PMID- 10557078
OWN - NLM
STAT- MEDLINE
DCOM- 19991210
LR  - 20111117
IS  - 0950-9232 (Print)
IS  - 0950-9232 (Linking)
VI  - 18
IP  - 43
DP  - 1999 Oct 21
TI  - Epsin binds to the EH domain of POB1 and regulates receptor-mediated endocytosis.
PG  - 5915-22
AB  - POB1 has been identified as a RalBP1-binding protein and has the Eps15 homology
      (EH) domain. The EH domain-containing proteins have been suggested to be involved
      in clathrin-dependent endocytosis. To clarify the function of POB1, we purified a
      protein which binds to the EH domain of POB1 from bovine brain cytosol and
      identified it as Epsin, which is known to bind to the EH domain of Eps15. Epsin
      has three Asn-Pro-Phe (NPF) motifs in the C-terminal region, which are known to
      form the core sequence for the binding to the EH domain. The EH domain of POB1
      interacted directly with the region containing the NPF motifs of Epsin.
      Expression of Epsin in CHO-IR cells inhibited internalization of insulin although
      it affected neither insulin-binding nor autophosphorylation activities of the
      insulin receptor. Taken together with the observations that Epsin is involved in 
      internalization of the receptors for epidermal growth factor and transferrin,
      these results suggest that Epsin is a binding partner of POB1 and their binding
      regulates receptor-mediated endocytosis.
FAU - Morinaka, K
AU  - Morinaka K
AD  - Department of Biochemistry, Hiroshima University School of Medicine, 1-2-3
      Kasumi, Minami-ku, Hiroshima 734-8551, Japan.
FAU - Koyama, S
AU  - Koyama S
FAU - Nakashima, S
AU  - Nakashima S
FAU - Hinoi, T
AU  - Hinoi T
FAU - Okawa, K
AU  - Okawa K
FAU - Iwamatsu, A
AU  - Iwamatsu A
FAU - Kikuchi, A
AU  - Kikuchi A
LA  - eng
SI  - GENBANK/AF073727
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - England
TA  - Oncogene
JT  - Oncogene
JID - 8711562
RN  - 0 (Adaptor Proteins, Vesicular Transport)
RN  - 0 (Carrier Proteins)
RN  - 0 (DNA, Complementary)
RN  - 0 (Insulin)
RN  - 0 (Intracellular Signaling Peptides and Proteins)
RN  - 0 (Neuropeptides)
RN  - 0 (Phosphoproteins)
RN  - 0 (REPS2 protein, human)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Vesicular Transport Proteins)
RN  - 0 (epsin)
SB  - IM
MH  - Adaptor Proteins, Vesicular Transport
MH  - Amino Acid Sequence
MH  - Animals
MH  - Base Sequence
MH  - Binding Sites
MH  - CHO Cells
MH  - COS Cells
MH  - Carrier Proteins/genetics/isolation & purification/*metabolism
MH  - Cattle
MH  - Cloning, Molecular
MH  - Cricetinae
MH  - DNA, Complementary
MH  - *Endocytosis
MH  - Humans
MH  - Insulin/metabolism
MH  - *Intracellular Signaling Peptides and Proteins
MH  - Molecular Sequence Data
MH  - Neuropeptides/genetics/isolation & purification/*metabolism
MH  - Phosphoproteins/*metabolism
MH  - Recombinant Fusion Proteins/metabolism
MH  - Sequence Homology, Amino Acid
MH  - *Vesicular Transport Proteins
EDAT- 1999/11/11 00:00
MHDA- 1999/11/11 00:01
CRDT- 1999/11/11 00:00
PHST- 1999/11/11 00:00 [pubmed]
PHST- 1999/11/11 00:01 [medline]
PHST- 1999/11/11 00:00 [entrez]
AID - 10.1038/sj.onc.1202974 [doi]
PST - ppublish
SO  - Oncogene. 1999 Oct 21;18(43):5915-22. doi: 10.1038/sj.onc.1202974.