Filamin A Rabbit Polyclonal Antibody

Function

Caldesmon, Filamin 1, Nebulin and Villin are differentially expressed and regulated Actin binding proteins. Both muscular (CDh) and non-muscular (CDl) forms of Caldesmon have been identified and each has been shown to bind to Actin as well as to calmodulin and Myosin. CDh is expressed predominantly on thin filaments in smooth muscle, whereas CDl is widely expressed in non-muscle tissues and cells. Filamin 1, which is ubiquitously expressed and exists as a homodimer, functions to crosslink Actin to filaments. Nebulin is a large filamentous protein specific to muscle tissue that may function as a ruler for filament length. Several isoforms of Nebulin are produced by alternative exon usage. Villin is Ca2+-regulated and is the major structural component of the brush border of absorptive cells.

Background References

1. Mizuhashi K et al. Filamin-interacting proteins, Cfm1 and Cfm2, are essential for the formation of cartilaginous skeletal elements. Hum Mol Genet 23(11):2953-67 (2014).

2. Adams M et al. A meckelin-filamin A interaction mediates ciliogenesis. Hum Mol Genet 21:1272-86 (2012).

Sequence Similarity

Belongs to the filamin family.

Tissue Specificity

Ubiquitous.

Post-translational Modification

Phosphorylation at Ser-2152 is negatively regulated by the autoinhibited conformation of filamin repeats 19-21. Ligand binding induces a conformational switch triggering phosphorylation at Ser-2152 by PKA.; Phosphorylation extent changes in response to cell activation.; Polyubiquitination in the CH1 domain by a SCF-like complex containing ASB2 leads to proteasomal degradation. Prior dissociation from actin may be required to expose the target lysines. Ubiquitinated in endothelial cells by RNF213 downstream of the non-canonical Wnt signaling pathway, leading to its degradation by the proteasome.

Subcellular Location

Cytoplasm, cytoskeleton, Cell projection.

UNIPROT

SwissProt: P21333 Human

SwissProt: Q8BTM8 Mouse

Entrez Gene: 293860 Rat

Synonyms