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

Identifieur interne : 000179 ( Main/Exploration ); précédent : 000178; suivant : 000180

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

Auteurs : Tien-Chen Lin [Allemagne] ; Annett Neuner [Allemagne] ; Yvonne T. Schlosser [Allemagne] ; Annette Nd Scharf [Allemagne] ; Lisa Weber [Allemagne] ; Elmar Schiebel [Allemagne]

Source :

RBID : PMC:4034690

Abstract

Budding yeast Spc110, a member of γ-tubulin complex receptor family (γ-TuCR), recruits γ-tubulin complexes to microtubule (MT) organizing centers (MTOCs). Biochemical studies suggest that Spc110 facilitates higher-order γ-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 γ-TuSC oligomerization and MT nucleation in a cell cycle dependent manner. Interaction between the N-terminus of the γ-TuSC subunit Spc98 and Spc110 is important for this activity. Besides the conserved CM1 motif in γ-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 γ-TuCRs. The two types of γ-TuCRs contain distinct but conserved C-terminal MTOC targeting domains.

DOI:http://dx.doi.org/10.7554/eLife.02208.001


Url:
DOI: 10.7554/eLife.02208
PubMed: 24842996
PubMed Central: 4034690


Affiliations:


Links toward previous steps (curation, corpus...)


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