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PMID: 8156997 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Neuronal differentiation signals are controlled by nerve growth factor receptor/Trk binding sites for SHC and PLC gamma.

The EMBO journal ·Vol. 13 ·No. 7 ·1994-04-01 ·Pages 1585-90

Obermeier A, Bradshaw RA, Seedorf K, Choidas A, Schlessinger J, Ullrich A

Abstract

Differentiation and survival of neuronal cell types requires the action of neurotrophic polypeptides such as nerve growth factor (NGF). In the central and peripheral nervous system and the phaeochromocytoma cell model PC12, NGF exerts its effects through the activation of the signalling capacity of Trk, a receptor tyrosine kinase (RTK) which upon interaction with NGF becomes phosphorylated on tyrosines and thereby acquires the potential to interact with signal-transducing proteins such as phospholipase C-gamma (PLC gamma), phosphatidylinositol-3'-kinase (PI3'-K) and SHC. Mutagenesis of the specific binding sites for these src homology 2 (SH2) domain-containing substrates within the Trk cytoplasmic domain suggests a non-essential function of PI3'-K and reveals a major role for the signal controlled by the SHC binding site at tyrosine 490 and a co-operative function of the PLC gamma-mediated pathway for neuronal differentiation of PC12 cells.

MeSH Terms
Animals Base Sequence Cell Differentiation/physiology Molecular Sequence Data Nerve Growth Factors/pharmacology Neurons/physiology PC12 Cells/physiology Phosphatidylinositol 3-Kinases Phosphotransferases (Alcohol Group Acceptor)/metabolism Platelet-Derived Growth Factor/pharmacology Protein-Tyrosine Kinases/metabolism Receptors, Nerve Growth Factor/metabolism Recombinant Proteins/metabolism Signal Transduction/physiology Transfection Type C Phospholipases/metabolism
Chemicals
Nerve Growth Factors Platelet-Derived Growth Factor Receptors, Nerve Growth Factor Recombinant Proteins Phosphatidylinositol 3-Kinases Phosphotransferases (Alcohol Group Acceptor) Protein-Tyrosine Kinases Type C Phospholipases
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Obermeier A
Department of Molecular Biology, Max-Planck-Institut für Biochemie, Martinsried, Germany.
Bradshaw R A
Seedorf K
Choidas A
Schlessinger J
Ullrich A
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1994-04-01
Pages
1585-90
Language
English
Region
England
NLM ID
8208664
PMCID
PMC394988
Subset
IM
External Links
PubMed source PMC Full Text View journal details
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