PMID- 2790960
OWN - NLM
STAT- MEDLINE
DCOM- 19891108
LR  - 20190705
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 59
IP  - 1
DP  - 1989 Oct 6
TI  - Functional independence of the epidermal growth factor receptor from a domain 
      required for ligand-induced internalization and calcium regulation.
PG  - 33-43
AB  - We have located the distal boundary of the tyrosine kinase domain of the EGF 
      receptor and have identified a distinct sequence in the C' terminus required for 
      EGF-dependent receptor internalization, leading to receptor down-regulation and 
      degradation. Within this receptor domain, an 18 amino acid highly negatively 
      charged region of predicted helical structure is required both for endocytosis 
      via a high-affinity, saturable pathway and for ligand-stimulated increases in 
      cytosolic calcium. In contrast to kinase-inactive, internalization-competent 
      receptors, kinase-active, internalization-defective receptors effectively 
      signaled gene transcription, morphological transformation, and growth. These 
      observations support the hypothesis that mitogenic responses to EGF are mediated 
      by activation of the intrinsic protein tyrosine kinase activity of the 
      membrane-bound receptor, with ligand-induced internalization serving to terminate 
      the signal.
FAU - Chen, W S
AU  - Chen WS
AD  - School of Medicine, University of California, San Diego, La Jolla 92093.
FAU - Lazar, C S
AU  - Lazar CS
FAU - Lund, K A
AU  - Lund KA
FAU - Welsh, J B
AU  - Welsh JB
FAU - Chang, C P
AU  - Chang CP
FAU - Walton, G M
AU  - Walton GM
FAU - Der, C J
AU  - Der CJ
FAU - Wiley, H S
AU  - Wiley HS
FAU - Gill, G N
AU  - Gill GN
FAU - Rosenfeld, M G
AU  - Rosenfeld MG
LA  - eng
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  - Cell
JT  - Cell
JID - 0413066
RN  - EC 2.7.10.1 (ErbB Receptors)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Amino Acid Sequence
MH  - Animals
MH  - Calcium/metabolism/*physiology
MH  - Cell Line
MH  - Down-Regulation
MH  - *Endocytosis
MH  - Enzyme Activation
MH  - ErbB Receptors/metabolism/*physiology
MH  - Humans
MH  - Kinetics
MH  - Mice
MH  - Molecular Sequence Data
MH  - Protein-Tyrosine Kinases/metabolism/physiology
EDAT- 1989/10/06 00:00
MHDA- 1989/10/06 00:01
CRDT- 1989/10/06 00:00
PHST- 1989/10/06 00:00 [pubmed]
PHST- 1989/10/06 00:01 [medline]
PHST- 1989/10/06 00:00 [entrez]
AID - 0092-8674(89)90867-2 [pii]
AID - 10.1016/0092-8674(89)90867-2 [doi]
PST - ppublish
SO  - Cell. 1989 Oct 6;59(1):33-43. doi: 10.1016/0092-8674(89)90867-2.