;
Novick, P .
SCIENCE, 1996, 271 (5255) :1533-1539
[6]   NMRPIPE - A MULTIDIMENSIONAL SPECTRAL PROCESSING SYSTEM BASED ON UNIX PIPES [J].
DELAGLIO, F ;
GRZESIEK, S ;
VUISTER, GW ;
ZHU, G ;
PFEIFER, J ;
BAX, A .
JOURNAL OF BIOMOLECULAR NMR, 1995, 6 (03) :277-293
[7]   Epsin binds to clathrin by associating directly with the clathrin-terminal domain - Evidence for cooperative binding through two discrete sites [J].
Drake, MT ;
Downs, MA ;
Traub, LM .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (09) :6479-6489
[8]   An actin-binding protein of the Sla2/Huntingtin interacting protein 1 family is a novel component of clathrin-coated pits and vesicles [J].
Engqvist-Goldstein, ÅEY ;
Kessels, MM ;
Chopra, VS ;
Hayden, MR ;
Drubin, DG .
JOURNAL OF CELL BIOLOGY, 1999, 147 (07) :1503-1518
[9]   THE MIDAS DISPLAY SYSTEM [J].
FERRIN, TE ;
HUANG, CC ;
JARVIS, LE ;
LANGRIDGE, R .
JOURNAL OF MOLECULAR GRAPHICS, 1988, 6 (01) :13-&
[10]   Direct interaction of the 170 kDa isoform of synaptojanin 1 with clathrin and with the clathrin adaptor AP-2 [J].
Haffner, C ;
Di Paolo, G ;
Rosenthal, JA ;
De Camilli, P .
CURRENT BIOLOGY, 2000, 10 (08) :471-474
123