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Gene Review

ACT1  -  actin

Saccharomyces cerevisiae S288c

Synonyms: ABY1, Actin, END7, YFL039C
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Disease relevance of ACT1

  • Several recent studies have demonstrated that Wiskott-Aldrich syndrome protein (WASP) family proteins and the actin-related protein (Arp) 2/3 complex are key factors in the nucleation of actin filaments in diverse eukaryotic organisms [1].
  • Our findings suggest that changes in the functions or organization of actin filaments might contribute to the establishment of the neoplastic state for these leukemias and lymphomas [2].
  • A series of yTm1 N-terminal constructs were made with either an Ala-Ser dipeptide extension previously shown to restore actin binding to skeletal muscle Tm or the natural extension found in fibroblast Tm 5a/b. All constructs bound actin tightly and showed similar CD spectra and thermal stability [3].
  • The yeast recombinant Cof produced in Escherichia coli exhibited in vitro activities on actin filaments similar to those of mammalian and avian Cof [4].
  • First, it promotes actin assembly on the surface of the motile intracellular pathogen Listeria monocytogenes [5].

Psychiatry related information on ACT1


High impact information on ACT1

  • The observation that the BAF chromatin remodeling complex in which actin was originally identified, is also a human tumor suppressor complex necessary for the actions of the retinoblastoma protein indicates that the study of nuclear actin is likely to contribute to understanding cell growth control [8].
  • Nuclear actin and actin-related proteins in chromatin remodeling [8].
  • In the absence of Cdc42 or Cdc24, the actin cytoskeleton does not become organized and budding does not take place [9].
  • Conventional kinesin and class V and VI myosins coordinate the mechanochemical cycles of their motor domains for processive movement of cargo along microtubules or actin filaments [10].
  • We show that these diverse formins have the same basic properties: movement is processive in the absence or presence of profilin; profilin accelerates elongation; and actin ATP hydrolysis is not required for processivity [11].

Chemical compound and disease context of ACT1


Biological context of ACT1

  • Diploid cells containing a single copy of ACT1 are osmosensitive (Osms), i.e., they fail to grow in high osmolarity media (D. Shortle, unpublished observations cited by Novick, P., and D. Botstein. 1985. Cell. 40:415-426) [17].
  • Molecular genetic analysis indicates ACT3 is represented by a single gene from which the corresponding mRNA is expressed at a low level compared to ACT1 [18].
  • To understand the RNA structural features that dictate mRNA decay rates in yeast, we have constructed PGK1/MAT alpha 1 and ACT1/MAT alpha 1 gene fusions and analyzed the decay rates of the resultant chimeric transcripts [19].
  • Primer extension analysis showed that the aar2 mutant and disruptant have a defect in splicing two short introns of the a1 pre-mRNA but not in splicing pre-mRNA of ACT1 [20].
  • Interestingly, we also observed that mutation of the poly(A) polymerase gene altered the site of ACT1 polyadenylation [21].

Anatomical context of ACT1

  • Finally, a yeast mutant bearing a temperature-sensitive mutation in the actin-encoding ACT1 gene (act1-3) displays temperature-dependent defects in transfer of mitochondria from mother cells to newly developed buds during yeast cell mitosis [22].
  • In both animal and yeast cells, this process is dependent on cytoplasmic microtubules interacting with the cortical actin-based cytoskeleton, although the motive force was unknown [23].
  • Actin, a major cytoskeletal component of all eukaryotic cells, is one of the most highly conserved proteins [24].
  • Vac8p is related to beta-catenin and plakoglobin, which connect a specific region of the plasma membrane to the actin cytoskeleton [25].
  • Double deletion mutants also display phenotypes associated with actin disorganization including accumulation of intracellular membranes and vesicles, cell rounding, random bud site selection, sensitivity to high osmotic strength, and low pH as well as defects in chitin and cell wall deposition, invertase secretion, and fluid phase endocytosis [26].

Associations of ACT1 with chemical compounds

  • Twelve "alanine scan" alleles of the single yeast actin gene (ACT1) were tested for effects on filamentation, unipolar budding, agar invasion, and cell elongation [27].
  • In comparison to CLN2, expression from the ACT1 promoter was stable after release from nocodazole [28].
  • Irrespective of whether induction was achieved with methanol or formate, the UAS-FM element enhanced the level of induction of the FDH1 promoter in a manner dependent on the number of copies, but independent of their orientation, and also converted the ACT1 promoter from a constitutive into an inducible element [29].
  • We report that the actin assembly inhibitor latrunculin-A (LAT-A) causes complete disruption of the yeast actin cytoskeleton within 2-5 min, suggesting that although yeast are nonmotile, their actin filaments undergo rapid cycles of assembly and disassembly in vivo [30].
  • Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p [31].

