The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

Gsn  -  gelsolin

Rattus norvegicus

Synonyms: ADF, Actin-depolymerizing factor, Brevin, Gelsolin
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of Gsn

  • Unphosphorylated gelsolin is localized in regions of cell-substratum contact or attachment in Rous sarcoma virus-transformed rat cells [1].
  • Cells of the neuronal lineage play a major role in the generation of amyloid precursor fragments in gelsolin-related amyloidosis [2].

High impact information on Gsn

  • Caspase-3 cleaves several essential downstream substrates involved in the expression of the apoptotic phenotype in vitro, including gelsolin, PAK2, fodrin, nuclear lamins and the inhibitory subunit of DNA fragmentation factor [3].
  • By immunogold labeling, we demonstrate that "millipede-like" structures seen previously in mammalian cell cytoskeletons after removal of actin by treatment with gelsolin are composed of the cores of vimentin IFs with sidearms containing plectin [4].
  • The association of IFs with stress fibers survived actin depletion by gelsolin suggesting that myosin II minifilaments or components closely associated with them may play a role as plectin targets [4].
  • In this study, we examined the role of actin filaments in regulated exocytosis by introducing highly specific actin monomer-binding proteins, the beta-thymosins or a gelsolin fragment, into streptolysin O-permeabilized pancreatic acinar cells [5].
  • 5. Using a sedimentation binding assay that uses gelsolin to shorten actin filaments and render membrane binding saturable (Schwartz, M. A., and E. J. Luna. 1986. J. Cell Biol. 102:2067-2075), we found that membranes stripped of endogenous actin bound 125I-actin in a specific and saturable manner [6].

Biological context of Gsn

  • Using the epididymis as a model system in which luminal acidification is crucial for sperm maturation and storage, we now report that modulation of the actin cytoskeleton by the calcium-activated actin-capping and -severing protein gelsolin plays a key role in regulating vacuolar H(+)-ATPase (V-ATPase) recycling [7].
  • We present a model for the disassembly of the actin layer of the adhesion complex that involves the hydrolysis of PtdIns(4,5)P(2) resulting in the release of gelsolin within the plaque [8].
  • Aging-associated increase of gelsolin for apoptosis resistance [9].
  • Thus, we tested the sensitivity of senescent cells to apoptosis by menadione, an apoptosis-inducing agent, before and after the down-regulation of gelsolin [9].
  • The ubiquitous increase of gelsolin in the aged organs and cells led us to assume that it might be related with one of the cardinal senescent phenotypes, aging-associated apoptosis resistency [9].

Anatomical context of Gsn


Associations of Gsn with chemical compounds

  • Thus, maintenance of the actin cytoskeleton in a depolymerized state by gelsolin facilitates calcium-dependent apical accumulation of V-ATPase in response to luminal pH alkalinization [7].
  • When jasplakinolide was used to overcome the severing action of gelsolin by polymerizing actin, complete inhibition of the alkaline pH- and cAMP-induced apical membrane accumulation of V-ATPase was observed [7].
  • This Ca(2+) surge would facilitate the actin severing function of gelsolin within the adhesion complex [8].
  • Thus, delivery of LPA to RCMs is affinity-coupled to Edg receptors by gelsolin in a PIP2-regulated process [10].
  • Gelsolin binding and cellular presentation of lysophosphatidic acid [10].

Physical interactions of Gsn

  • Similar short average lengths are obtained when gelsolin severs actin complexed with low Mr TMs (0.080 +/- 0.045 micron) or with nonmuscle caldesmon (0.11 +/- 0.072 micron) while longer average length (0.22 +/- 0.18 micron) is measured in the presence of high Mr TMs [11].

Regulatory relationships of Gsn

  • Furthermore, the actin binding of gelsolin is strongly inhibited by co-addition of high Mr TMs and nonmuscle caldesmon [11].

Other interactions of Gsn

  • Drebrin, actin, myosin, and gelsolin were co-precipitated [12].
  • While nonmuscle caldesmon alone or low Mr TMs alone show no significant protection against fragmentation by gelsolin, the low Mr TMs coupled with 83-kDa protein are able to protect actin filaments [11].
  • Production of PIP and PIP2 may be important downstream signals since these polyphosphoinositides are able to regulate the interaction of gelsolin and profilin with actin [13].
  • These effects were corroborated in vitro using recombinant gelsolin protein on isolated rat mitochondria stimulated with Ca(2+), atractyloside, or Bax [14].
  • In addition to alpha-smooth-muscle actin, these structures contain cytoplasmic actins, gelsolin and cofilin but not other major actin-binding proteins [15].

