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Gene Review:

VLN1 - villin-1

Arabidopsis thaliana

Synonyms: ATVLN1, F6K5.2, F6K5_2, villin 1, villin-like 1

Huang, S. et al., Yokota, E. et al., Klahre, U. et al.

Yokota, Vidali, Tominaga, Tahara, Orii, Morizane, Hepler, Shimmen,

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High impact information on VLN1

VILLIN1 (VLN1) has the least well-conserved type 1 and type 2 calcium binding sites among the Arabidopsis VILLIN isoforms [1].
These results suggest that AtVLNs have less-specialized functions than mammalian villin, which is found only in the microvilli of brush border cells [2].
In root hair cells of Hydrocharis dubia, this type of plant villin was co-localized with actin-filament bundles in the transvacuolar strands and the sub-cortical regions [3].

Analytical, diagnostic and therapeutic context of VLN1

Here we have identified a putative calcium-insensitive villin isoform through comparison of sequence alignments between human gelsolin and plant villins with x-ray crystallography data for vertebrate gelsolin [1].

References

Arabidopsis VILLIN1 generates actin filament cables that are resistant to depolymerization. Huang, S., Robinson, R.C., Gao, L.Y., Matsumoto, T., Brunet, A., Blanchoin, L., Staiger, C.J. Plant Cell (2005) [Pubmed]
Villin-like actin-binding proteins are expressed ubiquitously in Arabidopsis. Klahre, U., Friederich, E., Kost, B., Louvard, D., Chua, N.H. Plant Physiol. (2000) [Pubmed]
Plant 115-kDa actin-filament bundling protein, P-115-ABP, is a homologue of plant villin and is widely distributed in cells. Yokota, E., Vidali, L., Tominaga, M., Tahara, H., Orii, H., Morizane, Y., Hepler, P.K., Shimmen, T. Plant Cell Physiol. (2003) [Pubmed]

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