Please use this identifier to cite or link to this item: https://doi.org/10.1083/jcb.200801119
Title: A Cdo-Bnip-2-Cdc42 signaling pathway regulates p38α/β MAPK activity and myogenic differentiation
Authors: Kang, J.-S.
Bae, G.-U.
Yi, M.-J.
Yang, Y.-J.
Oh, J.-E.
Takaesu, G.
Yi, T.Z.
Boon, C.L. 
Krauss, R.S.
Issue Date: 11-Aug-2008
Citation: Kang, J.-S., Bae, G.-U., Yi, M.-J., Yang, Y.-J., Oh, J.-E., Takaesu, G., Yi, T.Z., Boon, C.L., Krauss, R.S. (2008-08-11). A Cdo-Bnip-2-Cdc42 signaling pathway regulates p38α/β MAPK activity and myogenic differentiation. Journal of Cell Biology 182 (3) : 497-507. ScholarBank@NUS Repository. https://doi.org/10.1083/jcb.200801119
Abstract: The p38α/β mitogen-activated protein kinase (MAPK) pathway promotes skeletal myogenesis, but the mechanisms by which it is activated during this process are unclear. During myoblast differentiation, the promyogenic cell surface receptor Cdo binds to the p38α/β pathway scaffold protein JLP and, via JLP, p38α/β itself. We report that Cdo also interacts with Bnip-2, a protein that binds the small guanosine triphosphatase (GTPase) Cdc42 and a negative regulator of Cdc42, Cdc42 GTPase-activating protein (GAP). Moreover, Bnip-2 and JLP are brought together through mutual interaction with Cdo. Gain- and loss-of-function experiments with myoblasts indicate that the Cdo-Bnip-2 interaction stimulates Cdc42 activity, which in turn promotes p38α/β activity and cell differentiation. These results reveal a previously unknown linkage between a cell surface receptor and downstream modulation of Cdc42 activity. Furthermore, interaction with multiple scaffold-type proteins is a distinctive mode of cell surface receptor signaling and provides one mechanism for specificity of p38α/β activation during cell differentiation. © 2008 Kang et al.
Source Title: Journal of Cell Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/99797
ISSN: 00219525
DOI: 10.1083/jcb.200801119
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