Physical interactions of ACT1

  • Thus Sac6p binds to actin in vitro, and functionally associates with actin structures involved in the development and maintenance of cell polarity in vivo [32].
  • The yeast IQGAP homologue, designated Iqg1p, displays a two-hybrid interaction with activated Cdc42p and coimmunoprecipitates with actin filaments [33].
  • Using the two-hybrid system, we show that verprolin binds actin [34].
  • The F-actin-binding activity of unacetylated Tpm1p is reduced severely relative to the acetylated form [35].
  • Through systematic mutagenesis of Aip1 surfaces, we identify two well-separated F-actin-binding sites, one of which contributes to actin filament binding and disassembly specifically in the presence of cofilin [36].

Enzymatic interactions of ACT1

  • In vivo importance of actin nucleotide exchange catalyzed by profilin [37].
  • Yeast actin mutants with acidic residues at the N terminus either neutralized (DNEQ) or deleted (delta-DSE) were used to assess the role of N-terminal acidic residues in the interactions of actin with myosin in the contractile cycle [38].

Co-localisations of ACT1


Regulatory relationships of ACT1

  • Bni1p and Bnr1p: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae [43].
  • These results suggest that Cdc42 is closely involved in regulating actin assembly during polarized cell growth [44].
  • Previously we reported that additional actin suppresses the temperature-dependent growth defect caused by a mutation in VRP1 [34].
  • Cdc28p activated by G1-cyclins triggers polarization of actin to the site of bud emergence and favors apical bud growth (Lew, D. J., and S. I. Reed. 1993. J. Cell Biol. 120:1305-1320) [45].
  • These results indicate that Bni1p regulates microtubule-dependent nuclear migration through the actin cytoskeleton [46].

Other interactions of ACT1

  • To our knowledge, the Act2 protein from S. cerevisiae is the first highly divergent actin molecule described [24].
  • Requirement of yeast fimbrin for actin organization and morphogenesis in vivo [32].
  • Bni1p may function as a Cdc42p target that links the pheromone response pathway to the actin cytoskeleton [47].
  • During mating pheromone response, bni1 mutants showed defects both in polarized morphogenesis and in reorganization of the underlying actin cytoskeleton [47].
  • This defect is seen not only in 3' splice site cis-competitions but also in the splicing of an unusual intron in the TUB3 gene and in the ACT1 intron when utilization of its 3' splice site is rate limiting for splicing [48].

