scholarly journals A Trk nerve growth factor (NGF) receptor point mutation affecting interaction with phospholipase C-gamma 1 abolishes NGF-promoted peripherin induction but not neurite outgrowth.

1994 ◽  
Vol 269 (12) ◽  
pp. 8901-8910
Author(s):  
D.M. Loeb ◽  
R.M. Stephens ◽  
T. Copeland ◽  
D.R. Kaplan ◽  
L.A. Greene
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Neurite Outgrowth ◽  
Phospholipase C ◽  
Point Mutation ◽  
Nerve Growth ◽  
Ngf Receptor ◽  
Phospholipase C Gamma

scholarly journals Nerve growth factor stimulates phosphorylation of phospholipase C-gamma in PC12 cells

1991 ◽  
Vol 266 (3) ◽  
pp. 1359-1362 ◽  
Author(s):  
U H Kim ◽  
D Fink ◽  
H S Kim ◽  
D J Park ◽  
M L Contreras ◽  
...  
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Phospholipase C ◽  
Pc12 Cells ◽  
Nerve Growth ◽  
Phospholipase C Gamma

scholarly journals Phosphorylation of the Unique C-Terminal Tail of the Alpha Isoform of the Scaffold Protein SH2B1 Controls the Ability of SH2B1α To Enhance Nerve Growth Factor Function

2017 ◽  
Vol 38 (6) ◽  
Author(s):  
Ray M. Joe ◽  
Anabel Flores ◽  
Michael E. Doche ◽  
Joel M. Cline ◽  
Erik S. Clutter ◽  
...  
Keyword(s):  
Gene Expression ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Neurite Outgrowth ◽  
Scaffold Protein ◽  
Nerve Growth ◽  
Ngf Receptor ◽  
Factor Function ◽  
Enhance Neurite Outgrowth

ABSTRACTThe scaffold protein SH2B1, a major regulator of body weight, is recruited to the receptors of multiple cytokines and growth factors, including nerve growth factor (NGF). The β isoform but not the α isoform of SH2B1 greatly enhances NGF-dependent neurite outgrowth of PC12 cells. Here, we asked how the unique C-terminal tails of the α and β isoforms modulate SH2B1 function. We compared the actions of SH2B1α and SH2B1β to those of the N-terminal 631 amino acids shared by both isoforms. In contrast to the β tail, the α tail inhibited the ability of SH2B1 to both cycle through the nucleus and enhance NGF-mediated neurite outgrowth, gene expression, phosphorylation of Akt and phospholipase C-gamma (PLC-γ), and autophosphorylation of the NGF receptor TrkA. These functions were restored when Tyr753 in the α tail was mutated to phenylalanine. We provide evidence that TrkA phosphorylates Tyr753 in SH2B1α, as well as tyrosines 439 and 55 in both SH2B1α and SH2B1β. Finally, coexpression of SH2B1α but not SH2B1α with a mutation of Y to F at position 753 (Y753F) inhibited the ability of SH2B1β to enhance neurite outgrowth. These results suggest that the C-terminal tails of SH2B1 isoforms are key determinants of the cellular role of SH2B1. Furthermore, the function of SH2B1α is regulated by phosphorylation of the α tail.

scholarly journals Expression of beta-nerve growth factor and its receptor in rat seminiferous epithelium: specific function at the onset of meiosis.

1992 ◽  
Vol 117 (3) ◽  
pp. 629-641 ◽  
Author(s):  
M Parvinen ◽  
M Pelto-Huikko ◽  
O Söder ◽  
R Schultz ◽  
A Kaipia ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Sertoli Cells ◽  
Seminiferous Epithelium ◽  
Receptor Protein ◽  
Tyrosine Kinase Receptor ◽  
Specific Expression ◽  
Nerve Growth ◽  
Ngf Receptor

beta-Nerve growth factor (NGF) is expressed in spermatogenic cells and has testosterone-downregulated low-affinity receptors on Sertoli cells suggesting a paracrine role in the regulation of spermatogenesis. An analysis of the stage-specific expression of NGF and its low affinity receptor during the cycle of the seminiferous epithelium in the rat revealed NGF mRNA and protein at all stages of the cycle. Tyrosine kinase receptor (trk) mRNA encoding an essential component of the high-affinity NGF receptor was also present at all stages. In contrast, expression of low affinity NGF receptor mRNA was only found in stages VIIcd and VIII of the cycle, the sites of onset of meiosis. The low-affinity NGF receptor protein was present in the plasma membrane of the apical Sertoli cell processes as well as in the basal plasma membrane of these cells at stages VIIcd to XI. NGF was shown to stimulate in vitro DNA synthesis of seminiferous tubule segments with preleptotene spermatocytes at the onset of meiosis while other segments remained nonresponsive. We conclude that NGF is a meiotic growth factor that acts through Sertoli cells.

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