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Cofilin 2
Cofilin 2 (muscle) also known as CFL2 is a protein which in humans is encoded by the ''CFL2'' gene. Function Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. Cofilin-2 is a member of the AC group of proteins that also includes cofilin-1 ( CFL1) and destrin (DSTN), all of which regulate actin-filament dynamics. The CFL2 gene encodes a skeletal muscle-specific isoform localized to the thin filaments, where it exerts its effect on actin, in part through interactions with tropomyosins. Clinical significance Mutations in the ''CFL2'' gene are associated with nemaline myopathy Nemaline myopathy (also called rod myopathy or nemaline rod myopathy) is a congenital, often hereditary neuromuscular disorder with many symptoms that can occur such as muscle weakness, hypoventilation, swallowing dysfunction, and impaired speech .... Deficiency ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid ...
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Cofilin
ADF/cofilin is a family of actin-binding proteins associated with the rapid depolymerization of actin microfilaments that give actin its characteristic dynamic instability. This dynamic instability is central to actin's role in muscle contraction, cell motility and transcription regulation. Three highly conserved and highly (70%-82%) identical genes belonging to this family have been described in humans and mice: * CFL1, coding for cofilin 1 (non-muscle, or n-cofilin) * CFL2, coding for cofilin 2 (found in muscle: m-cofilin) * DSTN, coding for destrin, also known as ADF or actin depolymerizing factor Actin-binding proteins regulate assembly and disassembly of actin filaments.Cooper, G. M. and R. E. Hausman. ''The Cell: A Molecular Approach,'' 3rd ed. Washington DC: ASM Press 2004 pp.436-440. Cofilin, a member of the ADF/cofilin family is actually a protein with 70% sequence identity to destrin, making it part of the ADF/cofilin family of small ADP-binding proteins. The prote ...
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Actin
Actin is a family of globular multi-functional proteins that form microfilaments in the cytoskeleton, and the thin filaments in muscle fibrils. It is found in essentially all eukaryotic cells, where it may be present at a concentration of over 100 μM; its mass is roughly 42 kDa, with a diameter of 4 to 7 nm. An actin protein is the monomeric subunit of two types of filaments in cells: microfilaments, one of the three major components of the cytoskeleton, and thin filaments, part of the contractile apparatus in muscle cells. It can be present as either a free monomer called G-actin (globular) or as part of a linear polymer microfilament called F-actin (filamentous), both of which are essential for such important cellular functions as the mobility and contraction of cells during cell division. Actin participates in many important cellular processes, including muscle contraction, cell motility, cell division and cytokinesis, vesicle and organelle movement ...
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CFL1
Cofilin 1 (non-muscle; n-cofilin), also known as CFL1, is a human gene, part of the ADF/cofilin family. Cofilin is a widely distributed intracellular actin-modulating protein that binds and depolymerizes filamentous F-actin and inhibits the polymerization of monomeric G-actin in a pH-dependent manner. It is involved in the translocation of actin-cofilin complex from cytoplasm to nucleus. One group reports that reelin signaling leads to serine3-phosphorylation of cofilin-1, and this interaction may play a role in the reelin-related regulation of neuronal migration. Interactions Cofilin 1 has been shown to interact with HSPH1 and LIMK1 LIM domain kinase 1 is an enzyme that in humans is encoded by the ''LIMK1'' gene. Function There are approximately 40 known eukaryotic LIM proteins, so named for the LIM domains they contain. LIM domains are highly conserved cysteine-rich struc .... References Further reading

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Destrin
Destrin or DSTN (also known as actin depolymerizing factor or ADF) is a protein which in humans is encoded by the ''DSTN'' gene. Destrin is a component protein in microfilaments. The product of this gene belongs to the actin-binding proteins ADF (Actin-Depolymerizing Factor)/cofilin family. This family of proteins is responsible for enhancing the turnover rate of actin in vivo. This gene encodes the actin depolymerizing protein that severs actin filaments (F-actin) and binds to actin monomers (G-actin). Two transcript variants encoding distinct isoforms have been identified for this gene. Structure The tertiary structure of destrin was determined by the use of triple-resonance multidimensional nuclear magnetic resonance, NMR. The secondary and tertiary structures of destrin are similar to the gelsolin family which is another actin-regulating protein family. There are three ordered layers to destrin which is a globular protein. There is a central β sheet that is composed of one ...
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