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Gene Review

PRF5  -  profilin 5

Arabidopsis thaliana

Synonyms: F6F22.20, F6F22_20
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High impact information on PRF5

  • The diverse cellular functions of the actin cytoskeleton are mediated by actin-binding proteins that nucleate, destabilize, and bundle actin filaments [1].
  • These second messengers might influence the actin cytoskeleton through known interactions with actin-binding proteins [2].
  • Analysis of pfn promoter-GUS fusion genes in transgenic Arabidopsis shows that pfn2 is specifically expressed in the vascular bundles of roots, hypocotyls, cotyledons, leaves, sepals, petals, stamen filaments and stalks of developing seeds, whereas expression of pfn4 is restricted to mature and germinating pollen grains [3].
  • Actin-binding proteins in the Arabidopsis genome database: properties of functionally distinct plant actin-depolymerizing factors/cofilins [4].
  • This structure is stimulus responsive, being affected by internal stimuli, by biotic and abiotic stresses mediated in signal transduction pathways by actin-binding proteins [4].

Biological context of PRF5

  • Changes in the cellular architecture are often assumed to require actin-binding proteins as stimulus-response modulators, because many of these proteins are regulated directly by binding to intracellular second messengers or signaling phospholipids [5].
  • The completion of the Arabidopsis genome sequence has allowed a comparative identification of many actin-binding proteins [4].
  • The result is in agreement with observations made with several mutant profilins and provides strong evidence for two regions on mammalian profilin mediating electrostatic interaction with phosphatidylinositol lipids; one close to the binding site for poly(L-proline), and one partially overlapping with the actin-binding surface [6].

Anatomical context of PRF5


Other interactions of PRF5


Analytical, diagnostic and therapeutic context of PRF5

  • Superposition of the four AC isoform structures permits an accurate sequence alignment that differs from previously reported data for the location of vertebrate-specific inserts and reveals a contiguous, vertebrate-specific surface opposite the putative actin-binding surface [11].


  1. Breaking the WAVE complex: the point of Arabidopsis trichomes. Szymanski, D.B. Curr. Opin. Plant Biol. (2005) [Pubmed]
  2. Signalling by tips. Feijó, J.A., Costa, S.S., Prado, A.M., Becker, J.D., Certal, A.C. Curr. Opin. Plant Biol. (2004) [Pubmed]
  3. Arabidopsis profilins are functionally similar to yeast profilins: identification of a vascular bundle-specific profilin and a pollen-specific profilin. Christensen, H.E., Ramachandran, S., Tan, C.T., Surana, U., Dong, C.H., Chua, N.H. Plant J. (1996) [Pubmed]
  4. Actin-binding proteins in the Arabidopsis genome database: properties of functionally distinct plant actin-depolymerizing factors/cofilins. Hussey, P.J., Allwood, E.G., Smertenko, A.P. Philos. Trans. R. Soc. Lond., B, Biol. Sci. (2002) [Pubmed]
  5. Heterodimeric capping protein from Arabidopsis is regulated by phosphatidic acid. Huang, S., Gao, L., Blanchoin, L., Staiger, C.J. Mol. Biol. Cell (2006) [Pubmed]
  6. Evidence for two interaction regions for phosphatidylinositol(4,5)-bisphosphate on mammalian profilin I. Skare, P., Karlsson, R. FEBS Lett. (2002) [Pubmed]
  7. Arabidopsis group Ie formins localize to specific cell membrane domains, interact with actin-binding proteins and cause defects in cell expansion upon aberrant expression. Deeks, M.J., Cvrcková, F., Machesky, L.M., Mikitová, V., Ketelaar, T., Zársky, V., Davies, B., Hussey, P.J. New Phytol. (2005) [Pubmed]
  8. Profilin plays a role in cell elongation, cell shape maintenance, and flowering in Arabidopsis. Ramachandran, S., Christensen, H.E., Ishimaru, Y., Dong, C.H., Chao-Ming, W., Cleary, A.L., Chua, N.H. Plant Physiol. (2000) [Pubmed]
  9. In vivo analysis of interactions between GFP-labeled microfilaments and plastid stromules. Kwok, E.Y., Hanson, M.R. BMC Plant Biol. (2004) [Pubmed]
  10. Molecular cloning and mRNA localization of tomato pollen profilin. Yu, L.X., Nasrallah, J., Valenta, R., Parthasarathy, M.V. Plant Mol. Biol. (1998) [Pubmed]
  11. A comparative structural analysis of the ADF/cofilin family. Bowman, G.D., Nodelman, I.M., Hong, Y., Chua, N.H., Lindberg, U., Schutt, C.E. Proteins (2000) [Pubmed]
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