Alix Protein Is Substrate of Ozz-E3 Ligase and Modulates Actin Remodeling in Skeletal Muscle

Bongiovanni, Antonella; Romancino, Daniele P.; Campos, Yvan; Paterniti, Gaetano; Qiu, Xiaohui; Moshiach, Simon; Felice, Valentina Di; Vergani, Naja; Ustek, Duran; d’Azzo, Alessandra

doi:10.1074/jbc.m111.297036

Cited by 26 publications

(55 citation statements)

References 44 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We have shown previously that, in muscle cells, Alix is one of the substrates of the RING‐type ubiquitin ligase, Ozz‐E3 [8]. This ligase complex includes the substrate‐recognition module Ozz, as well as Elongin B and C, Rbx1 and Cullin 5 [11].…”

Section: Resultsmentioning

confidence: 99%

Identification and characterization of the nano‐sized vesicles released by muscle cells

et al. 2013

Self Cite

View full text Add to dashboard Cite

Several cell types secrete small membranous vesicles that contain cell-specific collections of proteins, lipids, and genetic material. The function of these vesicles is to allow cell-to-cell signaling and the horizontal transfer of their cargo molecules. Here, we demonstrate that muscle cells secrete nano-sized vesicles and that their release increases during muscle differentiation. Analysis of these nanovesicles allowed us to characterize them as exosome-like particles and to define the potential role of the multifunctional protein Alix in their biogenesis.

show abstract

Section: Resultsmentioning

confidence: 99%

Identification and characterization of the nano‐sized vesicles released by muscle cells

et al. 2013

Self Cite

View full text Add to dashboard Cite

show abstract

“…The establishment of actin cytoskeletal interactions with the extracellular matrix and between cells is important for myoblast differentiation (Kim et al, 2007). In addition, numerous studies have shown that actin-regulating proteins are involved in muscle differentiation and development (Bongiovanni et al, 2012;Nowak et al, 2009;Richardson et al, 2008). Suppression of Rho family small-GTPase activity by pharmacological inhibitors interferes with actin remodeling and the expression of myogenic factors such as myogenin and MRF4 (Bryan et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

Sox4-mediated caldesmon expression facilitates skeletal myoblast differentiation

Jang

Kim

et al. 2013

Journal of Cell Science

View full text Add to dashboard Cite

Summary Caldesmon (CaD), which was originally identified as an actin-regulatory protein, is involved in the regulation of diverse actin-related signaling processes, including cell migration and proliferation, in various cells. The cellular function of CaD has been studied primarily in the smooth muscle system; nothing is known about its function in skeletal muscle differentiation. In this study, we found that the expression of CaD gradually increased as differentiation of C2C12 myoblasts progressed. Silencing of CaD inhibited cell spreading and migration, resulting in a decrease in myoblast differentiation. Promoter analysis of the caldesmon gene (Cald1) and gel mobility shift assays identified Sox4 as a major trans-acting factor for the regulation of Cald1 expression during myoblast differentiation. Silencing of Sox4 decreased not only CaD protein synthesis but also myoblast fusion in C2C12 cells and myofibril formation in mouse embryonic muscle. Overexpression of CaD in Sox4-silenced C2C12 cells rescued the differentiation process. These results clearly demonstrate that CaD, regulated by Sox4 transcriptional activity, contributes to skeletal muscle differentiation.

show abstract

“…With respect to myogenesis, the WASP and ARP2/3 protein complexes are essential for myoblast fusion (Baas et al, 2012;Berger et al, 2008;Richardson et al, 2007), and WASP proteins promote myoblast migration (Kawamura et al, 2004). Although the mechanisms that direct myotube elongation are thought to mimic those of migratory cells (Bongiovanni et al, 2012), the role of Tropomyosin during myotube elongation has not been characterized.…”

Section: Introductionmentioning

confidence: 99%

Noncanonical roles for Tropomyosin during myogenesis

et al. 2015

View full text Add to dashboard Cite

For skeletal muscle to produce movement, individual myofibers must form stable contacts with tendon cells and then assemble sarcomeres. The myofiber precursor is the nascent myotube, and during myogenesis the myotube completes guided elongation to reach its target tendons. Unlike the well-studied events of myogenesis, such as myoblast specification and myoblast fusion, the molecules that regulate myotube elongation are largely unknown. In Drosophila, hoi polloi (hoip) encodes a highly conserved RNAbinding protein and hoip mutant embryos are largely paralytic due to defects in myotube elongation and sarcomeric protein expression. We used the hoip mutant background as a platform to identify novel regulators of myogenesis, and uncovered surprising developmental functions for the sarcomeric protein Tropomyosin 2 (Tm2). We have identified Hoip-responsive sequences in the coding region of the Tm2 mRNA that are essential for Tm2 protein expression in developing myotubes. Tm2 overexpression rescued the hoip myogenic phenotype by promoting F-actin assembly at the myotube leading edge, by restoring the expression of additional sarcomeric RNAs, and by promoting myoblast fusion. Embryos that lack Tm2 also showed reduced sarcomeric protein expression, and embryos that expressed a gain-of-function Tm2 allele showed both fusion and elongation defects. Tropomyosin therefore dictates fundamental steps of myogenesis prior to regulating contraction in the sarcomere.

show abstract

Alix Protein Is Substrate of Ozz-E3 Ligase and Modulates Actin Remodeling in Skeletal Muscle

Cited by 26 publications

References 44 publications

Identification and characterization of the nano‐sized vesicles released by muscle cells

Identification and characterization of the nano‐sized vesicles released by muscle cells

Sox4-mediated caldesmon expression facilitates skeletal myoblast differentiation

Noncanonical roles for Tropomyosin during myogenesis

Contact Info

Product

Resources

About