Analytical, diagnostic and therapeutic context of Gsn


  1. Unphosphorylated gelsolin is localized in regions of cell-substratum contact or attachment in Rous sarcoma virus-transformed rat cells. Wang, E., Yin, H.L., Krueger, J.G., Caliguiri, L.A., Tamm, I. J. Cell Biol. (1984) [Pubmed]
  2. Cells of the neuronal lineage play a major role in the generation of amyloid precursor fragments in gelsolin-related amyloidosis. Paunio, T., Kangas, H., Heinonen, O., Buc-Caron, M.H., Robert, J.J., Kaasinen, S., Julkunen, I., Mallet, J., Peltonen, L. J. Biol. Chem. (1998) [Pubmed]
  3. Activation of the caspase-3 apoptotic cascade in traumatic spinal cord injury. Springer, J.E., Azbill, R.D., Knapp, P.E. Nat. Med. (1999) [Pubmed]
  4. Plectin sidearms mediate interaction of intermediate filaments with microtubules and other components of the cytoskeleton. Svitkina, T.M., Verkhovsky, A.B., Borisy, G.G. J. Cell Biol. (1996) [Pubmed]
  5. Actin filament disassembly is a sufficient final trigger for exocytosis in nonexcitable cells. Muallem, S., Kwiatkowska, K., Xu, X., Yin, H.L. J. Cell Biol. (1995) [Pubmed]
  6. Evidence for a direct, nucleotide-sensitive interaction between actin and liver cell membranes. Tranter, M.P., Sugrue, S.P., Schwartz, M.A. J. Cell Biol. (1989) [Pubmed]
  7. Modulation of the actin cytoskeleton via gelsolin regulates vacuolar H+-ATPase recycling. Beaulieu, V., Da Silva, N., Pastor-Soler, N., Brown, C.R., Smith, P.J., Brown, D., Breton, S. J. Biol. Chem. (2005) [Pubmed]
  8. Gelsolin--evidence for a role in turnover of junction-related actin filaments in Sertoli cells. Guttman, J.A., Janmey, P., Vogl, A.W. J. Cell. Sci. (2002) [Pubmed]
  9. Aging-associated increase of gelsolin for apoptosis resistance. Ahn, J.S., Jang, I.S., Kim, D.I., Cho, K.A., Park, Y.H., Kim, K., Kwak, C.S., Chul Park, S. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  10. Gelsolin binding and cellular presentation of lysophosphatidic acid. Goetzl, E.J., Lee, H., Azuma, T., Stossel, T.P., Turck, C.W., Karliner, J.S. J. Biol. Chem. (2000) [Pubmed]
  11. Differential modulation of actin-severing activity of gelsolin by multiple isoforms of cultured rat cell tropomyosin. Potentiation of protective ability of tropomyosins by 83-kDa nonmuscle caldesmon. Ishikawa, R., Yamashiro, S., Matsumura, F. J. Biol. Chem. (1989) [Pubmed]
  12. Modulatory role of drebrin on the cytoskeleton within dendritic spines in the rat cerebral cortex. Hayashi, K., Ishikawa, R., Ye, L.H., He, X.L., Takata, K., Kohama, K., Shirao, T. J. Neurosci. (1996) [Pubmed]
  13. Polymerization of actin in RBL-2H3 cells can be triggered through either the IgE receptor or the adenosine receptor but different signaling pathways are used. Apgar, J.R. Mol. Biol. Cell (1994) [Pubmed]
  14. Gelsolin inhibits apoptosis by blocking mitochondrial membrane potential loss and cytochrome c release. Koya, R.C., Fujita, H., Shimizu, S., Ohtsu, M., Takimoto, M., Tsujimoto, Y., Kuzumaki, N. J. Biol. Chem. (2000) [Pubmed]
  15. The N-terminal Ac-EEED sequence plays a role in alpha-smooth-muscle actin incorporation into stress fibers. Clément, S., Hinz, B., Dugina, V., Gabbiani, G., Chaponnier, C. J. Cell. Sci. (2005) [Pubmed]
  16. Localization and characterization of gelsolin in nervous tissues: gelsolin is specifically enriched in myelin-forming cells. Tanaka, J., Sobue, K. J. Neurosci. (1994) [Pubmed]
  17. Circulating actin-gelsolin complexes following oleic acid-induced lung injury. Smith, D.B., Janmey, P.A., Lind, S.E. Am. J. Pathol. (1988) [Pubmed]
  18. Dynein and plus-end microtubule-dependent motors are associated with specialized Sertoli cell junction plaques (ectoplasmic specializations). Guttman, J.A., Kimel, G.H., Vogl, A.W. J. Cell. Sci. (2000) [Pubmed]
  19. Inhibition of histone deacetylation protects wild-type but not gelsolin-deficient neurons from oxygen/glucose deprivation. Meisel, A., Harms, C., Yildirim, F., Bösel, J., Kronenberg, G., Harms, U., Fink, K.B., Endres, M. J. Neurochem. (2006) [Pubmed]
WikiGenes - Universities