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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Tropomodulin 1

tropomodulin, erythrocyte tropomodulin, Tmod
This gene encodes a member of the tropomodulin family. The encoded protein is an actin-capping protein that regulates tropomyosin by binding to its N-terminus, inhibiting depolymerization and elongation of the pointed end of actin filaments and thereby influencing the structure of the erythrocyte membrane skeleton. Multiple transcript variants encoding the same protein have been found for this gene. [provided by RefSeq, Oct 2009] (from NCBI)
Top mentioned proteins: Actin, TM3, CAN, CAPS, fibrillin-1
Papers on tropomodulin
Development of qualitative and quantitative PCR analysis for meat adulteration from RNA samples.
New
Sheu et al., Kao-hsiung, Taiwan. In Food Chem, Mar 2016
The primers were designed based on the mRNA sequences of troponin I (TnI), mitochondrial ribosomal protein (MRP) and tropomodulin genes to distinguish chicken, pork, goat, beef and ostrich.
Tropomodulin 1 directly controls thin filament length in both wild-type and tropomodulin 4-deficient skeletal muscle.
New
Fowler et al., Chicago, United States. In Development, Jan 2016
The sarcomeric tropomodulin (Tmod) isoforms Tmod1 and Tmod4 cap thin filament pointed ends and functionally interact with the leiomodin (Lmod) isoforms Lmod2 and Lmod3 to control myofibril organization, thin filament lengths, and actomyosin crossbridge formation in skeletal muscle fibers.
Quantitative proteomics reveals differential regulation of protein expression in recipient myocardium after trilineage cardiovascular cell transplantation.
New
Ge et al., Madison, United States. In Proteomics, Aug 2015
Among them, 12 proteins, including adenylyl cyclase-associated protein 1 and tropomodulin-1, are associated with positive regulation of muscular contraction whereas 11 proteins, such as desmoplakin and zyxin, are involved in embryonic and muscular development and regeneration.
Regulation of actin polymerization by tropomodulin-3 controls megakaryocyte actin organization and platelet biogenesis.
New
Fowler et al., Los Angeles, United States. In Blood, Aug 2015
Tropomodulin-3 (Tmod3), the only Tmod isoform detected in platelets and megakaryocytes (MKs), caps actin filament (F-actin) pointed ends and binds tropomyosins (TMs), regulating actin polymerization and stability.
Fluid Shear Stress Upregulates E-Tmod41 via miR-23b-3p and Contributes to F-Actin Cytoskeleton Remodeling during Erythropoiesis.
Yao et al., Beijing, China. In Plos One, 2014
Erythrocyte tropomodulin of 41 kDa (E-Tmod41) caps the pointed end of actin filament (F-actin) and is critical for the formation of hexagonal topology of erythrocyte membrane skeleton.
Mechanism of actin filament pointed-end capping by tropomodulin.
Impact
Dominguez et al., Philadelphia, United States. In Science, 2014
Whereas several proteins cap the rapidly growing barbed end, tropomodulin (Tmod) is the only protein known to cap the slowly growing pointed end.
Tropomodulins and tropomyosins: working as a team.
Review
Kostyukova et al., Pullman, United States. In J Muscle Res Cell Motil, 2013
Actin filament length is optimized by tropomodulin (Tmod), which caps the slow growing (pointed end) of thin filaments to inhibit polymerization or depolymerization.
Periodicities designed in the tropomyosin sequence and structure define its functions.
Review
Barua, United States. In Bioarchitecture, 2013
Tropomyosin is an actin binding protein that regulates actin filament dynamics and its interactions with actin binding proteins such as myosin, tropomodulin, formin, Arp2/3 and ADF-cofilin in most eukaryotic cells.
Tropomodulin 1 constrains fiber cell geometry during elongation and maturation in the lens cortex.
GeneRIF
Fowler et al., Los Angeles, United States. In J Histochem Cytochem, 2012
Tropomodulin 1 constrains fiber cell geometry during elongation and maturation in the lens cortex.
