Katarzyna Robaszkiewicz
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View article: Tropomyosin isoforms encoded by TPM2 control the actin-bundling activity of fascin-1
Tropomyosin isoforms encoded by TPM2 control the actin-bundling activity of fascin-1 Open
Background In many types of tumors, the expression patterns of actin-binding proteins –fascin-1 and various isoforms of tropomyosin – are altered. Fascin-1 is an actin-bundling protein that promotes cancer cell motility, whereas tropomyosi…
View article: Myopathy‐linked mutations in <i>TPM2</i> and their impact on troponin‐mediated regulation of actomyosin contractility
Myopathy‐linked mutations in <i>TPM2</i> and their impact on troponin‐mediated regulation of actomyosin contractility Open
In striated muscle, the regulatory complex of tropomyosin (Tpm) and troponin (Tn) governs the Ca 2+ ‐dependent interactions between myosin heads and actin, controlling muscle contraction. The N‐terminal and central regions of Tpm are cruci…
View article: Annexin <scp>A2</scp> Contributes to Release of Extracellular Vimentin in Response to Inflammation
Annexin <span>A2</span> Contributes to Release of Extracellular Vimentin in Response to Inflammation Open
Vimentin, an abundant intracellular cytoskeletal protein, is secreted into the extracellular space, where it can amplify tissue destruction in inflammatory diseases. The mechanisms by which inflammation promotes the release of extracellula…
View article: Mechanochemical consequences of myopathy‐linked mutations in Tpm2.2 on striated muscle contractility
Mechanochemical consequences of myopathy‐linked mutations in Tpm2.2 on striated muscle contractility Open
Tropomyosin (Tpm) is an actin‐binding protein central to muscle contraction regulation. The Tpm sequence consists of periodic repeats corresponding to seven actin‐binding sites, further divided in two functionally distinct halves. To clari…
View article: Troponin and a Myopathy-Linked Mutation in TPM3 Inhibit Cofilin-2-Induced Thin Filament Depolymerization
Troponin and a Myopathy-Linked Mutation in TPM3 Inhibit Cofilin-2-Induced Thin Filament Depolymerization Open
Uniform actin filament length is required for synchronized contraction of skeletal muscle. In myopathies linked to mutations in tropomyosin (Tpm) genes, irregular thin filaments are a common feature, which may result from defects in length…
View article: A Novel Variant in TPM3 Causing Muscle Weakness and Concomitant Hypercontractile Phenotype
A Novel Variant in TPM3 Causing Muscle Weakness and Concomitant Hypercontractile Phenotype Open
A novel variant of unknown significance c.8A > G (p.Glu3Gly) in TPM3 was detected in two unrelated families. TPM3 encodes the transcript variant Tpm3.12 (NM_152263.4), the tropomyosin isoform specifically expressed in slow skeletal muscle …
View article: Ca2+-dependent binding of S100A6 to cofilin-1 regulates actin filament polymerization-depolymerization dynamics
Ca2+-dependent binding of S100A6 to cofilin-1 regulates actin filament polymerization-depolymerization dynamics Open
S100A6 is a Ca2+-binding protein belonging to the S100 family. Many reports indicate that S100A6 is involved in actin filament organization, however the mechanism of S100A6 action in this process is not fully understood. By scre…
View article: Mutations Q93H and E97K in TPM2 Disrupt Ca-Dependent Regulation of Actin Filaments
Mutations Q93H and E97K in TPM2 Disrupt Ca-Dependent Regulation of Actin Filaments Open
Tropomyosin is a two-chain coiled coil protein, which together with the troponin complex controls interactions of actin with myosin in a Ca2+-dependent manner. In fast skeletal muscle, the contractile actin filaments are regulated by tropo…
View article: Binding of S100A6 to actin and the actin–tropomyosin complex
Binding of S100A6 to actin and the actin–tropomyosin complex Open
S100A6 is a low molecular weight Ca 2+ -binding protein belonging to the S100 family. Many reports indicate that in the cell S100A6 has an influence on the organization of actin filaments, but so far no direct interaction between S100A6 an…
View article: Regulation of Actin Filament Length by Muscle Isoforms of Tropomyosin and Cofilin
Regulation of Actin Filament Length by Muscle Isoforms of Tropomyosin and Cofilin Open
In striated muscle the extent of the overlap between actin and myosin filaments contributes to the development of force. In slow twitch muscle fibers actin filaments are longer than in fast twitch fibers, but the mechanism which determines…
View article: Congenital myopathy‐related mutations in tropomyosin disrupt regulatory function through altered actin affinity and tropomodulin binding
Congenital myopathy‐related mutations in tropomyosin disrupt regulatory function through altered actin affinity and tropomodulin binding Open
Tropomyosin (Tpm) binds along actin filaments and regulates myosin binding to control muscle contraction. Tropomodulin binds to the pointed end of a filament and regulates actin dynamics, which maintains the length of a thin filament. To d…
View article: Tropomyosin isoforms differentially modulate the regulation of actin filament polymerization and depolymerization by cofilins
Tropomyosin isoforms differentially modulate the regulation of actin filament polymerization and depolymerization by cofilins Open
The specific functions of actin filaments located in the contractile and cytoskeletal compartments of muscle cells depend on the stability and dynamic polymerization/depolymerization of filaments. Tropomyosins and cofilins control the leng…