Cell-cycle dependent phosphorylation of yeast pericentrin regulates ?-TuSC-mediated microtubule nucleation.

ABSTRACT: Budding yeast Spc110, a member of ?-tubulin complex receptor family (?-TuCR), recruits ?-tubulin complexes to microtubule (MT) organizing centers (MTOCs). Biochemical studies suggest that Spc110 facilitates higher-order ?-tubulin complex assembly (Kollman et al., 2010). Nevertheless the molecular basis for this activity and the regulation are unclear. Here we show that Spc110 phosphorylated by Mps1 and Cdk1 activates ?-TuSC oligomerization and MT nucleation in a cell cycle dependent manner. Interaction between the N-terminus of the ?-TuSC subunit Spc98 and Spc110 is important for this activity. Besides the conserved CM1 motif in ?-TuCRs (Sawin et al., 2004), a second motif that we named Spc110/Pcp1 motif (SPM) is also important for MT nucleation. The activating Mps1 and Cdk1 sites lie between SPM and CM1 motifs. Most organisms have both SPM-CM1 (Spc110/Pcp1/PCNT) and CM1-only (Spc72/Mto1/Cnn/CDK5RAP2/myomegalin) types of ?-TuCRs. The two types of ?-TuCRs contain distinct but conserved C-terminal MTOC targeting domains.DOI: http://dx.doi.org/10.7554/eLife.02208.001.

SUBMITTER: Lin TC 

PROVIDER: S-EPMC4034690 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature