PMID- 10567358
OWN - NLM
STAT- MEDLINE
DCOM- 19991229
LR  - 20190508
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 274
IP  - 48
DP  - 1999 Nov 26
TI  - The epsins define a family of proteins that interact with components of the
      clathrin coat and contain a new protein module.
PG  - 33959-65
AB  - Epsin (epsin 1) is an interacting partner for the EH domain-containing region of 
      Eps15 and has been implicated in conjunction with Eps15 in clathrin-mediated
      endocytosis. We report here the characterization of a similar protein (epsin 2), 
      which we have cloned from human and rat brain libraries. Epsin 1 and 2 are most
      similar in their NH(2)-terminal region, which represents a module (epsin NH(2)
      terminal homology domain, ENTH domain) found in a variety of other proteins of
      the data base. The multiple DPW motifs, typical of the central region of epsin 1,
      are only partially conserved in epsin 2. Both proteins, however, interact through
      this central region with the clathrin adaptor AP-2. In addition, we show here
      that both epsin 1 and 2 interact with clathrin. The three NPF motifs of the
      COOH-terminal region of epsin 1 are conserved in the corresponding region of
      epsin 2, consistent with the binding of both proteins to Eps15. Epsin 2, like
      epsin 1, is enriched in brain, is present in a brain-derived clathrin-coated
      vesicle fraction, is concentrated in the peri-Golgi region and at the cell
      periphery of transfected cells, and partially colocalizes with clathrin. High
      overexpression of green fluorescent protein-epsin 2 mislocalizes components of
      the clathrin coat and inhibits clathrin-mediated endocytosis. The epsins define a
      new protein family implicated in membrane dynamics at the cell surface.
FAU - Rosenthal, J A
AU  - Rosenthal JA
AD  - Howard Hughes Medical Institute and Department of Cell Biology, Yale University
      School of Medicine, New Haven, Connecticut 06510, USA.
FAU - Chen, H
AU  - Chen H
FAU - Slepnev, V I
AU  - Slepnev VI
FAU - Pellegrini, L
AU  - Pellegrini L
FAU - Salcini, A E
AU  - Salcini AE
FAU - Di Fiore, P P
AU  - Di Fiore PP
FAU - De Camilli, P
AU  - De Camilli P
LA  - eng
SI  - GENBANK/AF062084
SI  - GENBANK/AF062085
GR  - CA46128/CA/NCI NIH HHS/United States
GR  - NS1024-01/NS/NINDS NIH HHS/United States
GR  - NS36251/NS/NINDS NIH HHS/United States
GR  - etc.
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - J Biol Chem
JT  - The Journal of biological chemistry
JID - 2985121R
RN  - 0 (Adaptor Protein Complex alpha Subunits)
RN  - 0 (Adaptor Proteins, Signal Transducing)
RN  - 0 (Adaptor Proteins, Vesicular Transport)
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Clathrin)
RN  - 0 (DNA, Complementary)
RN  - 0 (EPN2 protein, human)
RN  - 0 (EPS15 protein, human)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Membrane Proteins)
RN  - 0 (Neuropeptides)
RN  - 0 (Phosphoproteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Vesicular Transport Proteins)
RN  - 0 (epsin)
RN  - EC 1.13.12.- (Luciferases)
SB  - IM
MH  - Adaptor Protein Complex alpha Subunits
MH  - Adaptor Proteins, Signal Transducing
MH  - Adaptor Proteins, Vesicular Transport
MH  - Amino Acid Sequence
MH  - Animals
MH  - CHO Cells
MH  - Calcium-Binding Proteins/metabolism
MH  - Carrier Proteins/chemistry/*genetics/metabolism
MH  - Clathrin/*metabolism
MH  - Coated Vesicles/metabolism
MH  - Cricetinae
MH  - DNA, Complementary/chemistry/genetics
MH  - Fluorescent Antibody Technique
MH  - Gene Expression
MH  - Humans
MH  - Intracellular Signaling Peptides and Proteins
MH  - Luciferases/genetics/metabolism
MH  - Male
MH  - Membrane Proteins/metabolism
MH  - Molecular Sequence Data
MH  - Neuropeptides/chemistry/*genetics/metabolism
MH  - Phosphoproteins/metabolism
MH  - Phylogeny
MH  - Protein Binding
MH  - Protein Structure, Tertiary
MH  - Rats
MH  - Recombinant Fusion Proteins/genetics/metabolism
MH  - Sequence Alignment
MH  - Sequence Analysis, DNA
MH  - Sequence Homology, Amino Acid
MH  - Tissue Distribution
MH  - *Vesicular Transport Proteins
EDAT- 1999/11/24 00:00
MHDA- 1999/11/24 00:01
CRDT- 1999/11/24 00:00
PHST- 1999/11/24 00:00 [pubmed]
PHST- 1999/11/24 00:01 [medline]
PHST- 1999/11/24 00:00 [entrez]
AID - 10.1074/jbc.274.48.33959 [doi]
PST - ppublish
SO  - J Biol Chem. 1999 Nov 26;274(48):33959-65. doi: 10.1074/jbc.274.48.33959.