PMID- 11161217
OWN - NLM
STAT- MEDLINE
DCOM- 20010322
LR  - 20191210
IS  - 0036-8075 (Print)
IS  - 0036-8075 (Linking)
VI  - 291
IP  - 5506
DP  - 2001 Feb 9
TI  - Role of the ENTH domain in phosphatidylinositol-4,5-bisphosphate binding and 
      endocytosis.
PG  - 1047-51
AB  - 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 [PtdIns(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. 
      Overexpression 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 PtdIns(4,5)P2 is 
      essential for endocytosis mediated by clathrin-coated pits.
FAU - Itoh, T
AU  - Itoh T
AD  - Department of Biochemistry, Institute of Medical Science, University of Tokyo, 
      4-6-1 Shirokanedai, Minato-ku, Tokyo 108-8639, Japan.
FAU - Koshiba, S
AU  - Koshiba S
FAU - Kigawa, T
AU  - Kigawa T
FAU - Kikuchi, A
AU  - Kikuchi A
FAU - Yokoyama, S
AU  - Yokoyama S
FAU - Takenawa, T
AU  - Takenawa T
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Science
JT  - Science (New York, N.Y.)
JID - 0404511
RN  - 0 (Adaptor Proteins, Vesicular Transport)
RN  - 0 (Carrier Proteins)
RN  - 0 (Clathrin)
RN  - 0 (DNA-Binding Proteins)
RN  - 0 (Inositol Phosphates)
RN  - 0 (Liposomes)
RN  - 0 (Neuropeptides)
RN  - 0 (Phosphatidylinositol 4,5-Diphosphate)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Transcription Factors)
RN  - 0 (Vesicular Transport Proteins)
RN  - 0 (epsin)
RN  - 62229-50-9 (Epidermal Growth Factor)
SB  - IM
CIN - Science. 2001 Feb 9;291(5506):993-4. PMID: 11232585
MH  - Adaptor Proteins, Vesicular Transport
MH  - Amino Acid Motifs
MH  - Amino Acid Substitution
MH  - Animals
MH  - COS Cells
MH  - Carrier Proteins/*chemistry/*metabolism
MH  - Chlorocebus aethiops
MH  - Clathrin/metabolism
MH  - Coated Pits, Cell-Membrane/metabolism
MH  - DNA-Binding Proteins/metabolism
MH  - *Endocytosis
MH  - Epidermal Growth Factor/metabolism
MH  - Inositol Phosphates/metabolism
MH  - Liposomes/metabolism
MH  - Models, Molecular
MH  - Neuropeptides/*chemistry/*metabolism
MH  - Nuclear Magnetic Resonance, Biomolecular
MH  - Phosphatidylinositol 4,5-Diphosphate/*metabolism
MH  - Protein Conformation
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Recombinant Fusion Proteins/chemistry/metabolism
MH  - Transcription Factors/metabolism
MH  - *Vesicular Transport Proteins
MH  - Zinc Fingers
EDAT- 2001/02/13 11:00
MHDA- 2001/03/27 10:01
CRDT- 2001/02/13 11:00
PHST- 2001/02/13 11:00 [pubmed]
PHST- 2001/03/27 10:01 [medline]
PHST- 2001/02/13 11:00 [entrez]
AID - 291/5506/1047 [pii]
AID - 10.1126/science.291.5506.1047 [doi]
PST - ppublish
SO  - Science. 2001 Feb 9;291(5506):1047-51. doi: 10.1126/science.291.5506.1047.