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Gene Review

PFY1  -  profilin

Saccharomyces cerevisiae S288c

Synonyms: CLS5, O3275, PFY, PRF1, Profilin, ...
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Disease relevance of PFY1


High impact information on PFY1

  • 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 [2].
  • We propose that CAP and profilin provide a link between growth signals and remodeling of the cellular cytoskeleton [3].
  • The phenotype of cells lacking PFY resembles that of cells lacking the CAP C-terminal domain [3].
  • Thus, formin and profilin mediate actin nucleation by an Arp2/3-independent mechanism [4].
  • However, fluid phase endocytosis is defective in act1-159 strains. act1-159 is synthetically lethal with cofilin and profilin mutants, supporting the conclusion that mutations in all of these genes impair the polymerization/ depolymerization cycle [5].

Chemical compound and disease context of PFY1


Biological context of PFY1

  • The PFY1 promoter dispenses with classical transactivators and a consensus TATA box; however, it contains a canonic site for the abundant multifunctional nuclear factor rDNA enhancer-binding protein (Reb1p) combined with a dA.dT element [6].
  • In contrast, overexpression of the profilin gene, PFY1, encoding an actin-binding protein, leads to no very obvious phenotype [7].
  • In contrast, the patterns for profilin and the SH3 domain proteins suggest a shared binding site and commonality in mechanism [8].
  • The severity of various morphological abnormalities of the strains was also attenuated with increased protein levels, suggesting that profilin polyproline-binding mutations are deleterious to cell growth unless overexpressed [9].
  • In light of recent studies with profilins, we propose that Cdc3-profilin plays an essential role in cytokinesis by catalyzing the formation of the F-actin contractile ring [10].

Anatomical context of PFY1


Associations of PFY1 with chemical compounds


Physical interactions of PFY1

  • Moreover, yeast two-hybrid and biochemical studies demonstrate that Bni1p and Bnr1p interact directly with profilin at the FH1 domains [15].
  • Actin was bound to the profilin localized in the cytosol [11].
  • All of the sec3 alleles genetically interact with a profilin mutation, pfy1-111 [16].

Enzymatic interactions of PFY1


Regulatory relationships of PFY1


Other interactions of PFY1

  • These results indicate that Bni1p and Bnr1p are potential targets of the Rho family members, interact with profilin and regulate the reorganization of actin cytoskeleton [15].
  • These results indicate that Bnr1p directly interacts with Hof1p as well as with profilin to regulate cytoskeletal functions in S. cerevisiae [18].
  • SEC3 mutations are synthetically lethal with profilin mutations and cause defects in diploid-specific bud-site selection [13].
  • It contains the transcription termination region of the convergently transcribed yeast genes, GCY1 and PFY1, together with sequences corresponding to the mapped 3'-ends of the respective mRNAs [19].
  • These phenotypes are similar to those of the mutant of PFY1, which encodes profilin, an actin-binding protein [15].

Analytical, diagnostic and therapeutic context of PFY1


  1. 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]
  2. 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]
  3. Evidence for a functional link between profilin and CAP in the yeast S. cerevisiae. Vojtek, A., Haarer, B., Field, J., Gerst, J., Pollard, T.D., Brown, S., Wigler, M. Cell (1991) [Pubmed]
  4. An actin nucleation mechanism mediated by Bni1 and profilin. Sagot, I., Rodal, A.A., Moseley, J., Goode, B.L., Pellman, D. Nat. Cell Biol. (2002) [Pubmed]
  5. The yeast V159N actin mutant reveals roles for actin dynamics in vivo. Belmont, L.D., Drubin, D.G. J. Cell Biol. (1998) [Pubmed]
  6. Reb1p-dependent DNA bending effects nucleosome positioning and constitutive transcription at the yeast profilin promoter. Angermayr, M., Oechsner, U., Bandlow, W. J. Biol. Chem. (2003) [Pubmed]
  7. High levels of profilin suppress the lethality caused by overproduction of actin in yeast cells. Magdolen, V., Drubin, D.G., Mages, G., Bandlow, W. FEBS Lett. (1993) [Pubmed]
  8. Defining protein interactions with yeast actin in vivo. Amberg, D.C., Basart, E., Botstein, D. Nat. Struct. Biol. (1995) [Pubmed]
  9. Polyproline binding is an essential function of human profilin in yeast. Ostrander, D.B., Ernst, E.G., Lavoie, T.B., Gorman, J.A. Eur. J. Biochem. (1999) [Pubmed]
  10. The Schizosaccharomyces pombe cdc3+ gene encodes a profilin essential for cytokinesis. Balasubramanian, M.K., Hirani, B.R., Burke, J.D., Gould, K.L. J. Cell Biol. (1994) [Pubmed]
  11. Regulation of profilin localization in Saccharomyces cerevisiae by phosphoinositide metabolism. Ostrander, D.B., Gorman, J.A., Carman, G.M. J. Biol. Chem. (1995) [Pubmed]
  12. Suppression of the profilin-deficient phenotype by the RHO2 signaling pathway in Saccharomyces cerevisiae. Marcoux, N., Cloutier, S., Zakrzewska, E., Charest, P.M., Bourbonnais, Y., Pallotta, D. Genetics (2000) [Pubmed]
  13. SEC3 mutations are synthetically lethal with profilin mutations and cause defects in diploid-specific bud-site selection. Haarer, B.K., Corbett, A., Kweon, Y., Petzold, A.S., Silver, P., Brown, S.S. Genetics (1996) [Pubmed]
  14. 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]
  15. 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]
  16. Sec3p is involved in secretion and morphogenesis in Saccharomyces cerevisiae. Finger, F.P., Novick, P. Mol. Biol. Cell (1997) [Pubmed]
  17. Overexpression of MID2 suppresses the profilin-deficient phenotype of yeast cells. Marcoux, N., Bourbonnais, Y., Charest, P.M., Pallotta, D. Mol. Microbiol. (1998) [Pubmed]
  18. Interaction of Bnr1p with a novel Src homology 3 domain-containing Hof1p. Implication in cytokinesis in Saccharomyces cerevisiae. Kamei, T., Tanaka, K., Hihara, T., Umikawa, M., Imamura, H., Kikyo, M., Ozaki, K., Takai, Y. J. Biol. Chem. (1998) [Pubmed]
  19. pYLZ vectors: Saccharomyces cerevisiae/Escherichia coli shuttle plasmids to analyze yeast promoters. Hermann, H., Häcker, U., Bandlow, W., Magdolen, V. Gene (1992) [Pubmed]
  20. Characterization of a mutant profilin with reduced actin-binding capacity: effects in vitro and in vivo. Hájková, L., Björkegren Sjögren, C., Korenbaum, E., Nordberg, P., Karlsson, R. Exp. Cell Res. (1997) [Pubmed]
  21. Structure determination and characterization of Saccharomyces cerevisiae profilin. Eads, J.C., Mahoney, N.M., Vorobiev, S., Bresnick, A.R., Wen, K.K., Rubenstein, P.A., Haarer, B.K., Almo, S.C. Biochemistry (1998) [Pubmed]
  22. Production, isolation and characterization of human profilin from Saccharomyces cerevisiae. Aspenström, P., Lassing, I., Karlsson, R. J. Muscle Res. Cell. Motil. (1991) [Pubmed]
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