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Cdo Interacts with APPL1 and Activates AKT in Myoblast Differentiation

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-cadher...

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Autores principales: Bae, Gyu-Un, Lee, Jae-Rin, Kim, Bok-Geon, Han, Ji-Won, Leem, Young-Eun, Lee, Hey-Jin, Ho, Seok-Man, Hahn, Myong-Joon, Kang, Jong-Sun
Formato: Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2903669/
https://www.ncbi.nlm.nih.gov/pubmed/20484574
http://dx.doi.org/10.1091/mbc.E09-12-1011
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author Bae, Gyu-Un
Lee, Jae-Rin
Kim, Bok-Geon
Han, Ji-Won
Leem, Young-Eun
Lee, Hey-Jin
Ho, Seok-Man
Hahn, Myong-Joon
Kang, Jong-Sun
author_facet Bae, Gyu-Un
Lee, Jae-Rin
Kim, Bok-Geon
Han, Ji-Won
Leem, Young-Eun
Lee, Hey-Jin
Ho, Seok-Man
Hahn, Myong-Joon
Kang, Jong-Sun
author_sort Bae, Gyu-Un
collection PubMed
description 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.
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spelling pubmed-29036692010-09-30 Cdo Interacts with APPL1 and Activates AKT in Myoblast Differentiation Bae, Gyu-Un Lee, Jae-Rin Kim, Bok-Geon Han, Ji-Won Leem, Young-Eun Lee, Hey-Jin Ho, Seok-Man Hahn, Myong-Joon Kang, Jong-Sun Mol Biol Cell Articles 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. The American Society for Cell Biology 2010-07-15 /pmc/articles/PMC2903669/ /pubmed/20484574 http://dx.doi.org/10.1091/mbc.E09-12-1011 Text en © 2010 by The American Society for Cell Biology
spellingShingle Articles
Bae, Gyu-Un
Lee, Jae-Rin
Kim, Bok-Geon
Han, Ji-Won
Leem, Young-Eun
Lee, Hey-Jin
Ho, Seok-Man
Hahn, Myong-Joon
Kang, Jong-Sun
Cdo Interacts with APPL1 and Activates AKT in Myoblast Differentiation
title Cdo Interacts with APPL1 and Activates AKT in Myoblast Differentiation
title_full Cdo Interacts with APPL1 and Activates AKT in Myoblast Differentiation
title_fullStr Cdo Interacts with APPL1 and Activates AKT in Myoblast Differentiation
title_full_unstemmed Cdo Interacts with APPL1 and Activates AKT in Myoblast Differentiation
title_short Cdo Interacts with APPL1 and Activates AKT in Myoblast Differentiation
title_sort cdo interacts with appl1 and activates akt in myoblast differentiation
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2903669/
https://www.ncbi.nlm.nih.gov/pubmed/20484574
http://dx.doi.org/10.1091/mbc.E09-12-1011
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