Paper
28 February 2014 A molecular imaging analysis of C×43 association with Cdo during skeletal myoblast differentiation
Daniele Nosi, Raffaella Mercatelli, Flaminia Chellini, Silvia Soria, Alessandro Pini, Lucia Formigli, Franco Quercioli
Author Affiliations +
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. Connexin43, the main connexin forming gap junctions, also plays a key role in myogenesis. At least part of its effects are 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.
© (2014) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Daniele Nosi, Raffaella Mercatelli, Flaminia Chellini, Silvia Soria, Alessandro Pini, Lucia Formigli, and Franco Quercioli "A molecular imaging analysis of C×43 association with Cdo during skeletal myoblast differentiation", Proc. SPIE 8948, Multiphoton Microscopy in the Biomedical Sciences XIV, 89481N (28 February 2014); https://doi.org/10.1117/12.2041667
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KEYWORDS
Luminescence

Fluorescence resonance energy transfer

Confocal microscopy

Proteins

Control systems

Fluorescence lifetime imaging

Molecular imaging

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