title: FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle.
abstract: We report the identification and characterization of a novel 32-kDa protein expressed in skeletal muscle and located in the Z-disc of the sarcomere. We found that this protein binds to three other Z-disc proteins; therefore, we have named it FATZ, gamma-filamin/ABP-L, alpha-actinin and telethonin binding protein of the Z-disc. From yeast two-hybrid experiments we are able to show that the SR3-SR4 domains of alpha-actinin 2 are required to bind the COOH-terminal region of the FATZ as does gamma-filamin/ABP-L. Furthermore, by using a glutathione S-transferase overlay assay we find that FATZ also binds telethonin. The level of FATZ protein in muscle cells increases during differentiation, being clearly detectable before the onset of myosin. Although FATZ has no known interaction domains, it would appear to be involved in a complex network of interactions with other Z-band components. On the basis of the information known about its binding partners, we could envisage a central role for FATZ in the myofibrillogenesis. After screening our muscle expressed sequence tag data base and the public expressed sequence tag data bases, we were able to assemble two other muscle transcripts that show a high level of identity with FATZ in two different domains. Therefore, FATZ may be the first member of a small family of novel muscle proteins.
authors.affiliation: International Centre for Genetic Engineering and Biotechnology, Padriciano 99, I-34012 Trieste, Padova, Italy.
authors.forename: G
authors.initials: G
authors.lastname: Faulkner
authors.forename: A
authors.initials: A
authors.lastname: Pallavicini
authors.forename: A
authors.initials: A
authors.lastname: Comelli
authors.forename: M
authors.initials: M
authors.lastname: Salamon
authors.forename: G
authors.initials: G
authors.lastname: Bortoletto
authors.forename: C
authors.initials: C
authors.lastname: Ievolella
authors.forename: S
authors.initials: S
authors.lastname: Trevisan
authors.forename: S
authors.initials: S
authors.lastname: Kojic'
authors.forename: F
authors.initials: F
authors.lastname: Dalla Vecchia
authors.forename: P
authors.initials: P
authors.lastname: Laveder
authors.forename: G
authors.initials: G
authors.lastname: Valle
authors.forename: G
authors.initials: G
authors.lastname: Lanfranchi
mesh_terms: D000185:Actinin / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002352:Carrier Proteins / Q000032:analysis* / Q000737:chemistry / Q000235:genetics; D002454:Cell Differentiation; D002478:Cells, Cultured; D003001:Cloning, Molecular; D064211:Connectin; D003285:Contractile Proteins / Q000378:metabolism*; D064448:Filamins; D006801:Humans; D051379:Mice; D008840:Microfilament Proteins / Q000378:metabolism*; D008969:Molecular Sequence Data; D009124:Muscle Proteins / Q000032:analysis* / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000737:chemistry*
chemical_list: D002352:Carrier Proteins; D064211:Connectin; D003285:Contractile Proteins; D064448:Filamins; D008840:Microfilament Proteins; D009124:Muscle Proteins; C577292:TCAP protein, human; C577294:Tcap protein, mouse; D000185:Actinin