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- Table of Contents
3 Q&As
Facts about Cofilin-2.
It has the ability to bind G- and F-actin in a 1:1 ratio of cofilin to actin. It's the major component of intranuclear and cytoplasmic actin rods.
Human | |
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Gene Name: | CFL2 |
Uniprot: | Q9Y281 |
Entrez: | 1073 |
Belongs to: |
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actin-binding proteins ADF family |
cofilin 2 (muscle); Cofilin, muscle isoform; cofilin-2; NEM7
Mass (kDA):
18.737 kDA
Human | |
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Location: | 14q13.1 |
Sequence: | 14; NC_000014.9 (34709113..34714823, complement) |
Isoform CFL2b is expressed predominantly in skeletal muscle and heart. Isoform CFL2a is expressed in various tissues.
Nucleus matrix. Cytoplasm, cytoskeleton. Colocalizes with CSPR3 in the Z line of sarcomeres.
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If you're looking for a high-quality antibody to target cofilin-2, the Boster Bio Anti-Cofilin 2/CFL2-Marker may be your answer. Boster Bio products are cross-reactive with Human, Mouse, and Rat. The boster bio anti-Cofilin 2/CFL2 antibody contains Trehalose, NaCl, and Na2HPO4.
Cofilin pathology alters myocardial contractility through a triple mechanism. It may alter sarcomeric structure and function, gain PAO toxicity, or lose mechanical integrity. In addition, other misfolded prone proteins may affect myocardial contractility. For this reason, Cofilin 2 is a particularly useful marker in identifying cofilin-related diseases.
Cofilin is a member of the actin-binding protein family. It plays an essential role in depolymerization of actin filaments and has a higher affinity for ATP-actin monomers than cofilin-1. It also regulates ATP-G-actin pools by recycling older ADP-F-actin and recycling old ADP-F-actin.
Cofilin-2 is a highly abundant protein in human myocardium and can be detected in tumor samples using SDS-PAGE. However, cofilin-1 is also overexpressed in some tumors. Although few studies have documented altered expression levels of cofilin, this protein is involved in actin filament remodeling and is directly involved in chemotaxis, migration, and metastasis.
The activity of cofilin is controlled by phosphorylation of ser3 in the protein. Both phosphorylation and dephosphorylation in cofilin regulate its ability to bind actin. The phosphorylation of cofilin-2 in donor and iDCM tissue is a consequence of a defect in cofilin structure and function. In iDCM, this protein is increased in the PAOs complex and causes nemaline myopathy.
ARP2/3 is a family of kinases that regulate the actin cytoskeleton. It binds to F-actin and nucleates daughter filaments, which in turn generate dendritic networks at the leading edge of migratory cells. It also interacts with CAPZ, which inhibits filament assembly. In addition to actin fibers, cofilin is also involved in cell adhesion and disassembly.
Cofilin is a member of the actin network and is known to play a role in neurodegenerative disorders as well as nemaline myopathy. Moreover, it promotes translocation of Bax to mitochondria and activates the cell death pathway. Phosphorylation of cofilin-2 impairs cell clearance, interfering with its beneficial effects on cellular survival. Cofilin pattern may contribute to cardiomyopathy. This abnormal pattern of cofilin can affect tissue remodeling and the ability of the cardiomyocyte to respond to stress.
The CFL2 gene polymorphisms are associated with growth traits and body mass in cattle from the QC population. The polymorphisms are structural and functional, suggesting that they could be used as genetic markers to breed new cattle. This marker also demonstrates the ability to detect novel mutations. However, further validation is necessary to confirm that it is a useful marker. Therefore, the QC breeders must validate it first to confirm its usefulness.
Although CFL2 is structurally and functionally distinct from cofilin, the gene is functionally similar to both. Further research is needed to determine the functional mechanisms and biological activities of CFL2 variants. In addition, further study is needed to determine whether the CFL2 gene has negative consequences or positive consequences. Nonetheless, the CFL2 gene is an important genetic marker for skeletal muscle disease. If successful, the CFL2 gene will be useful for marker-assisted selection in both positive and negative conditions.
Molecular genetic markers, such as the CFL2 gene, are useful for quantitative traits analysis. The CFL2 nucleotide polymorphism is relevant to Qinchuan Cattle growth traits, and therefore, its use as a molecular genetic marker is beneficial for evaluating breeding values and improving selection efficiency. Mononucleotide polymorphisms are easily detected by RFLP-PCR, a simple and cost-effective method for DNA analysis.
The gene product CFL2a is found in various tissues, although it is mainly present in mature skeletal muscle. It has various functions in the body, including binding filamentous F-actin and inhibiting the polymerization of monomeric G-actin. Other CFL interactions include tropomyosins and AMPKa1.
The CFL2 gene is the target gene for miR-429-3p, and its 3'UTR contains a specific binding site for miR-429-3p. To confirm the CFL2 mRNA-targeting miR, pmirGLO-CFL2wt or pmirGLO-CFL2mut cells were co-transfected with 200 nM of scRNA. Luciferase reporter assays were performed 24 h after transfection with 200 nM of scRNA. CFL2 expression levels were determined by quantitative real-time PCR.
Transient transfection of CFL2 siRNA is a simple method for knocking down CFL2 gene expression in differentiated cells. Transfection of CFL2 siRNA with liposomes at 50% confluence was highly effective. Western blot analysis and reverse transcription-quantitative polymerase chain reaction confirmed that the siRNA was highly effective in suppressing CFL2 expression. In addition, single cells were screened with 500 ug/ml G418 to confirm the presence of CFL2 protein.
Transfection of CFL2 with MyHC cells reduced MyHC expression. Transfection of CFL2-transfected cells with 2% horse serum did not affect CFL2 mRNA or protein expression. Transfection of CFL2-transfected cells did not affect the expression of MyHC in undifferentiated cells. As a result, CFL2 may be important for the regulation of MyHC in undifferentiated cells.
In skeletal muscle, the cofilin 2 (CFL2) gene regulates actin dynamics and myogenesis. Expression of CFL2 is tightly linked to skeletal myogenesis and cell proliferation, and knocking down cofilin 2 in mice results in an abnormal sarcomere architecture and accumulation of F-actin. Therefore, CFL2 is an essential regulator of myogenic differentiation. The gene encodes two protein variants, cofilin 1a and cofilin 2, which can affect cell proliferation.
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PMID: 11422377 by Thirion C., et al. Characterization of human muscle type cofilin (CFL2) in normal and regenerating muscle.
PMID: 19752190 by Papalouka V., et al. Muscle LIM protein interacts with cofilin 2 and regulates F-actin dynamics in cardiac and skeletal muscle.