The Drosophila Z-disc Protein Z(210) Is an Adult Muscle Isoform of Zasp52, Which Is Required for Normal Myofibril Organization in Indirect Flight Muscles

Chechenova, Maria B.; Bryantsev, Anton L.; Cripps, Richard M.

doi:10.1074/jbc.m112.401794

Cited by 15 publications

(14 citation statements)

References 28 publications

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“…Besides α-Actinin, Zasp52 is another important Z-disk protein that is thought to interact with α-Actinin and cooperate in Z-disk formation (Katzemich et al, 2013;Liao et al, 2016). Using a monoclonal antibody (Table S1) against a muscle-specific Zasp52 isoform (also known as Z(210); Chechenova et al, 2013) reveals a band-type distribution ( Fig. 4, C-E) with a half bandwidth of 39.4 nm.…”

Section: Z-disk Organization and Elastic Filament Localization In Thementioning

confidence: 99%

Nanoscopy reveals the layered organization of the sarcomeric H-zone and I-band complexes

Szikora

Gajdos

Novák

et al. 2019

Journal of Cell Biology

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Sarcomeres are extremely highly ordered macromolecular assemblies where structural organization is intimately linked to their functionality as contractile units. Although the structural basis of actin and Myosin interaction is revealed at a quasiatomic resolution, much less is known about the molecular organization of the I-band and H-zone. We report the development of a powerful nanoscopic approach, combined with a structure-averaging algorithm, that allowed us to determine the position of 27 sarcomeric proteins in Drosophila melanogaster flight muscles with a quasimolecular, ∼5- to 10-nm localization precision. With this protein localization atlas and template-based protein structure modeling, we have assembled refined I-band and H-zone models with unparalleled scope and resolution. In addition, we found that actin regulatory proteins of the H-zone are organized into two distinct layers, suggesting that the major place of thin filament assembly is an M-line–centered narrow domain where short actin oligomers can form and subsequently anneal to the pointed end.

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Section: Z-disk Organization and Elastic Filament Localization In Thementioning

confidence: 99%

Nanoscopy reveals the layered organization of the sarcomeric H-zone and I-band complexes

Szikora

Gajdos

Novák

et al. 2019

Journal of Cell Biology

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“…In Drosophila , Zasp52 has a PDZ, ZM (Zasp-like motif) and four LIM domains; while Zasp66 and Zasp67 only feature the N-terminal PDZ domain and a weakly conserved ZM domain. Zasp52 colocalizes with α-actinin at Z-discs and plays a role in myofibril assembly and maintenance [3, 17, 18]. Many different Zasp52 splice isoforms have been identified resulting in up to 61 different proteins, some of them restricted to specific muscle types [19, 20].…”

Section: Introductionmentioning

confidence: 99%

Zasp52, a Core Z-disc Protein in Drosophila Indirect Flight Muscles, Interacts with α-Actinin via an Extended PDZ Domain

2016

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Z-discs are organizing centers that establish and maintain myofibril structure and function. Important Z-disc proteins are α-actinin, which cross-links actin thin filaments at the Z-disc and Zasp PDZ domain proteins, which directly interact with α-actinin. Here we investigate the biochemical and genetic nature of this interaction in more detail. Zasp52 is the major Drosophila Zasp PDZ domain protein, and is required for myofibril assembly and maintenance. We show by in vitro biochemistry that the PDZ domain plus a C-terminal extension is the only area of Zasp52 involved in the interaction with α-actinin. In addition, site-directed mutagenesis of 5 amino acid residues in the N-terminal part of the PDZ domain, within the PWGFRL motif, abolish binding to α-actinin, demonstrating the importance of this motif for α-actinin binding. Rescue assays of a novel Zasp52 allele demonstrate the crucial importance of the PDZ domain for Zasp52 function. Flight assays also show that a Zasp52 mutant suppresses the α-actinin mutant phenotype, indicating that both proteins are core structural Z-disc proteins required for optimal Z-disc function.

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“…In Drosophila, Zasp52 has a PDZ, ZM (Zasp-like motif) and four LIM domains; while Zasp66 and Zasp67 feature only the N-terminal PDZ domain and a weakly conserved ZM domain. Zasp52 colocalizes with a-actinin at Z-discs and plays a role in myofibril assembly and maintenance (Jani and Schöck 2007;Chechenova et al 2013;Katzemich et al 2013). Many different Zasp52 splice isoforms have been identified, resulting in up to 61 different proteins, some of which are restricted to specific muscle types (Katzemich et al 2011;Brown et al 2014).…”

mentioning

confidence: 99%

Different Evolutionary Trajectories of Two Insect-Specific Paralogous Proteins Involved in Stabilizing Muscle Myofibrils

González-Morales¹,

Marsh²,

Katzemich³

et al. 2019

Genetics

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Alp/Enigma family members have a unique PDZ domain followed by zero to four LIM domains, and are essential for myofibril assembly across all species analyzed so far. Drosophila melanogaster has three Alp/Enigma family members, Zasp52, Zasp66, and Zasp67. Ortholog search and phylogenetic tree analysis suggest that Zasp genes have a common ancestor, and that Zasp66 and Zasp67 arose by duplication in insects. While Zasp66 has a conserved domain structure across orthologs, Zasp67 domains and lengths are highly variable. In flies, Zasp67 appears to be expressed only in indirect flight muscles, where it colocalizes with Zasp52 at Z-discs. We generated a CRISPR null mutant of Zasp67, which is viable but flightless. We can rescue all phenotypes by re-expressing a Zasp67 transgene at endogenous levels. Zasp67 mutants show extended and broken Z-discs in adult flies, indicating that the protein helps stabilize the highly regular myofibrils of indirect flight muscles. In contrast, a Zasp66 CRISPR null mutant has limited viability, but only mild indirect flight muscle defects illustrating the diverging evolutionary paths these two paralogous genes have taken since they arose by duplication.

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The Drosophila Z-disc Protein Z(210) Is an Adult Muscle Isoform of Zasp52, Which Is Required for Normal Myofibril Organization in Indirect Flight Muscles

Cited by 15 publications

References 28 publications

Nanoscopy reveals the layered organization of the sarcomeric H-zone and I-band complexes

Nanoscopy reveals the layered organization of the sarcomeric H-zone and I-band complexes

Zasp52, a Core Z-disc Protein in Drosophila Indirect Flight Muscles, Interacts with α-Actinin via an Extended PDZ Domain

Different Evolutionary Trajectories of Two Insect-Specific Paralogous Proteins Involved in Stabilizing Muscle Myofibrils

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