High impact information on SPC42

• We find that Mlp2p binds directly to Spc110p, Spc42p, and Spc29p, which are three core components of the spindle pole body (SPB), the nuclear envelope-associated yeast spindle organizer [1].
• A screen for dosage suppressors of the mps1-8 conditional growth phenotype identified the gene encoding the integral SPB component SPC42 [2].
• We conclude that Mps1p regulates assembly of the integral SPB component Spc42p during SPB duplication [2].
• Additionally, distinct spots of Ndc1p localization colocalize with a known SPB component, Spc42p [3].
• Finally, we isolated a complex containing Spc110p, Spc42p, calmodulin and a 35 kDa protein, suggesting that these four proteins interact in the SPB [4].

Biological context of SPC42

• We have investigated the role that the major yeast cyclin-dependent kinase Cdc28/Cdk1 plays in assembly of a core SPB component, Spc42, to better understand how SPB duplication is coordinated with cell cycle progression [5].
• In the yeast Saccharomyces cerevisiae, SPC42 is an essential gene, which encodes one of the major components of the spindle pole body (SPB) [6].
• Spc42p is a phosphoprotein which shows some cell cycle-regulated phosphorylation [7].
• The delamination is likely due to a perturbed interaction between Spc42p and Spc110-226p as detected by fluorescence resonance energy transfer analysis [8].
• We have probed single kinetochore microtubule (k-MT) dynamics in budding yeast in the G1 phase of the cell cycle by automated tracking of a green fluorescent protein tag placed proximal to the centromere on chromosome IV and of a green fluorescent protein tag fused to the spindle pole body protein Spc42p [9].

Anatomical context of SPC42

• Taken together, these data suggest that Spc42p forms a polymeric layer at the periphery of the SPB central plaque which has an essential function during SPB duplication and may facilitate attachment of the SPB to the nuclear membrane [7].

Associations of SPC42 with chemical compounds

• We found that a change to a proline residue in a potential coiled-coil region of Spc42p was responsible for the ts phenotype in at least three alleles, suggesting that formation of the coiled-coil is essential in normal function [7].

Other interactions of SPC42

• In agreement with this, overexpressed Spc29p was found to be a nuclear protein, whereas Spc42p is cytoplasmic [10].
• Spc29p acts as a linker between the central plaque component Spc42p and the inner plaque protein Spc110p [10].
• The yeast protein kinase Mps1p is required for assembly of the integral spindle pole body component Spc42p [2].

Analytical, diagnostic and therapeutic context of SPC42

• Seven temperature-sensitive (ts) mutants in SPC42 were prepared by error-prone PCR [7].

References