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Gene Review

MLP1  -  Mlp1p

Saccharomyces cerevisiae S288c

Synonyms: Myosin-like protein 1, Protein MLP1, YKR095W, YKR415
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High impact information on MLP1

  • When overall pre-mRNA levels are increased by deletion of RRP6, a nuclear exosome component, MLP1 deletion augments leakage of only the intron-containing portion of mRNAs [1].
  • The Mlp1-dependent leakage of intron-containing RNAs is increased in presence of ts-prp18 delta, a splicing mutant [1].
  • Furthermore, double deletion of MLP1 and MLP2 disrupts the clustering of perinuclear telomeres and releases telomeric gene repression [2].
  • High-resolution mapping of association of chromosome III with Mlp1 revealed alpha-factor-dependent determinants of nuclear pore association, including origins of replication, specific intergenic regions, and the 3' ends of transcriptionally activated genes [3].
  • The loss of Mlp1p/Mlp2p, two TPR-like proteins attached to nuclear pores, rescues LacZ mRNA levels and increases their appearance in the cytoplasm, without restoring bulk poly(A)+ RNA export [4].

Biological context of MLP1

  • Remarkably, cells harboring a double deletion of MLP1 and MLP2 were viable, although they showed a slower net rate of active nuclear import and faster passive efflux of a reporter protein [5].
  • Cells lacking MLP1 and GRX5 are hypersensitive to oxidative stress caused by external agents and exhibit increased protein oxidation in relation to single mutants [6].
  • Overexpression of MLP1 suppresses the caffeine-sensitive phenotype of the bck1 delta mutation [7].
  • Mutants bearing disruptions of the MLP1 gene were viable, but more sensitive to ultraviolet light than wild-type strains, suggesting an involvement of MLP1 in DNA repair [8].
  • The MLP1 gene was mapped to chromosome 11, 25 cM from met1 [8].

Anatomical context of MLP1

  • It has been reported that two large coiled-coil proteins of the nuclear envelope, myosin-like proteins 1 and 2, play direct roles in anchoring yeast telomeres to the nuclear periphery, thereby creating a subcompartment enriched for Sir proteins [9].
  • Several have features reminiscent of cytoskeleton or motor elements (keratin-like, myosin-like) and several others have characteristics of proteins which interact with DNA (extremely basic, b-Zip structure and/or acidic domains) [10].
  • Here we show that nuclear-pore-complex extensions formed by the conserved TPR homologues Mlp1 and Mlp2 are responsible for the structural and functional organization of perinuclear chromatin [2].
  • In mouse epithelial cells the yeast anti-MLP1 antibodies stained the nucleus [8].
  • These findings suggest that myosin or a myosin-like protein plays a key role in insulin-regulated movement of GLUT4 to the plasma membrane in rat adipocytes [11].

Physical interactions of MLP1


Other interactions of MLP1

  • Myosin-like proteins 1 and 2 are not required for silencing or telomere anchoring, but act in the Tel1 pathway of telomere length control [9].
  • One of these is MLP1, which codes for a homologue of the Slt2 kinase [6].
  • In addition, our experiments reveal that the C-terminal domain of Mlp1p is both necessary and sufficient to cause accumulation of poly(A) RNA and Nab2p in the nucleus [12].
  • We identified a yeast two-hybrid interaction between the C-terminal globular domain of Mlp1p and Nab2p, a shuttling heterogeneous nuclear ribonucleoprotein that is required for mRNA export [12].
  • The phenotype of the TPM1 disrupted cells is very similar to that of a conditional mutation in the MYO2 gene, which encodes a myosin-like protein (Johnston, G. C., J. A. Prendergast, and R. A. Singer. 1991. J. Cell Biol. 113:539-551) [13].


  1. Nuclear retention of unspliced mRNAs in yeast is mediated by perinuclear Mlp1. Galy, V., Gadal, O., Fromont-Racine, M., Romano, A., Jacquier, A., Nehrbass, U. Cell (2004) [Pubmed]
  2. Nuclear pore complexes in the organization of silent telomeric chromatin. Galy, V., Olivo-Marin, J.C., Scherthan, H., Doye, V., Rascalou, N., Nehrbass, U. Nature (2000) [Pubmed]
  3. Developmentally induced changes in transcriptional program alter spatial organization across chromosomes. Casolari, J.M., Brown, C.R., Drubin, D.A., Rando, O.J., Silver, P.A. Genes Dev. (2005) [Pubmed]
  4. Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export. Vinciguerra, P., Iglesias, N., Camblong, J., Zenklusen, D., Stutz, F. EMBO J. (2005) [Pubmed]
  5. Proteins connecting the nuclear pore complex with the nuclear interior. Strambio-de-Castillia, C., Blobel, G., Rout, M.P. J. Cell Biol. (1999) [Pubmed]
  6. Saccharomyces cerevisiae glutaredoxin 5-deficient cells subjected to continuous oxidizing conditions are affected in the expression of specific sets of genes. Bellí, G., Molina, M.M., García-Martínez, J., Pérez-Ortín, J.E., Herrero, E. J. Biol. Chem. (2004) [Pubmed]
  7. Characterization of a serum response factor-like protein in Saccharomyces cerevisiae, Rlm1, which has transcriptional activity regulated by the Mpk1 (Slt2) mitogen-activated protein kinase pathway. Watanabe, Y., Takaesu, G., Hagiwara, M., Irie, K., Matsumoto, K. Mol. Cell. Biol. (1997) [Pubmed]
  8. A new yeast gene with a myosin-like heptad repeat structure. Kölling, R., Nguyen, T., Chen, E.Y., Botstein, D. Mol. Gen. Genet. (1993) [Pubmed]
  9. Myosin-like proteins 1 and 2 are not required for silencing or telomere anchoring, but act in the Tel1 pathway of telomere length control. Hediger, F., Dubrana, K., Gasser, S.M. J. Struct. Biol. (2002) [Pubmed]
  10. The sequence of a 54.7 kb fragment of yeast chromosome XV reveals the presence of two tRNAs and 24 new open reading frames. Valens, M., Bohn, C., Daignan-Fornier, B., Dang, V.D., Bolotin-Fukuhara, M. Yeast (1997) [Pubmed]
  11. A myosin-derived peptide C109 binds to GLUT4-vesicles and inhibits the insulin-induced glucose transport stimulation and GLUT4 recruitment in rat adipocytes. Lee, W., Samuel, J., Zhang, W., Rampal, A.L., Lachaal, M., Jung, C.Y. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  12. The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export. Green, D.M., Johnson, C.P., Hagan, H., Corbett, A.H. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  13. Characterization of TPM1 disrupted yeast cells indicates an involvement of tropomyosin in directed vesicular transport. Liu, H., Bretscher, A. J. Cell Biol. (1992) [Pubmed]
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