PMID- 8617810
OWN - NLM
STAT- MEDLINE
DCOM- 19960611
LR  - 20210210
IS  - 0021-9258 (Print)
IS  - 0021-9258 (Linking)
VI  - 271
IP  - 9
DP  - 1996 Mar 1
TI  - All ErbB receptors other than the epidermal growth factor receptor are 
      endocytosis impaired.
PG  - 5251-7
AB  - Four transmembrane tyrosine kinases constitute the ErbB receptor family: the 
      epidermal growth factor (EGF) receptor, ErbB-2, ErbB-3, and ErbB-4. We have 
      measured the endocytic capacities of all four members of the EGF receptor family, 
      including ErbB-3 and ErbB-4, which have not been described previously. 
      EGF-responsive chimeric receptors containing the EGF receptor extracellular 
      domain and different ErbB cytoplasmic domains (EGFR/ErbB) have been employed. The 
      capacity of these growth factor-receptor complexes to mediate 125I-EGF 
      internalization, receptor down-regulation, receptor degradation, and receptor 
      co-immunoprecipitation with AP-2 was assayed. In contrast to the EGF receptor, 
      all EGFR/ErbB receptors show impaired ligand-induced rapid internalization, 
      down-regulation, degradation, and AP-2 association. Also, we have analyzed the 
      heregulin-responsive wild-type ErbB-4 receptor, which does not mediate the rapid 
      internalization of 125I-heregulin, demonstrates no heregulin-regulated receptor 
      degradation, and fails to form association complexes with AP-2. Despite the 
      substantial differences in ligand-induced receptor trafficking between the EGF 
      and ErbB-4 receptors, EGF and heregulin have equivalent capacities to stimulate 
      DNA synthesis in quiescent cells. These results show that the ligand-dependent 
      down-regulation mechanism of the EGF receptor, surprisingly, is not a property of 
      any other known ErbB receptor family member. Since endocytosis is thought to be 
      an attenuation mechanism for growth factor-receptor complexes, these data imply 
      that substantial differences in attenuation mechanisms exist within one family of 
      structurally related receptors.
FAU - Baulida, J
AU  - Baulida J
AD  - Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, 
      Tennessee 37232-0146, USA.
FAU - Kraus, M H
AU  - Kraus MH
FAU - Alimandi, M
AU  - Alimandi M
FAU - Di Fiore, P P
AU  - Di Fiore PP
FAU - Carpenter, G
AU  - Carpenter G
LA  - eng
GR  - CA24071/CA/NCI NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
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 (Carrier Proteins)
RN  - 0 (DNA Primers)
RN  - 0 (Glycoproteins)
RN  - 0 (Neuregulin-1)
RN  - 0 (Neuregulins)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 155646-83-6 (heregulin beta1)
RN  - 62229-50-9 (Epidermal Growth Factor)
RN  - EC 2.7.10.1 (ERBB4 protein, human)
RN  - EC 2.7.10.1 (ErbB Receptors)
RN  - EC 2.7.10.1 (Erbb4 protein, mouse)
RN  - EC 2.7.10.1 (Receptor, ErbB-2)
RN  - EC 2.7.10.1 (Receptor, ErbB-3)
RN  - EC 2.7.10.1 (Receptor, ErbB-4)
SB  - IM
MH  - 3T3 Cells
MH  - Animals
MH  - Base Sequence
MH  - Carrier Proteins/pharmacology
MH  - DNA Primers
MH  - DNA Replication/drug effects
MH  - Down-Regulation
MH  - *Endocytosis/drug effects
MH  - Epidermal Growth Factor/metabolism/*pharmacology
MH  - ErbB Receptors/drug effects/isolation & purification/*metabolism/*physiology
MH  - Glycoproteins/pharmacology
MH  - Humans
MH  - Kinetics
MH  - Mice
MH  - Molecular Sequence Data
MH  - *Neuregulin-1
MH  - Neuregulins
MH  - Polymerase Chain Reaction
MH  - Proto-Oncogene Proteins/drug effects/isolation & purification/*physiology
MH  - Receptor, ErbB-2/drug effects/isolation & purification/*physiology
MH  - Receptor, ErbB-3
MH  - Receptor, ErbB-4
MH  - Recombinant Fusion Proteins/drug effects/metabolism
MH  - Transfection
EDAT- 1996/03/01 00:00
MHDA- 1996/03/01 00:01
CRDT- 1996/03/01 00:00
PHST- 1996/03/01 00:00 [pubmed]
PHST- 1996/03/01 00:01 [medline]
PHST- 1996/03/01 00:00 [entrez]
AID - S0021-9258(18)82577-7 [pii]
AID - 10.1074/jbc.271.9.5251 [doi]
PST - ppublish
SO  - J Biol Chem. 1996 Mar 1;271(9):5251-7. doi: 10.1074/jbc.271.9.5251.