Analytical, diagnostic and therapeutic context of ACT1


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  2. A nuclear protein with sequence similarity to proteins implicated in human acute leukemias is important for cellular morphogenesis and actin cytoskeletal function in Saccharomyces cerevisiae. Welch, M.D., Drubin, D.G. Mol. Biol. Cell (1994) [Pubmed]
  3. Actomyosin regulatory properties of yeast tropomyosin are dependent upon N-terminal modification. Maytum, R., Geeves, M.A., Konrad, M. Biochemistry (2000) [Pubmed]
  4. Isolation of a yeast essential gene, COF1, that encodes a homologue of mammalian cofilin, a low-M(r) actin-binding and depolymerizing protein. Iida, K., Moriyama, K., Matsumoto, S., Kawasaki, H., Nishida, E., Yahara, I. Gene (1993) [Pubmed]
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  7. Glycolytic enzyme interactions with yeast and skeletal muscle F-actin. Waingeh, V.F., Gustafson, C.D., Kozliak, E.I., Lowe, S.L., Knull, H.R., Thomasson, K.A. Biophys. J. (2006) [Pubmed]
  8. Nuclear actin and actin-related proteins in chromatin remodeling. Olave, I.A., Reck-Peterson, S.L., Crabtree, G.R. Annu. Rev. Biochem. (2002) [Pubmed]
  9. Role of small G proteins in yeast cell polarization and wall biosynthesis. Cabib, E., Drgonová, J., Drgon, T. Annu. Rev. Biochem. (1998) [Pubmed]
  10. Vik1 Modulates Microtubule-Kar3 Interactions through a Motor Domain that Lacks an Active Site. Allingham, J.S., Sproul, L.R., Rayment, I., Gilbert, S.P. Cell (2007) [Pubmed]
  11. Control of the assembly of ATP- and ADP-actin by formins and profilin. Kovar, D.R., Harris, E.S., Mahaffy, R., Higgs, H.N., Pollard, T.D. Cell (2006) [Pubmed]
  12. The Yeast PH Domain Proteins Slm1 and Slm2 Are Targets of Sphingolipid Signaling during the Response to Heat Stress. Daquinag, A., Fadri, M., Jung, S.Y., Qin, J., Kunz, J. Mol. Cell. Biol. (2007) [Pubmed]
  13. Vaccinia virus expresses a novel profilin with a higher affinity for polyphosphoinositides than actin. Machesky, L.M., Cole, N.B., Moss, B., Pollard, T.D. Biochemistry (1994) [Pubmed]
  14. Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton. Takeda, T., McQuistan, T., Orlando, R.A., Farquhar, M.G. J. Clin. Invest. (2001) [Pubmed]
  15. Dominant selection system for use in Cryptococcus neoformans. Cox, G.M., Toffaletti, D.L., Perfect, J.R. J. Med. Vet. Mycol. (1996) [Pubmed]
  16. Sphingolipid functions in Saccharomyces cerevisiae. Dickson, R.C., Lester, R.L. Biochim. Biophys. Acta (2002) [Pubmed]
  17. Osmotic stress and the yeast cytoskeleton: phenotype-specific suppression of an actin mutation. Chowdhury, S., Smith, K.W., Gustin, M.C. J. Cell Biol. (1992) [Pubmed]
  18. ACT3: a putative centractin homologue in S. cerevisiae is required for proper orientation of the mitotic spindle. Clark, S.W., Meyer, D.I. J. Cell Biol. (1994) [Pubmed]
  19. Translation and a 42-nucleotide segment within the coding region of the mRNA encoded by the MAT alpha 1 gene are involved in promoting rapid mRNA decay in yeast. Parker, R., Jacobson, A. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  20. AAR2, a gene for splicing pre-mRNA of the MATa1 cistron in cell type control of Saccharomyces cerevisiae. Nakazawa, N., Harashima, S., Oshima, Y. Mol. Cell. Biol. (1991) [Pubmed]
  21. Effects of mutations in the Saccharomyces cerevisiae RNA14, RNA15, and PAP1 genes on polyadenylation in vivo. Mandart, E., Parker, R. Mol. Cell. Biol. (1995) [Pubmed]
  22. Yeast mitochondria contain ATP-sensitive, reversible actin-binding activity. Lazzarino, D.A., Boldogh, I., Smith, M.G., Rosand, J., Pon, L.A. Mol. Biol. Cell (1994) [Pubmed]
  23. Myosin V orientates the mitotic spindle in yeast. Yin, H., Pruyne, D., Huffaker, T.C., Bretscher, A. Nature (2000) [Pubmed]
  24. New yeast actin-like gene required late in the cell cycle. Schwob, E., Martin, R.P. Nature (1992) [Pubmed]
  25. Vac8p, a vacuolar protein with armadillo repeats, functions in both vacuole inheritance and protein targeting from the cytoplasm to vacuole. Wang, Y.X., Catlett, N.L., Weisman, L.S. J. Cell Biol. (1998) [Pubmed]
  26. Synthetic lethality screen identifies a novel yeast myosin I gene (MYO5): myosin I proteins are required for polarization of the actin cytoskeleton. Goodson, H.V., Anderson, B.L., Warrick, H.M., Pon, L.A., Spudich, J.A. J. Cell Biol. (1996) [Pubmed]
  27. Multiple functions for actin during filamentous growth of Saccharomyces cerevisiae. Cali, B.M., Doyle, T.C., Botstein, D., Fink, G.R. Mol. Biol. Cell (1998) [Pubmed]
  28. Destabilized green fluorescent protein for monitoring dynamic changes in yeast gene expression with flow cytometry. Mateus, C., Avery, S.V. Yeast (2000) [Pubmed]
