| Literature DB >> 22930637 |
Daniele Nosi1, Raffaella Mercatelli, Flaminia Chellini, Silvia Soria, Alessandro Pini, Lucia Formigli, Franco Quercioli.
Abstract
Cell-to-cell contacts are crucial for cell differentiation. The promyogenic cell surface protein, Cdo, functions as a component of multiprotein clusters to mediate cell adhesion signaling. Connexin 43, the main connexin forming gap junctions, also plays a key role in myogenesis. At least part of its effects is independent of the intercellular channel function, but the mechanisms underlying are unknown. Here, using multiple optical approaches, we provided the first evidence that Cx43 physically interacts with Cdo to form dynamic complexes during myoblast differentiation, offering clues for considering this interaction a structural basis of the channel-independent function of Cx43.Entities:
Keywords: C2C12 myoblasts; Förster resonance energy transfer; fluorescence lifetime imaging microscopy; myogenesis
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Year: 2012 PMID: 22930637 DOI: 10.1002/jbio.201200063
Source DB: PubMed Journal: J Biophotonics ISSN: 1864-063X Impact factor: 3.207