scholarly journals Identification and characterization of early growth response 2, a zinc-finger transcription factor, as a p53-regulated proapoptotic gene

2010 ◽  
Vol 37 (6) ◽  
Author(s):  
Tokino
2004 ◽  
Vol 173 (12) ◽  
pp. 7331-7338 ◽  
Author(s):  
John E. Harris ◽  
Kenneth D. Bishop ◽  
Nancy E. Phillips ◽  
John P. Mordes ◽  
Dale L. Greiner ◽  
...  

2014 ◽  
Vol 742 ◽  
pp. 8-14 ◽  
Author(s):  
Stefanie Klenke ◽  
Katharina Rump ◽  
Kai Buschkamp ◽  
Andrea Engler ◽  
Jürgen Peters ◽  
...  

2004 ◽  
Vol 279 (24) ◽  
pp. 25653-25664 ◽  
Author(s):  
María B. Durán Alonso ◽  
Georg Zoidl ◽  
Carla Taveggia ◽  
Frank Bosse ◽  
Christiane Zoidl ◽  
...  

2008 ◽  
Vol 76 (10) ◽  
pp. 4703-4712 ◽  
Author(s):  
Eric D. Phelps ◽  
Kristin R. Sweeney ◽  
Ira J. Blader

ABSTRACT Toxoplasma gondii is a ubiquitous apicomplexan parasite that can cause severe disease in fetuses and immune-compromised patients. Rhoptries, micronemes, and dense granules, which are secretory organelles unique to Toxoplasma and other apicomplexan parasites, play critical roles in parasite growth and virulence. To understand how these organelles modulate infected host cells, we sought to identify host cell transcription factors triggered by their release. Early growth response 2 (EGR2) is a host cell transcription factor that is rapidly upregulated and activated in Toxoplasma-infected cells but not in cells infected with the closely related apicomplexan parasite Neospora caninum. EGR2 upregulation occurred only when live parasites were in direct contact with the host cell and not from exposure to cell extracts that contain dense granule or micronemal proteins. When microneme-mediated attachment was blocked by pretreating parasites with a calcium chelator, EGR2 expression was significantly reduced. In contrast, when host cells were infected with parasites in the presence of cytochalasin D, which allows rhoptry secretion but prevents parasite invasion, EGR2 was activated. Finally, we demonstrate that Toxoplasma activation of host p38 mitogen-activated protein kinase is necessary but not sufficient for EGR2 activation. Collectively, these data indicate that EGR2 is specifically upregulated by a parasite-derived secreted factor that is most likely a resident rhoptry protein.


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