Tropomodulins: pointed-end capping proteins that regulate actin filament architecture in diverse cell types.
Review
Fowler et al., Los Angeles, United States. In Cytoskeleton (hoboken), 2012
By understanding Tmods' functions in the context of their molecular structure, actin regulation, binding partners, and related variants (leiomodins 1-3), we can draw broad conclusions that can explain the diverse morphological and functional phenotypes that arise from Tmod perturbation experiments in vitro and in vivo.
Cytoplasmic gamma-actin and tropomodulin isoforms link to the sarcoplasmic reticulum in skeletal muscle fibers.
GeneRIF
Fowler et al., Los Angeles, United States. In J Cell Biol, 2011
The Tmod1 deletion caused Tmod3 to leave its SR compartment, leading to mislocalization and destabilization of the Tmod3-gamma(cyto)-actin-sAnk1.5 complex.
[The capping protein on the slow-growing end of actin filament: erythrocyte tropomodulin].
Review
Yao et al., Beijing, China. In Sheng Li Ke Xue Jin Zhan, 2011
Erythrocyte tropomodulin (E-Tmod) is first isolated from human erythrocyte membrane as a TM-binding protein.
Identification of residues within tropomodulin-1 responsible for its localization at the pointed ends of the actin filaments in cardiac myocytes.
GeneRIF
Kostyukova et al., Tucson, United States. In J Biol Chem, 2011
Identification of residues within tropomodulin-1 responsible for its localization at the pointed ends of the actin filaments in cardiac myocytes.
Tropomodulin capping of actin filaments in striated muscle development and physiology.
Review
Fowler et al., Los Angeles, United States. In J Biomed Biotechnol, 2010
We first describe the mechanisms by which Tmods regulate myofibril assembly and thin filament lengths, as well as the roles of closely related Tmod family variants, the leiomodins (Lmods), in these processes.
Erythrocyte tropomodulin isoforms with and without the N-terminal actin-binding domain.
GeneRIF
Sung et al., San Diego, United States. In J Biol Chem, 2010
Erythrocyte tropomodulin isoforms with and without the N-terminal actin-binding domain.
Different localizations and cellular behaviors of leiomodin and tropomodulin in mature cardiomyocyte sarcomeres.
GeneRIF
Lappalainen et al., Helsinki, Finland. In Mol Biol Cell, 2010
Lmod contributes to the final organization and maintenance of sarcomere architecture by promoting tropomyosin-dependent actin filament nucleation.
Leiomodin is an actin filament nucleator in muscle cells.
Impact
Dominguez et al., Watertown, United States. In Science, 2008
Leiomodin shared two actin-binding sites with the filament pointed end-capping protein tropomodulin: a flexible N-terminal region and a leucine-rich repeat domain.
Tropomyosin-based regulation of the actin cytoskeleton in time and space.
Review
Impact
Hardeman et al., Westmead, Australia. In Physiol Rev, 2008
The functional specificity of tropomyosins is related to the collaborative interactions of the isoforms with different actin binding proteins such as cofilin, gelsolin, Arp 2/3, myosin, caldesmon, and tropomodulin.
Actin binding proteins: regulation of cytoskeletal microfilaments.
Review
Impact
Nosworthy et al., Sydney, Australia. In Physiol Rev, 2003
In this review we selected several ABPs (ADF/cofilin, profilin, gelsolin, thymosin beta4, DNase I, CapZ, tropomodulin, and Arp2/3) that regulate actin-driven assembly, i.e., movement that is independent of motor proteins.
Actin dynamics at pointed ends regulates thin filament length in striated muscle.
Impact
Fowler et al., Los Angeles, United States. In Nat Cell Biol, 2001
In striated muscle, it is believed that tight capping of the fast-growing (barbed) ends by CapZ and of the slow-growing (pointed) ends by tropomodulin (Tmod) stabilizes the uniform lengths of actin (thin) filaments in myofibrils.
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