[HTML][HTML] The N-BAR domain protein, Bin3, regulates Rac1-and Cdc42-dependent processes in myogenesis

A Simionescu-Bankston, G Leoni, Y Wang… - Developmental …, 2013 - Elsevier
A Simionescu-Bankston, G Leoni, Y Wang, PP Pham, A Ramalingam, JB DuHadaway
Developmental biology, 2013Elsevier
Actin dynamics are necessary at multiple steps in the formation of multinucleated muscle
cells. BAR domain proteins can regulate actin dynamics in several cell types, but have been
little studied in skeletal muscle. Here, we identify novel functions for the N-BAR domain
protein, Bridging integrator 3 (Bin3), during myogenesis in mice. Bin3 plays an important
role in regulating myofiber size in vitro and in vivo. During early myogenesis, Bin3 promotes
migration of differentiated muscle cells, where it colocalizes with F-actin in lamellipodia. In …
Abstract
Actin dynamics are necessary at multiple steps in the formation of multinucleated muscle cells. BAR domain proteins can regulate actin dynamics in several cell types, but have been little studied in skeletal muscle. Here, we identify novel functions for the N-BAR domain protein, Bridging integrator 3 (Bin3), during myogenesis in mice. Bin3 plays an important role in regulating myofiber size in vitro and in vivo. During early myogenesis, Bin3 promotes migration of differentiated muscle cells, where it colocalizes with F-actin in lamellipodia. In addition, Bin3 forms a complex with Rac1 and Cdc42, Rho GTPases involved in actin polymerization, which are known to be essential for myotube formation. Importantly, a Bin3-dependent pathway is a major regulator of Rac1 and Cdc42 activity in differentiated muscle cells. Overall, these data classify N-BAR domain proteins as novel regulators of actin-dependent processes in myogenesis, and further implicate BAR domain proteins in muscle growth and repair.
Elsevier