  29. Cis-acting elements sufficient for induction of FDH1 expression by formate in the methylotrophic yeast Candida boidinii. Komeda, T., Yurimoto, H., Kato, N., Sakai, Y., Kondo, K. Mol. Genet. Genomics (2003) [Pubmed]
  30. High rates of actin filament turnover in budding yeast and roles for actin in establishment and maintenance of cell polarity revealed using the actin inhibitor latrunculin-A. Ayscough, K.R., Stryker, J., Pokala, N., Sanders, M., Crews, P., Drubin, D.G. J. Cell Biol. (1997) [Pubmed]
  31. Regulation of the actin cytoskeleton organization in yeast by a novel serine/threonine kinase Prk1p. Zeng, G., Cai, M. J. Cell Biol. (1999) [Pubmed]
  32. Requirement of yeast fimbrin for actin organization and morphogenesis in vivo. Adams, A.E., Botstein, D., Drubin, D.G. Nature (1991) [Pubmed]
  33. Iqg1p, a yeast homologue of the mammalian IQGAPs, mediates cdc42p effects on the actin cytoskeleton. Osman, M.A., Cerione, R.A. J. Cell Biol. (1998) [Pubmed]
  34. Actin-binding verprolin is a polarity development protein required for the morphogenesis and function of the yeast actin cytoskeleton. Vaduva, G., Martin, N.C., Hopper, A.K. J. Cell Biol. (1997) [Pubmed]
  35. Mdm20 protein functions with Nat3 protein to acetylate Tpm1 protein and regulate tropomyosin-actin interactions in budding yeast. Singer, J.M., Shaw, J.M. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  36. Aip1 and cofilin promote rapid turnover of yeast actin patches and cables: a coordinated mechanism for severing and capping filaments. Okada, K., Ravi, H., Smith, E.M., Goode, B.L. Mol. Biol. Cell (2006) [Pubmed]
  37. In vivo importance of actin nucleotide exchange catalyzed by profilin. Wolven, A.K., Belmont, L.D., Mahoney, N.M., Almo, S.C., Drubin, D.G. J. Cell Biol. (2000) [Pubmed]
  38. Mutational analysis of the role of the N terminus of actin in actomyosin interactions. Comparison with other mutant actins and implications for the cross-bridge cycle. Miller, C.J., Wong, W.W., Bobkova, E., Rubenstein, P.A., Reisler, E. Biochemistry (1996) [Pubmed]
  39. The EH-domain-containing protein Pan1 is required for normal organization of the actin cytoskeleton in Saccharomyces cerevisiae. Tang, H.Y., Cai, M. Mol. Cell. Biol. (1996) [Pubmed]
  40. SCP1 encodes an actin-bundling protein in yeast. Winder, S.J., Jess, T., Ayscough, K.R. Biochem. J. (2003) [Pubmed]
  41. An IQGAP-related protein controls actin-ring formation and cytokinesis in yeast. Epp, J.A., Chant, J. Curr. Biol. (1997) [Pubmed]
  42. Rvs167p, the budding yeast homolog of amphiphysin, colocalizes with actin patches. Balguerie, A., Sivadon, P., Bonneu, M., Aigle, M. J. Cell. Sci. (1999) [Pubmed]
  43. Bni1p and Bnr1p: downstream targets of the Rho family small G-proteins which interact with profilin and regulate actin cytoskeleton in Saccharomyces cerevisiae. Imamura, H., Tanaka, K., Hihara, T., Umikawa, M., Kamei, T., Takahashi, K., Sasaki, T., Takai, Y. EMBO J. (1997) [Pubmed]
  44. Regulation of cortical actin cytoskeleton assembly during polarized cell growth in budding yeast. Li, R., Zheng, Y., Drubin, D.G. J. Cell Biol. (1995) [Pubmed]
  45. The SLT2 (MPK1) MAP kinase homolog is involved in polarized cell growth in Saccharomyces cerevisiae. Mazzoni, C., Zarov, P., Rambourg, A., Mann, C. J. Cell Biol. (1993) [Pubmed]
  46. Bni1p regulates microtubule-dependent nuclear migration through the actin cytoskeleton in Saccharomyces cerevisiae. Fujiwara, T., Tanaka, K., Inoue, E., Kikyo, M., Takai, Y. Mol. Cell. Biol. (1999) [Pubmed]
  47. Bni1p, a yeast formin linking cdc42p and the actin cytoskeleton during polarized morphogenesis. Evangelista, M., Blundell, K., Longtine, M.S., Chow, C.J., Adames, N., Pringle, J.R., Peter, M., Boone, C. Science (1997) [Pubmed]
  48. A novel role for a U5 snRNP protein in 3' splice site selection. Umen, J.G., Guthrie, C. Genes Dev. (1995) [Pubmed]
  49. Molecular genetic study of introgression between Saccharomyces bayanus and S. cerevisiae. Naumova, E.S., Naumov, G.I., Masneuf-Pomarède, I., Aigle, M., Dubourdieu, D. Yeast (2005) [Pubmed]
  50. The intron of the yeast actin gene contains the promoter for an antisense RNA. Thompson-Jäger, S., Domdey, H. Curr. Genet. (1990) [Pubmed]
  51. Yeast actin patches are networks of branched actin filaments. Young, M.E., Cooper, J.A., Bridgman, P.C. J. Cell Biol. (2004) [Pubmed]
  52. Cofilin is an essential component of the yeast cortical cytoskeleton. Moon, A.L., Janmey, P.A., Louie, K.A., Drubin, D.G. J. Cell Biol. (1993) [Pubmed]
  53. A role for the divergent actin gene, ACT2, in nuclear pore structure and function. Yan, C., Leibowitz, N., Mélèse, T. EMBO J. (1997) [Pubmed]
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