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Gene Review

SLA1  -  Sla1p

Saccharomyces cerevisiae S288c

Synonyms: Actin cytoskeleton-regulatory complex protein SLA1, YBL007C, YBL0321
 
 
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High impact information on SLA1

 

Biological context of SLA1

  • Despite relatively low overall sequence homology, this gene was able to rescue the temperature sensitivity associated with a deletion of SLA1 in Saccharomyces cerevisiae [4].
  • The two SLA1 SH3 domains required for this inhibitory activity in vitro were also required in vivo, in combination with BBC1, for cell viability and normal actin organization [5].
  • Finally, we demonstrate marked defects in both fluid-phase and receptor-mediated endocytosis in cells that do not express SLA1, indicating that Sla1p is central to the requirement in yeast to couple endocytosis with the actin cytoskeleton [6].
  • Expression of mutant forms of Sla1p in which specific domains were deleted showed that the phenotypes associated with the full deletion are functionally separable [4].
  • These results indicate that the functions of Pan1p, End3p, and Sla1p in cell wall morphogenesis may depend on the formation of a heterotrimeric complex [7].
 

Anatomical context of SLA1

  • Mislocalization of Rho1p in sla1 null cells is consistent with our observation that these cells possess aberrantly thick cell walls [4].
  • Overexpression of the interacting fragment of Sla1p causes reduced fluid-phase endocytosis and, interestingly, defects in subsequent trafficking to vacuoles [8].
 

Associations of SLA1 with chemical compounds

  • In a Sla1(-) background, [PSI] curing by dimethylsulfoxide or excess Hsp104 is increased, while translational readthrough and de novo [PSI] formation induced by excess Sup35 or Sup35N are decreased [9].
 

Physical interactions of SLA1

 

Regulatory relationships of SLA1

  • Here we use a combination of immunofluorescence microscopy and biochemical approaches to demonstrate interactions of Sla1p both with proteins regulating actin dynamics and with proteins required for endocytosis [6].
 

Other interactions of SLA1

  • Here, we show that Sla1p, like Abp1p, localizes to cortical actin patches [4].
  • Sla1p contains three SH3 domains and is essential for the proper formation of the cortical actin cytoskeleton [3].
  • Localisation of Sla1p at the cell cortex is, however, dependent on the EH-domain-containing protein End3p, which is part of the yeast endocytic machinery [6].
  • Sla1p is a protein required for cortical actin patch structure and organisation in budding yeast [6].
  • In further support of these roles for Anc1p, the anc1 delta 1::HIS3 mutation was found to be synthetically lethal in combination with a null mutation in SLA1, a gene that is important for membrane cytoskeleton function [11].

References

  1. The actin cytoskeleton, RAS-cAMP signaling and mitochondrial ROS in yeast apoptosis. Breitenbach, M., Laun, P., Gimona, M. Trends Cell Biol. (2005) [Pubmed]
  2. Sla1p serves as the targeting signal recognition factor for NPFX(1,2)D-mediated endocytosis. Howard, J.P., Hutton, J.L., Olson, J.M., Payne, G.S. J. Cell Biol. (2002) [Pubmed]
  3. Synthetic-lethal interactions identify two novel genes, SLA1 and SLA2, that control membrane cytoskeleton assembly in Saccharomyces cerevisiae. Holtzman, D.A., Yang, S., Drubin, D.G. J. Cell Biol. (1993) [Pubmed]
  4. Sla1p is a functionally modular component of the yeast cortical actin cytoskeleton required for correct localization of both Rho1p-GTPase and Sla2p, a protein with talin homology. Ayscough, K.R., Eby, J.J., Lila, T., Dewar, H., Kozminski, K.G., Drubin, D.G. Mol. Biol. Cell (1999) [Pubmed]
  5. Negative regulation of yeast WASp by two SH3 domain-containing proteins. Rodal, A.A., Manning, A.L., Goode, B.L., Drubin, D.G. Curr. Biol. (2003) [Pubmed]
  6. Sla1p couples the yeast endocytic machinery to proteins regulating actin dynamics. Warren, D.T., Andrews, P.D., Gourlay, C.W., Ayscough, K.R. J. Cell. Sci. (2002) [Pubmed]
  7. Pan1p, End3p, and S1a1p, three yeast proteins required for normal cortical actin cytoskeleton organization, associate with each other and play essential roles in cell wall morphogenesis. Tang, H.Y., Xu, J., Cai, M. Mol. Cell. Biol. (2000) [Pubmed]
  8. An interaction between Sla1p and Sla2p plays a role in regulating actin dynamics and endocytosis in budding yeast. Gourlay, C.W., Dewar, H., Warren, D.T., Costa, R., Satish, N., Ayscough, K.R. J. Cell. Sci. (2003) [Pubmed]
  9. Genetic study of interactions between the cytoskeletal assembly protein sla1 and prion-forming domain of the release factor Sup35 (eRF3) in Saccharomyces cerevisiae. Bailleul, P.A., Newnam, G.P., Steenbergen, J.N., Chernoff, Y.O. Genetics (1999) [Pubmed]
  10. The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the yeast CIN85-endophilin complex, Sla1-Rvs167. Stamenova, S.D., Dunn, R., Adler, A.S., Hicke, L. J. Biol. Chem. (2004) [Pubmed]
  11. 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]
 
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