PMID- 1351469
OWN - NLM
STAT- MEDLINE
DCOM- 19920717
LR  - 20190620
IS  - 0014-5793 (Print)
IS  - 0014-5793 (Linking)
VI  - 303
IP  - 2-3
DP  - 1992 Jun 1
TI  - The effects of the normal and oncogenic forms of the neu tyrosine kinase, and the 
      corresponding forms of an immunoglobulin E receptor/neu tyrosine kinase fusion 
      protein, on Xenopus oocyte maturation.
PG  - 164-8
AB  - In this work, we have used Xenopus oocyte maturation as a read-out for examining 
      the ability of the neu tyrosine kinase (p185neu) to participate with the 
      epidermal growth factor (EGF) receptor in a common signal transduction pathway. 
      We find that unlike the case for the EGF receptor, which elicits EGF-dependent 
      maturation of these oocytes as reflected by their germinal vesicle breakdown 
      (GVBD), neither the normal neu tyrosine kinase (p185val664) nor the oncogenic 
      form of neu (p185glu664) are able to effectively trigger this maturation event. 
      However, expression of p185glu664 causes a specific and significant promotion of 
      the progesterone-induced GVBD, reducing the half-time for this maturation even 
      from approximately 9 h to approximately 5 h. Stimulation of the 
      progesterone-induced GVBD did not occur following the expression of a 
      kinase-deficient p185neu protein (in which a lysine residue at position 758 was 
      changed to alanine). Essentially identical results were obtained when the mRNAs 
      coding for fusion proteins comprised of the extracellular domain of the receptor 
      for immunoglobulin E (IgE), and the membrane-spanning and tyrosine kinase domains 
      of normal or oncogenic p185neu (designated IgER/p185val664 and IgER/p185glu664, 
      respectively), were injected into oocytes. Antigen-induced crosslinking of 
      IgER/p185val164 proteins expressed in oocytes caused a reduction in the half-time 
      for the progesterone-stimulated GVBD from approximately 9 h to approximately 7 h. 
      Thus, the aggregation of the membrane-spanning and/or tyrosine kinase domains of 
      p185val664 partially mimics the effects of the oncogenic forms of p185neu. 
      Overall, the results of these studies suggest that the activation of the p185neu 
      tyrosine kinase by a point mutation within its membrane-spanning helix, or an 
      aggregation event, can result in the facilitation of oocyte maturation events 
      that are elicited by other factors (e.g. progesterone). However, the activated 
      p185neu tyrosine kinases are not able to mimic the EGF-stimulated EGF receptor 
      tyrosine kinase in triggering oocyte maturation, which suggests that the EGF 
      receptor and the p185neu tyrosine kinase do not input into identical signal 
      transduction pathways in these cells.
FAU - Narasimhan, V
AU  - Narasimhan V
AD  - Department of Pharmacology, Cornell University, Ithaca, NY 14853-6401.
FAU - Hamill, O
AU  - Hamill O
FAU - Cerione, R A
AU  - Cerione RA
LA  - eng
GR  - GM40654/GM/NIGMS NIH HHS/United States
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - FEBS Lett
JT  - FEBS letters
JID - 0155157
RN  - 0 (Antigens, Differentiation, B-Lymphocyte)
RN  - 0 (Oncogene Proteins)
RN  - 0 (Proto-Oncogene Proteins)
RN  - 0 (Receptors, Fc)
RN  - 0 (Receptors, IgE)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 62229-50-9 (Epidermal Growth Factor)
RN  - EC 2.7.10.1 (Protein-Tyrosine Kinases)
RN  - EC 2.7.10.1 (Receptor, ErbB-2)
SB  - IM
MH  - Animals
MH  - Antigens, Differentiation, B-Lymphocyte/genetics/*metabolism
MH  - Cell Division
MH  - Cells, Cultured
MH  - Epidermal Growth Factor/physiology
MH  - Kinetics
MH  - Microinjections
MH  - Oncogene Proteins/genetics/metabolism
MH  - Oocytes/*cytology
MH  - Protein-Tyrosine Kinases/genetics/*metabolism
MH  - Proto-Oncogene Proteins/genetics/*metabolism
MH  - Receptor, ErbB-2
MH  - Receptors, Fc/genetics/*metabolism
MH  - Receptors, IgE
MH  - Recombinant Fusion Proteins/genetics/metabolism
MH  - Signal Transduction
MH  - Xenopus laevis
EDAT- 1992/06/01 00:00
MHDA- 1992/06/01 00:01
CRDT- 1992/06/01 00:00
PHST- 1992/06/01 00:00 [pubmed]
PHST- 1992/06/01 00:01 [medline]
PHST- 1992/06/01 00:00 [entrez]
AID - 0014-5793(92)80510-N [pii]
AID - 10.1016/0014-5793(92)80510-n [doi]
PST - ppublish
SO  - FEBS Lett. 1992 Jun 1;303(2-3):164-8. doi: 10.1016/0014-5793(92)80510-n.