High impact information on Twf1

• Previous studies suggested that these mammalian proteins were tyrosine kinases, and therefore they were named A6 protein tyrosine kinase [1].
• Here we show that this protein, which we named twinfilin-2, is indeed an actin monomer-binding protein [2].
• Formins are defined by a Formin Homology 2 (FH2) domain, as well as a proline-rich FH1 domain that binds the actin monomer binding protein, profilin, and other ligands [3].
• Profilin is an ubiquitous 12-15-kDa actin monomer-binding protein, the amino acid sequence of which was previously reported for the cow and Acanthamoeba [4].
• We find that the coactosin structure is homologous to ADF/cofilin and to the ADF-H domains of twinfilin [5].

Biological context of Twf1

• The identification of a potential actin/phosphoinositide binding domain and consensus phosphorylation sites, coupled with A6's expression in a variety of cell types suggest that the A6 gene product may play a role in basic cellular processes [6].
• Here, we isolated a mouse A6 cDNA clone from a murine myeloid progenitor 32D cell library using a 1.1 kb cDNA probe containing the entire human A6 open reading frame (ORF) [6].

Anatomical context of Twf1

• Northern blot analysis of total RNA from mouse cell lines derived from diverse tissues including NIH 3T3 fibroblasts, L cell fibroblasts, C2C12 myoblasts, M1 myeloblasts, BALB/MK cells, 70Z/3 preB lymphocytes, and p388D1 monocytes demonstrated widespread A6 mRNA expression [6].

Other interactions of Twf1

• In vitro translation, as well as immunoprecipitation of 32D cell lysates confirmed expression of mouse A6 as a 40 kDa protein [6].

References