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Mlp-dependent anchorage and stabilization of a desumoylating enzyme is required to prevent clonal lethality.
- Source :
-
The Journal of cell biology [J Cell Biol] 2004 Nov 22; Vol. 167 (4), pp. 605-11. - Publication Year :
- 2004
-
Abstract
- Myosin-like proteins 1 and 2 (Mlp1 and Mlp2) form filaments attached to the nucleoplasmic side of the nuclear pore complexes via interaction with the nucleoporin Nup60. Here, we show that Mlps and Nup60, but not several other nucleoporins, are required to localize and stabilize a desumoylating enzyme Ulp1. Moreover, like Mlps, Ulp1 exhibits a unique asymmetric distribution on the nuclear envelope. Consistent with a role in regulating Ulp1, removal of either or both MLPs affects the SUMO conjugate pattern. We also show that deleting MLPs or the localization domains of Ulp1 results in DNA damage sensitivity and clonal lethality, the latter of which is caused by increased levels of 2-micron circle DNA. Epistatic and dosage suppression analyses further demonstrate that Mlps function upstream of Ulp1 in 2-micron circle maintenance and the damage response. Together, our results reveal that Mlps play important roles in regulating Ulp1 and subsequently affect sumoylation stasis, growth, and DNA repair.
- Subjects :
- Clone Cells metabolism
Cysteine Endopeptidases genetics
DNA Damage genetics
DNA Repair genetics
DNA, Circular genetics
Enzyme Stability genetics
Epistasis, Genetic
Gene Dosage
Genes, Lethal genetics
Nuclear Pore genetics
Nuclear Pore Complex Proteins genetics
Nuclear Proteins genetics
Protein Structure, Tertiary genetics
RNA-Binding Proteins
SUMO-1 Protein genetics
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae Proteins genetics
Cysteine Endopeptidases metabolism
Nuclear Pore metabolism
Nuclear Pore Complex Proteins metabolism
Nuclear Proteins metabolism
SUMO-1 Protein metabolism
Saccharomyces cerevisiae metabolism
Saccharomyces cerevisiae Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9525
- Volume :
- 167
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- The Journal of cell biology
- Publication Type :
- Academic Journal
- Accession number :
- 15557117
- Full Text :
- https://doi.org/10.1083/jcb.200405168