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Gamma-1-syntrophin mediates trafficking of gamma-enolase towards the plasma membrane and enhances its neurotrophic activity
Pišlar, Anja (Author), Obermajer, Nataša (Author), Kos, Janko (Author)

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Abstract
Syntrophins are scaffold proteins that can bind several signaling molecules and localize them to the plasma membrane. We demonstrate here that in neuroblastoma SH-SY5Y cells, brain-specific gamma1-syntrophin binds the neurotrophic factor gamma-enolase through its PDZ domain, and translocates it to the plasma membrane, as shown by immunoprecipitation, surface plasmon resonance, fluorescence colocalization and flow cytometry. Extensive colocalization of gamma1-syntrophin and gamma-enolase was observed in neurite growth cones in differentiated SH-SY5Y cells. Silencing of the gamma1-syntrophin gene by RNA interference significantly reduced the re-distribution of gamma-enolase to theplasma membrane and impaired its neurotrophic effects. We demonstrated thatan intact C-terminal end of gamma-enolase is essential for its gamma1-syntrophin-assisted trafficking. The cleavage of two amino acids at C-terminal end of gamma-enolase by the carboxypeptidase cathepsin X prevents binding with the gamma1-syntrophin PDZ domain. Collectively, these data demonstrate that gamma1-syntrophin participates in gamma-enolase translocation towardsthe plasma membrane, a pre-requisite for its neurotrophic activity. By disrupting this gamma1-syntrophin-guided subcellular distribution, cathepsin X reduces gamma-enolase-induced neurotrophic signaling.

Language:English
Keywords:gamma-1-sintropin, gama enolaze, katepsin X, nevrotropična aktivnost
Work type:Not categorized (r6)
Tipology:1.01 - Original Scientific Article
Organization:FFA - Faculty of Pharmacy
Year:2010
Number of pages:str. 246-258
Numbering:Vol. 18, no. 4
UDC:577.2
ISSN on article:1424-862X
DOI:10.1159/000324292 Link is opened in a new window
COBISS.SI-ID:2965617 Link is opened in a new window
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Downloads:216
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Record is a part of a journal

Title:NeuroSignals
Shortened title:NeuroSignals
Publisher:S. Karger
ISSN:1424-862X
COBISS.SI-ID:514941977 This link opens in a new window

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