ArticleThe Journal of biological chemistry2001
Yeast Mps1p phosphorylates the spindle pole component Spc110p in the N-terminal domain.
Article in The Journal of biological chemistry, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- Article
- Phosphosites of the yeast centrosome component Spc110 contribute to cell cycle progression and mitotic exit.Biology open · 2022Article
- Microtubule nucleation by γ-tubulin complexes and beyond.Essays in biochemistry · 2018Review
- Novel phosphorylation states of the yeast spindle pole body.Biology open · 2018Article
- Higher-order oligomerization of Spc110p drives γ-tubulin ring complex assembly.Molecular biology of the cell · 2016Article
- Mps1Mph1 Kinase Phosphorylates Mad3 to Inhibit Cdc20Slp1-APC/C and Maintain Spindle Checkpoint Arrests.PLoS genetics · 2016Article
- Interaction of CK1δ with γTuSC ensures proper microtubule assembly and spindle positioning.Molecular biology of the cell · 2015Article
- Cell-cycle dependent phosphorylation of yeast pericentrin regulates γ-TuSC-mediated microtubule nucleation.eLife · 2014Article
- Mitotic spindle form and function.Genetics · 2012Article
- The MPS1 family of protein kinases.Annual review of biochemistry · 2012Review
- A cell cycle phosphoproteome of the yeast centrosome.Science (New York, N.Y.) · 2011Article
- Article
- An overview of Cdk1-controlled targets and processes.Cell division · 2010Article
- Budding yeast centrosome duplication requires stabilization of Spc29 via Mps1-mediated phosphorylation.The Journal of biological chemistry · 2009Article
- Centrosomes and checkpoints: the MPS1 family of kinases.Oncogene · 2002Review
- Centrosomal proteins CG-NAP and kendrin provide microtubule nucleation sites by anchoring gamma-tubulin ring complex.Molecular biology of the cell · 2002Article
- The yeast protein kinase Mps1p is required for assembly of the integral spindle pole body component Spc42p.The Journal of cell biology · 2002Article
- Requirement of the spindle pole body for targeting and/or tethering proteins to the inner nuclear membrane.Nucleus (Austin, Tex.)Article
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Authors and funding
12 authors.
Funding
Abstract
The yeast spindle pole body (SPB) component Spc110p (Nuf1p) undergoes specific serine/threonine phosphorylation as the mitotic spindle apparatus forms, and this phosphorylation persists until cells enter anaphase. We demonstrate that the dual-specificity kinase Mps1p is essential for the mitosis-specific phosphorylation of Spc110p in vivo and that Mps1p phosphorylates Spc110p in vitro. Phosphopeptides generated by proteolytic cleavage were identified and sequenced by mass spectrometry. Ser(60), Thr(64), and Thr(68) are the major sites in Spc110p phosphorylated by Mps1p in vitro, and alanine substitution at these sites abolishes the mitosis-specific isoform in vivo. This is the first time that phosphorylation sites of an SPB component have been determined, and these are the first sites of Mps1p phosphorylation identified. Alanine substitution for any one of these phosphorylated residues, in conjunction with an alanine substitution at residue Ser(36), is lethal in combination with alleles of SPC97, which encodes a component of the Tub4p complex. Consistent with a specific dysfunction for the alanine substitution mutations, simultaneous mutation of all four serine/threonine residues to aspartate does not confer any defect. Sites of Mps1p phosphorylation and Ser(36) are located within the N-terminal globular domain of Spc110p, which resides at the inner plaque of the SPB and binds the Tub4p complex.
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