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Cofilin 2

Cofilin 2, CFL2
This gene encodes an intracellular protein that is involved in the regulation of actin-filament dynamics. This protein is a major component of intranuclear and cytoplasmic actin rods. It can bind G- and F-actin in a 1:1 ratio of cofilin to actin, and it reversibly controls actin polymerization and depolymerization in a pH-dependent manner. Mutations in this gene cause nemaline myopathy type 7, a form of congenital myopathy. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2009] (from NCBI)
Papers on Cofilin 2
Normal myofibrillar development followed by progressive sarcomeric disruption with actin accumulations in a mouse Cfl2 knockout demonstrates requirement of cofilin-2 for muscle maintenance.
GeneRIF
Beggs et al., Boston, United States. In Hum Mol Genet, 2012
cofilin-2, although not critical for muscle development, is essential for muscle maintenance.
Cofilin weakly interacts with 14-3-3 and therefore can only indirectly participate in regulation of cell motility by small heat shock protein HspB6 (Hsp20).
GeneRIF
Gusev et al., Moscow, Russia. In Arch Biochem Biophys, 2012
cofilins 1 and 2 only weakly interact with 14-3-3 and therefore cannot directly compete with phosphorylated small heat shock protein HspB6 for its binding to 14-3-3 zeta
Remodeling of actin filaments by ADF/cofilin proteins.
GeneRIF
Egelman et al., Charlottesville, United States. In Proc Natl Acad Sci U S A, 2012
the cofilin-induced change in the filament twist is due to a unique conformation of the actin molecule unrelated to any previously observed state
Differential expression of up-regulated cofilin-1 and down-regulated cofilin-2 characteristic of pancreatic cancer tissues.
GeneRIF
Nakamura et al., Ube, Japan. In Oncol Rep, 2011
Differential expression of up-regulated cofilin-1 and down-regulated cofilin-2 characteristic of pancreatic cancer tissues
Prolyl hydroxylase domain (PHD) 2 affects cell migration and F-actin formation via RhoA/rho-associated kinase-dependent cofilin phosphorylation.
GeneRIF
Katschinski et al., Göttingen, Germany. In J Biol Chem, 2010
PHD2 affects cell migration and F-actin formation via RhoA/rho-associated kinase-dependent cofilin phosphorylation
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