PMID- 3494473
OWN - NLM
STAT- MEDLINE
DCOM- 19870605
LR  - 20220330
IS  - 0006-2960 (Print)
IS  - 0006-2960 (Linking)
VI  - 26
IP  - 5
DP  - 1987 Mar 10
TI  - Epidermal growth factor induces rapid, reversible aggregation of the purified 
      epidermal growth factor receptor.
PG  - 1443-51
AB  - Epidermal growth factor (EGF) receptor from A-431 cells was purified by affinity 
      chromatography with monoclonal anti-receptor antibodies. The purified 
      radiolabeled receptor was incubated with EGF and then analyzed by gel 
      electrophoresis under nondenaturing conditions. In these gels, the EGF receptor 
      migrates in two forms: a fast-migrating (low) form and an EGF-induced 
      slow-migrating (high) form. On the basis of the various control and calibration 
      experiments described, it is concluded that the low form represents the monomeric 
      170-kilodalton EGF receptor and the high form represents an EGF receptor dimer. 
      The binding of EGF causes a rapid, temperature-sensitive dimerization of the EGF 
      receptor. Receptor dimerization is fully reversible and involves saturable, 
      noncovalent interactions that are stable at neutral pH and in nonionic 
      detergents. Both the monomeric and dimeric forms of the receptor bind EGF and 
      undergo self-phosphorylation. The dimeric form of the receptor may possess higher 
      ligand binding affinity, and it seems to be phosphorylated earlier than the 
      monomeric form following the addition of EGF and [gamma-32P]ATP. On the basis of 
      these results, it is concluded that receptor oligomerization is an intrinsic 
      property of the occupied EGF receptor and that it may play a role in the 
      activation of the kinase function and the subsequent transmembrane signaling 
      process.
FAU - Yarden, Y
AU  - Yarden Y
FAU - Schlessinger, J
AU  - Schlessinger J
LA  - eng
GR  - CA 25820/CA/NCI NIH HHS/United States
PT  - Journal Article
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - United States
TA  - Biochemistry
JT  - Biochemistry
JID - 0370623
RN  - 0 (Cross-Linking Reagents)
RN  - 0 (Macromolecular Substances)
RN  - 62229-50-9 (Epidermal Growth Factor)
RN  - EC 2.7.10.1 (ErbB Receptors)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
SB  - IM
MH  - Allosteric Regulation
MH  - Cell Line
MH  - Cross-Linking Reagents
MH  - Epidermal Growth Factor/*physiology
MH  - ErbB Receptors/*physiology
MH  - Humans
MH  - Macromolecular Substances
MH  - Phosphorylation
MH  - Protein Binding
MH  - Protein-Tyrosine Kinases/metabolism
MH  - Structure-Activity Relationship
MH  - Temperature
EDAT- 1987/03/10 00:00
MHDA- 1987/03/10 00:01
CRDT- 1987/03/10 00:00
PHST- 1987/03/10 00:00 [pubmed]
PHST- 1987/03/10 00:01 [medline]
PHST- 1987/03/10 00:00 [entrez]
AID - 10.1021/bi00379a035 [doi]
PST - ppublish
SO  - Biochemistry. 1987 Mar 10;26(5):1443-51. doi: 10.1021/bi00379a035.