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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2011-1-4
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pubmed:abstractText |
We previously reported that the scaffold protein c-Jun NH?-terminal kinase (JNK)/stress-activated protein kinase-associated protein 1 (JSAP1) functions in cerebellar granule cell precursors (GCPs) to promote their cell-cycle exit and differentiation. In this study, we used immunocytochemistry to examine the subcellular distribution of JSAP1 in proliferating cultured GCPs. We found that when stimulated with fibroblast growth factor-2 (FGF-2), a factor that promotes GCP differentiation through JNK and extracellular signal-regulated kinase (ERK) signaling, JSAP1 translocated to the plasma membrane and colocalized with activated JNK and ERK. In transfected cells expressing a constitutively activated FGF receptor (FGFR), JSAP1 and the activated FGFR colocalized at the plasma membrane with not only activated but also unphosphorylated and inactive JNK and ERK. These colocalizations did not occur when a mutant JSAP1 lacking the JNK-binding domain was substituted for wild-type JSAP1. Biochemical analyses of transfected cells showed that activated FGFR increased JSAP1's affinity for JNK and ERK and that JSAP1 enhanced FGFR-induced JNK and ERK activation. Collectively, these results suggest that when stimulated by FGFR, JSAP1 translocates to the plasma membrane, where it recruits JNK and ERK and facilitates their activation, leading to the differentiation of cerebellar GCPs.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
1365-2443
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pubmed:author |
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pubmed:copyrightInfo |
© 2010 The Authors. Journal compilation © 2010 by the Molecular Biology Society of Japan/Blackwell Publishing Ltd.
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pubmed:issnType |
Electronic
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pubmed:volume |
16
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
58-68
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pubmed:meshHeading |
pubmed-meshheading:21156008-Adaptor Proteins, Signal Transducing,
pubmed-meshheading:21156008-Animals,
pubmed-meshheading:21156008-Cell Differentiation,
pubmed-meshheading:21156008-Cell Membrane,
pubmed-meshheading:21156008-Cell Movement,
pubmed-meshheading:21156008-Cell Proliferation,
pubmed-meshheading:21156008-Cells, Cultured,
pubmed-meshheading:21156008-Cerebellum,
pubmed-meshheading:21156008-Enzyme Activation,
pubmed-meshheading:21156008-Extracellular Signal-Regulated MAP Kinases,
pubmed-meshheading:21156008-Fibroblast Growth Factor 2,
pubmed-meshheading:21156008-HEK293 Cells,
pubmed-meshheading:21156008-Humans,
pubmed-meshheading:21156008-Immunohistochemistry,
pubmed-meshheading:21156008-MAP Kinase Signaling System,
pubmed-meshheading:21156008-Mice,
pubmed-meshheading:21156008-Mice, Inbred C57BL,
pubmed-meshheading:21156008-Mitogen-Activated Protein Kinase 8,
pubmed-meshheading:21156008-Mitogen-Activated Protein Kinase 9,
pubmed-meshheading:21156008-Nerve Tissue Proteins,
pubmed-meshheading:21156008-Protein Binding,
pubmed-meshheading:21156008-Stem Cells,
pubmed-meshheading:21156008-Transfection
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pubmed:year |
2011
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pubmed:articleTitle |
Role of plasma membrane localization of the scaffold protein JSAP1 during differentiation of cerebellar granule cell precursors.
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pubmed:affiliation |
Division of Molecular Cell Signaling, Cancer Research Institute, Kanazawa University, Kanazawa 920-1192, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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