Please use this identifier to cite or link to this item:http://hdl.handle.net/20.500.12105/7899
Title
Shoc2/Sur8 Protein Regulates Neurite Outgrowth
Author(s)
Leon-Espinosa, Gonzalo ISCIII | Sanchez-Ruiloba, Lucia | Perez-Rodriguez, Andrea ISCIII | Gragera, Teresa ISCIII | Martinez, Natalia ISCIII | Hernandez, Silvia ISCIII | Anta-Felez, Berta ISCIII | Calero, Olga ISCIII | Garcia-Dominguez, Carlota A ISCIII | Dura, Lara M ISCIII | Peña-Jimenez, Daniel ISCIII | Castro, Judith ISCIII | Zarich-Dimitrievich, Natasha ISCIII | Sanchez-Gomez, Pilar ISCIII | Calero, Miguel ISCIII | Iglesias, Teresa | Oliva-Martinez, Jose Luis ISCIII | Rojas-Cabañeros, Jose Maria ISCIII
Date issued
2014
Citation
PLoS One. 2014 Dec 16;9(12):e114837
Language
Inglés
Abstract
The Shoc2 protein has been implicated in the positive regulation of the Ras-ERK pathway by increasing the functional binding interaction between Ras and Raf, leading to increased ERK activity. Here we found that Shoc2 overexpression induced sustained ERK phosphorylation, notably in the case of EGF stimulation, and Shoc2 knockdown inhibited ERK activation. We demonstrate that ectopic overexpression of human Shoc2 in PC12 cells significantly promotes neurite extension in the presence of EGF, a stimulus that induces proliferation rather than differentiation in these cells. Finally, Shoc2 depletion reduces both NGF-induced neurite outgrowth and ERK activation in PC12 cells. Our data indicate that Shoc2 is essential to modulate the Ras-ERK signaling outcome in cell differentiation processes involved in neurite outgrowth.
MESH
Animals | Cell Line, Tumor | Enzyme Activation | Epidermal Growth Factor | Extracellular Signal-Regulated MAP Kinases | HEK293 Cells | Humans | Intracellular Signaling Peptides and Proteins | MAP Kinase Signaling System | Neurites | PC12 Cells | Phosphorylation | RNA Interference | RNA, Small Interfering | Rats | ras Proteins
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