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Gene Review

PLS1  -  plastin 1

Gallus gallus

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Disease relevance of PLS1

  • During recovery of the BP following acoustic trauma, the appearance of fimbrin in regenerating hair cells was first seen approximately 96 h after the onset of the sound exposure [1].
  • These five serovars and a single isolate of S. typhi (D1) were also detected by hybridization of genomic DNA from 732 Salmonella isolates of 117 serogroups to gene probes derived from the S. enteritidis sefA (fimbrin gene), sefB (chaperone) or sefC (outer membrane protein) genes encoding proteins involved in SEF14 biosynthesis [2].
  • DNA sequence of type 1 fimbrin, Fpul1, gene from a chicken pathogenic Escherichia coli serotype O78 [3].

High impact information on PLS1

  • Role of fimbrin and villin in determining the interfilament distances of actin bundles [4].
  • Thus fimbrin appears to be responsible for paracrystallin packing of actin filaments in stereocillia; an isoform of spectrin resides in the cuticular plate where it forms the whisker-like crossbridges, and alpha actinin is the actin crosslinking protein of the circumferential ZA bundle [5].
  • Fimbrin is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia [6].
  • The differences in expression, sequence, and phosphorylation suggest possible functional differences between fimbrin isoforms [6].
  • Because the actin filaments in the stereocilia of hair borders still remain as compact bundles, albeit very disordered, there must be an additional uncharacterized protein besides fimbrin that cross-links the actin filaments together [7].

Biological context of PLS1


Anatomical context of PLS1


Associations of PLS1 with chemical compounds

  • In reconstitution experiments, actin filaments incubated in EGTA with purified fimbrin and villin form smooth-sided bundles containing an apparently random number of filaments [12].
  • The iron chelator desferrioxamine (100 microM) in vitro prevented the aminoglycoside-induced reduction in relative expression of mRNA for both fimbrin and class III beta-tubulin [13].

Other interactions of PLS1

  • Actin filaments within the stereocilia are cross-linked by fimbrin, but this did not appear to interfere with the motility of myosin [14].
  • In view of recent studies showing that L-plastin, the leukocyte homolog of fimbrin, has a higher binding affinity for beta-actin than for gamma-actin, a mechanism is proposed for how hair cells might restrict formation of actin filament bundles to a single cellular site (i.e. the stereocilia) [15].
  • Moreover, the predicted structure of the calponin CH domain is identical to that found by X-ray studies of the spectrin, fimbrin and utrophin CH domains [16].

Analytical, diagnostic and therapeutic context of PLS1


  1. Localization of the hair-cell-specific protein fimbrin during regeneration in the chicken cochlea. Lee, K.H., Cotanche, D.A. Audiol. Neurootol. (1996) [Pubmed]
  2. Diagnostic potential of sefA DNA probes to Salmonella enteritidis and certain other O-serogroup D1 Salmonella serovars. Doran, J.L., Collinson, S.K., Clouthier, S.C., Cebula, T.A., Koch, W.H., Burian, J., Banser, P.A., Todd, E.C., Kay, W.W. Mol. Cell. Probes (1996) [Pubmed]
  3. DNA sequence of type 1 fimbrin, Fpul1, gene from a chicken pathogenic Escherichia coli serotype O78. Sekizaki, T., Ito, H., Asawa, T., Nonomura, I. J. Vet. Med. Sci. (1993) [Pubmed]
  4. Role of fimbrin and villin in determining the interfilament distances of actin bundles. Matsudaira, P., Mandelkow, E., Renner, W., Hesterberg, L.K., Weber, K. Nature (1983) [Pubmed]
  5. Three different actin filament assemblies occur in every hair cell: each contains a specific actin crosslinking protein. Drenckhahn, D., Engel, K., Höfer, D., Merte, C., Tilney, L., Tilney, M. J. Cell Biol. (1991) [Pubmed]
  6. Fimbrin is a homologue of the cytoplasmic phosphoprotein plastin and has domains homologous with calmodulin and actin gelation proteins. de Arruda, M.V., Watson, S., Lin, C.S., Leavitt, J., Matsudaira, P. J. Cell Biol. (1990) [Pubmed]
  7. Preliminary biochemical characterization of the stereocilia and cuticular plate of hair cells of the chick cochlea. Tilney, M.S., Tilney, L.G., Stephens, R.E., Merte, C., Drenckhahn, D., Cotanche, D.A., Bretscher, A. J. Cell Biol. (1989) [Pubmed]
  8. Microvillus assembly. Not actin alone. Fath, K.R., Burgess, D.R. Curr. Biol. (1995) [Pubmed]
  9. Fimbrin, a new microfilament-associated protein present in microvilli and other cell surface structures. Bretscher, A., Weber, K. J. Cell Biol. (1980) [Pubmed]
  10. Terminal differentiation of osteoblasts to osteocytes is accompanied by dramatic changes in the distribution of actin-binding proteins. Kamioka, H., Sugawara, Y., Honjo, T., Yamashiro, T., Takano-Yamamoto, T. J. Bone Miner. Res. (2004) [Pubmed]
  11. Osteocyte shape is dependent on actin filaments and osteocyte processes are unique actin-rich projections. Tanaka-Kamioka, K., Kamioka, H., Ris, H., Lim, S.S. J. Bone Miner. Res. (1998) [Pubmed]
  12. Reassociation of microvillar core proteins: making a microvillar core in vitro. Coluccio, L.M., Bretscher, A. J. Cell Biol. (1989) [Pubmed]
  13. Cytoskeletal protein mRNA expression in the chick utricle after treatment in vitro with aminoglycoside antibiotics: effects of insulin, iron chelators and cyclic nucleotides. Stacey, D.J., McLean, W.G. Brain Res. (2000) [Pubmed]
  14. Actin cores of hair-cell stereocilia support myosin motility. Shepherd, G.M., Corey, D.P., Block, S.M. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  15. Sorting of actin isoforms in chicken auditory hair cells. Höfer, D., Ness, W., Drenckhahn, D. J. Cell. Sci. (1997) [Pubmed]
  16. Size, shape and secondary structure of calponin. Czurylo, E.A., Eimer, W., Kulikova, N., Hellweg, T. Acta Biochim. Pol. (2000) [Pubmed]
  17. Fimbrin is a cytoskeletal protein that crosslinks F-actin in vitro. Bretscher, A. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
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