Key Points
- Identify and characterize FATZ, a novel 32-kDa skeletal muscle Z-disc protein, and assess its molecular interactions with core sarcomeric structural components.
- Conducted yeast two-hybrid experiments to evaluate binding of FATZ to alpha-actinin 2 and gamma-filamin/ABP-L domains.
- Performed glutathione S-transferase (GST) overlay assays to examine interactions between FATZ and telethonin.
- Screened internal and public muscle expressed sequence tag (EST) databases to identify transcripts homologous to FATZ.
- Demonstrated that the COOH-terminal region of FATZ binds the SR3-SR4 domains of alpha-actinin 2, binds gamma-filamin/ABP-L, and directly interacts with telethonin.
- Observed that FATZ protein levels increase during myogenic differentiation, becoming detectable prior to the expression of myosin.
- Identified two additional muscle transcripts sharing high domain homology with FATZ, defining a new family of muscle proteins.
Structured PICO
PPopulationSkeletal muscle cells/tissue (preclinical model)
IInterventionIdentification and characterization of FATZ protein
OOutcomeBinding interactions of FATZ with other Z-disc proteins (gamma-filamin/ABP-L, alpha-actinin, telethonin)
Identification of FATZ, a novel Z-disc protein that binds to filamin, actinin, and telethonin, suggesting a central role in myofibrillogenesis.