Premium
Ribosomal protein L10 interacts with the SH3 domain and regulates GDNF‐induced neurite growth in SH‐SY‐5y cells
Author(s) -
Park Seyeon,
Jeong DocGyun
Publication year - 2006
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.20888
Subject(s) - glial cell line derived neurotrophic factor , neurite , signal transducing adaptor protein , sh3 domain , microbiology and biotechnology , transfection , wiskott–aldrich syndrome protein , biology , proto oncogene tyrosine protein kinase src , neurotrophic factors , scaffold protein , cell culture , chemistry , phosphorylation , cell , signal transduction , actin cytoskeleton , genetics , receptor , cytoskeleton , in vitro
The 24.5 kDa ribosomal protein L10 (RP‐L10), which was encoded by QM gene, was known to interact with the SH3 domain of Yes kinase. Herein, we demonstrate that RP‐L10 interacts with the SH3 domain of Src and activates the binding of the Nck1 adaptor protein with skeletal proteins such as the Wiskott‐Aldrich Syndrome Protein (WASP) and WASP interacting protein (WIP) in neuroblastoma cell line, SH‐SY‐5y. The RP‐L10 was associated with the SH3 domains of Src and Yes. It is shown that two different regions of RP‐L10 are associated with the Src‐SH3. The effect of ectopic RP‐L10 expression on neuronal cell scaffolding was explored in cells transiently transfected with QM. SH‐SY‐5y human neuroblastoma cells transfected with QM were considerably more susceptible to neurite outgrowth induced by glial cell line‐derived neurotrophic factor (GDNF). However, RP‐L10 did not directly interact with actin assembly. Taken together, these results suggest that the RP‐L10 may positively regulate the GDNF/Ret‐mediated signaling of neurite outgrowth in the neuroblastoma cell line, SH‐SY‐5y. J. Cell. Biochem. 99: 624–634, 2006. © 2006 Wiley‐Liss, Inc.