Specificity of nerve growth factor signaling: Differential patterns of early tyrosine phosphorylation events induced by NGF, EGF, and bFGF

1995 ◽  
Vol 41 (5) ◽  
pp. 628-639 ◽  
Author(s):  
D. Blumberg ◽  
M. J. Radeke ◽  
S. C. Feinstein
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Tyrosine Phosphorylation ◽  
Growth Factor Signaling ◽  
Nerve Growth

scholarly journals The statistical mechanics of complex signaling networks: nerve growth factor signaling

2004 ◽  
Vol 1 (3) ◽  
pp. 184-195 ◽  
Author(s):  
K S Brown ◽  
C C Hill ◽  
G A Calero ◽  
C R Myers ◽  
K H Lee ◽  
...  
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Statistical Mechanics ◽  
Signaling Networks ◽  
Growth Factor Signaling ◽  
Nerve Growth ◽  
Complex Signaling

scholarly journals Nerve Growth Factor Stimulates Multisite Tyrosine Phosphorylation and Activation of the Atypical Protein Kinase C's via a src Kinase Pathway

2001 ◽  
Vol 21 (24) ◽  
pp. 8414-8427 ◽  
Author(s):  
Marie W. Wooten ◽  
Michel L. Vandenplas ◽  
M. Lamar Seibenhener ◽  
Thangiah Geetha ◽  
Maria T. Diaz-Meco
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Protein Kinase ◽  
Tyrosine Phosphorylation ◽  
Pc12 Cells ◽  
Catalytic Domain ◽  
Src Kinase ◽  
Dependent Manner ◽  
Nerve Growth ◽  
Atypical Protein Kinase

ABSTRACT Atypical protein kinase C (PKC) isoforms are required for nerve growth factor (NGF)-initiated differentiation of PC12 cells. In the present study, we report that PKC-ι becomes tyrosine phosphorylated in the membrane coincident with activation posttreatment with nerve growth factor. Tyrosine phosphorylation and activation of PKC-ι were inhibited in a dose-dependent manner by both PP2 and K252a, src and TrkA kinase inhibitors. Purified src was observed to phosphorylate and activate PKC-ι in vitro. In PC12 cells deficient in src kinase activity, both NGF-induced tyrosine phosphorylation and activation of PKC-ι were also diminished. Furthermore, we demonstrate activation of src by NGF along with formation of a signal complex including the TrkA receptor, src, and PKC-ι. Recruitment of PKC-ι into the complex was dependent on the tyrosine phosphorylation state of PKC-ι. The association of src and PKC-ι was constitutive but was enhanced by NGF treatment, with the src homology 3 domain interacting with a PXXP sequence within the regulatory domain of PKC-ι (amino acids 98 to 114). Altogether, these findings support a role for src in regulation of PKC-ι. Tyrosine 256, 271, and 325 were identified as major sites phosphorylated by src in the catalytic domain. Y256F and Y271F mutations did not alter src-induced activation of PKC-ι, whereas the Y325F mutation significantly reduced src-induced activation of PKC-ι. The functional relevance of these mutations was tested by determining the ability of each mutant to support TRAF6 activation of NF-κB, with significant impairment by the Y325F PKC-ι mutant. Moreover, when the Y352F mutant was expressed in PC12 cells, NGF's ability to promote survival in serum-free media was reduced. In summary, we have identified a novel mechanism for NGF-induced activation of atypical PKC involving tyrosine phosphorylation by c-Src.

scholarly journals The Neurotrophin Receptor Homolog-2 regulates Nerve Growth Factor signaling.

2008 ◽  
Author(s):  
Agnes W Wong ◽  
Melanie Willingham ◽  
Junhua Xiao ◽  
Trevor J Kilpatrick ◽  
Simon S Murray
Keyword(s):  
Nerve Growth Factor ◽  
Growth Factor ◽  
Neurotrophin Receptor ◽  
Growth Factor Signaling ◽  
Nerve Growth

scholarly journals Human carbonic anhydrase-8 AAV8 gene therapy inhibits nerve growth factor signaling producing prolonged analgesia and anti-hyperalgesia in mice

Gene Therapy ◽  
2018 ◽  
Vol 25 (4) ◽  
pp. 297-311 ◽  
Author(s):  
Gerald Z. Zhuang ◽  
Udita Upadhyay ◽  
Xiaoying Tong ◽  
Yuan Kang ◽  
Diana M. Erasso ◽  
...  
Keyword(s):  
Gene Therapy ◽  
Nerve Growth Factor ◽  
Growth Factor ◽  
Carbonic Anhydrase ◽  
Growth Factor Signaling ◽  
Nerve Growth ◽  
Human Carbonic Anhydrase
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