Document Detail

Cdo interacts with APPL1 and activates Akt in myoblast differentiation.
MedLine Citation:
PMID:  20484574     Owner:  NLM     Status:  MEDLINE    
Cell-cell interactions between muscle precursors are required for myogenic differentiation; however, underlying mechanisms are largely unknown. Promyogenic cell surface protein Cdo functions as a component of multiprotein complexes containing other cell adhesion molecules, Boc, Neogenin and N-cadherin, and mediates some of signals triggered by cell-cell interactions between muscle precursors. Cdo activates p38MAPK via interaction with two scaffold proteins JLP and Bnip-2 to promote myogenesis. p38MAPK and Akt signaling are required for myogenic differentiation and activation of both signaling pathways is crucial for efficient myogenic differentiation. We report here that APPL1, an interacting partner of Akt, forms complexes with Cdo and Boc in differentiating myoblasts. Both Cdo and APPL1 are required for efficient Akt activation during myoblast differentiation. The defective differentiation of Cdo-depleted cells is fully rescued by overexpression of a constitutively active form of Akt, whereas overexpression of APPL1 fails to do so. Taken together, Cdo activates Akt through association with APPL1 during myoblast differentiation, and this complex likely mediates some of the promyogenic effect of cell-cell interaction. The promyogenic function of Cdo involves a coordinated activation of p38MAPK and Akt via association with scaffold proteins, JLP and Bnip-2 for p38MAPK and APPL1 for Akt.
Gyu-Un Bae; Jae-Rin Lee; Bok-Geon Kim; Ji-Won Han; Young-Eun Leem; Hey-Jin Lee; Seok-Man Ho; Myong-Joon Hahn; Jong-Sun Kang
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Publication Detail:
Type:  Journal Article     Date:  2010-05-19
Journal Detail:
Title:  Molecular biology of the cell     Volume:  21     ISSN:  1939-4586     ISO Abbreviation:  Mol. Biol. Cell     Publication Date:  2010 Jul 
Date Detail:
Created Date:  2010-07-14     Completed Date:  2010-10-21     Revised Date:  2013-05-29    
Medline Journal Info:
Nlm Unique ID:  9201390     Medline TA:  Mol Biol Cell     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2399-411     Citation Subset:  IM    
Department of Molecular Cell Biology, Center for Molecular Medicine, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon 440-746, Republic of Korea.
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MeSH Terms
Adaptor Proteins, Signal Transducing / metabolism*
Amino Acids / metabolism
Cadherins / metabolism
Cell Adhesion Molecules / deficiency,  metabolism*
Cell Differentiation*
Cell Line
Enzyme Activation
Membrane Proteins / metabolism
Muscle Development
Myoblasts / cytology*,  enzymology*
Protein Binding
Proto-Oncogene Proteins c-akt / metabolism*
Reg. No./Substance:
0/APPL1 protein, human; 0/Adaptor Proteins, Signal Transducing; 0/Amino Acids; 0/Appl1 protein, mouse; 0/Cadherins; 0/Cdo protein, mouse; 0/Cell Adhesion Molecules; 0/Membrane Proteins; 0/neogenin; EC Proteins c-akt

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