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Endocytic proteins such as epsin, AP180, and Hip1R (Sla2p) share a
conserved modular region termed the epsin NH2-terminalhomology (ENTH) domain, which plays a crucial role in clathrin-mediatedendocytosis through an unknown target. Here, we demonstrate astrong
affinity of the ENTH domain for phosphatidylinositol-4,5-bisphosphate[PtdIns(4,5)P2]. With nuclear magnetic resonance analysis
of theepsin ENTH domain, we determined that a cleft formed with
positivelycharged residues contributed to phosphoinositide binding.
Overexpressionof a mutant, epsin Lys76 Ala76, with an ENTH domain defective in phosphoinositide
binding, blockedepidermal growth factor internalization in COS-7
cells. Thus,interaction between the ENTH domain and
PtdIns(4,5)P2 is essentialfor endocytosis mediated by
clathrin-coated pits.
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.
*
To whom correspondence should be addressed. E-mail:
takenawa{at}ims.u-tokyo.ac.jp
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REPORTS
Marijn G. J. Ford, Barbara M. F. Pearse, Matthew K. Higgins, Yvonne Vallis, David J. Owen, Adele Gibson, Colin R. Hopkins, Philip R. Evans, and Harvey T. McMahon (9 February 2001) Science291 (5506), 1051.
[DOI: 10.1126/science.291.5506.1051] |Abstract »|Full Text »|PDF »
PERSPECTIVES
David J. Gillooly and Harald Stenmark (9 February 2001) Science291 (5506), 993.
[DOI: 10.1126/science.291.5506.993] |Summary »|Full Text »
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A. E.Y. Engqvist-Goldstein, R. A. Warren, M. M. Kessels, J. H. Keen, J. Heuser, and D. G. Drubin (2001)
J. Cell Biol.
154, 1209-1224
|Abstract »|Full Text »|PDF »
Modulation of HIV-like particle assembly in vitro by inositol phosphates.
S. Campbell, R. J. Fisher, E. M. Towler, S. Fox, H. J. Issaq, T. Wolfe, L. R. Phillips, and A. Rein (2001)
PNAS
|Abstract »|Full Text »|PDF »
The huntingtin interacting protein HIP1 is a clathrin and {alpha}-adaptin-binding protein involved in receptor-mediated endocytosis.
S. Waelter, E. Scherzinger, R. Hasenbank, E. Nordhoff, R. Lurz, H. Goehler, C. Gauss, K. Sathasivam, G. P. Bates, H. Lehrach, et al. (2001)
Hum. Mol. Genet.
10, 1807-1817
|Abstract »|Full Text »|PDF »
Signaling with Phosphoinositides: Better than Binary.
M. Overduin, M. L. Cheever, and T. G. Kutateladze (2001)
Mol. Interv.
1, 150-159
|Abstract »|Full Text »|PDF »
Regulation of presynaptic phosphatidylinositol 4,5-biphosphate by neuronal activity.
K. D. Micheva, R. W. Holz, and S. J. Smith (2001)
J. Cell Biol.
154, 355-368
|Abstract »|Full Text »|PDF »
Phosphoinositides in membrane traffic at the synapse.
O Cremona and P De Camilli (2001)
J. Cell Sci.
114, 1041-1052
|Abstract »|PDF »
Golgi-localizing, gamma -Adaptin Ear Homology Domain, ADP-ribosylation Factor-binding (GGA) Proteins Interact with Acidic Dileucine Sequences within the Cytoplasmic Domains of Sorting Receptors through Their Vps27p/Hrs/STAM (VHS) Domains.
H. Takatsu, Y. Katoh, Y. Shiba, and K. Nakayama (2001)
J. Biol. Chem.
276, 28541-28545
|Abstract »|Full Text »|PDF »
Interaction of Two Structurally Distinct Sequence Types with the Clathrin Terminal Domain beta -Propeller.
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
PtdIns(4,5)P2 is essential for endocytosis mediated by
clathrin-coated pits.
