Tropomodulin binds to filensin intermediate filaments [PDF]
Tropomodulin (Tmod) is an actin filament pointed end capping protein found in the membrane skeleton of lens fiber cells. We demonstrate that Tmod4 is able to bind the lens‐specific intermediate filament protein, filensin, in either co‐sedimentation or solid phase binding assays in a saturable fashion, but with low affinity and stoichiometry ...
Fischer, R.S. +2 more
openaire +2 more sources
Tmod3 Phosphorylation Mediates AMPK-Dependent GLUT4 Plasma Membrane Insertion in Myoblasts
Insulin and muscle contractions mediate glucose transporter 4 (GLUT4) translocation and insertion into the plasma membrane (PM) for glucose uptake in skeletal muscles.
Man Mohan Shrestha +5 more
doaj +1 more source
Effect of Chitosan Composite Preservative on Proteome Changes of Grass Carp Muscle during Cold Storage [PDF]
To explore the effect of a chitosan-based preservative solution (10 mg/mL chitosan + 5 mg/mL tea polyphenol + 2 000 U/mL lysozyme) on the change in the muscle proteome of grass carp during cold storage, differential proteomic analysis of fresh fish and ...
LI Jialei, CHEN Sai, TIAN Mingli, YU Jian, LIU Yongle, WANG Faxiang
doaj +1 more source
Proper muscle contraction requires the assembly and maintenance of sarcomeres and myofibrils. While the protein components of myofibrils are generally known, less is known about the mechanisms by which they individually function and together synergize ...
Carolina Zapater i Morales +5 more
semanticscholar +1 more source
Leiomodin creates a leaky cap at the pointed end of actin-thin filaments.
Improper lengths of actin-thin filaments are associated with altered contractile activity and lethal myopathies. Leiomodin, a member of the tropomodulin family of proteins, is critical in thin filament assembly and maintenance; however, its role is under
Dmitri Tolkatchev +7 more
doaj +1 more source
Tropomodulins are negative regulators of neurite outgrowth [PDF]
Regulation of the actin cytoskeleton is critical for neurite formation. Tropomodulins (Tmods) regulate polymerization at actin filament pointed ends. Previous experiments using a mouse model deficient for the neuron specific isoform Tmod2 suggested a role for Tmods in neuronal function by impacting processes underlying learning and memory. However, the
Fath, T. +4 more
openaire +3 more sources
Plasmodium falciparum ligand binding to erythrocytes induce alterations in deformability essential for invasion [PDF]
The most lethal form of malaria in humans is caused by Plasmodium falciparum. These parasites invade erythrocytes, a complex process involving multiple ligand-receptor interactions.
Cowman, Alan +12 more
core +2 more sources
Tropomodulins and tropomyosins: working as a team [PDF]
Actin filaments are major components of the cytoskeleton in eukaryotic cells and are involved in vital cellular functions such as cell motility and muscle contraction. Tmod and TM are crucial constituents of the actin filament network, making their presence indispensable in living cells.
Colpan, Mert +2 more
openaire +3 more sources
The transcriptional profile of iron deficiency in patients with heart failure: Heme-sparing and reduced immune processes. [PDF]
The analysis workflow, findings and potential clinical consequences of iron deficiency in heart failure (HF). From 881 patients with worsening HF, whole blood transcriptome was analysed using the Affymetrix Human Transcriptome Array (HTA) 2.0. Subjects were stratified according to their transferrin saturation (TSAT) levels as iron‐deficient (TSAT <20%)
Grote Beverborg N +17 more
europepmc +2 more sources
Functions of actin‐binding proteins in cilia structure remodeling and signaling
Wang et al. review recent progresses about roles of actin‐binding proteins (ABPs) in the regulation of cilia morphology and signaling including TGF‐β, Wnt, and Hedgehog signaling pathways. The dysregulation of ciliogenesis and ciliary signaling are closely linked with cilia‐related diseases such as polycystic kidney disease (PKD) and myocardial ...
Siqi Wang +9 more
wiley +1 more source

