A molecular imaging analysis of C×43 association with Cdo during skeletal myoblast differentiation

Year: 2014

Authors: Nosi D., Mercatelli R., Chellini F., Soria S., Pini A., Formigli L., Quercioli F.

Autors Affiliation: Dipartimento di Anatomia, Istologia e Medicina Legale, Università di Firenze, Largo Brambilla 3, Firenze, Italy; ISC-CNR, Istituto Dei Sistemi Complessi, Via Madonna del Piano 10, 50019 Sesto Fiorentino (FI), Italy; IFAC-CNR, Istituto di Fisica Applicata N. Carrara, Via Madonna del Piano 10, 50019 Sesto Fiorentino (FI), Italy; Istituto Nazionale di Ottica, Consiglio Nazionale Delle Ricerche, Via Nello Carrara 1, Sesto Fiorentino, Italy

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.

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KeyWords: Cell adhesion; Cell membranes; Confocal microscopy; Photonic crystal fibers, Adhesion signaling; Cell differentiation; Cell surface proteins; Channel functions; Fluorescence lifetime imaging; Gap junctions; Structural basis; Supercontinuum, Molecular imaging