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

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

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 ba...

Full description

Bibliographic Details
Main Authors: Lin, Tien-chen, Neuner, Annett, Schlosser, Yvonne T, Scharf, Annette ND, Weber, Lisa, Schiebel, Elmar
Format: Online
Language:English
Published: eLife Sciences Publications, Ltd 2014
Online Access:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4034690/
id pubmed-4034690
recordtype oai_dc
spelling pubmed-40346902014-06-02 Cell-cycle dependent phosphorylation of yeast pericentrin regulates γ-TuSC-mediated microtubule nucleation Lin, Tien-chen Neuner, Annett Schlosser, Yvonne T Scharf, Annette ND Weber, Lisa Schiebel, Elmar Biochemistry 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. eLife Sciences Publications, Ltd 2014-04-30 /pmc/articles/PMC4034690/ /pubmed/24842996 http://dx.doi.org/10.7554/eLife.02208 Text en Copyright © 2014, Lin et al http://creativecommons.org/licenses/by/3.0/ This article is distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/3.0/) , which permits unrestricted use and redistribution provided that the original author and source are credited.
repository_type Open Access Journal
institution_category Foreign Institution
institution US National Center for Biotechnology Information
building NCBI PubMed
collection Online Access
language English
format Online
author Lin, Tien-chen
Neuner, Annett
Schlosser, Yvonne T
Scharf, Annette ND
Weber, Lisa
Schiebel, Elmar
spellingShingle Lin, Tien-chen
Neuner, Annett
Schlosser, Yvonne T
Scharf, Annette ND
Weber, Lisa
Schiebel, Elmar
Cell-cycle dependent phosphorylation of yeast pericentrin regulates γ-TuSC-mediated microtubule nucleation
author_facet Lin, Tien-chen
Neuner, Annett
Schlosser, Yvonne T
Scharf, Annette ND
Weber, Lisa
Schiebel, Elmar
author_sort Lin, Tien-chen
title Cell-cycle dependent phosphorylation of yeast pericentrin regulates γ-TuSC-mediated microtubule nucleation
title_short Cell-cycle dependent phosphorylation of yeast pericentrin regulates γ-TuSC-mediated microtubule nucleation
title_full Cell-cycle dependent phosphorylation of yeast pericentrin regulates γ-TuSC-mediated microtubule nucleation
title_fullStr Cell-cycle dependent phosphorylation of yeast pericentrin regulates γ-TuSC-mediated microtubule nucleation
title_full_unstemmed Cell-cycle dependent phosphorylation of yeast pericentrin regulates γ-TuSC-mediated microtubule nucleation
title_sort cell-cycle dependent phosphorylation of yeast pericentrin regulates γ-tusc-mediated microtubule nucleation
description 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.
publisher eLife Sciences Publications, Ltd
publishDate 2014
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4034690/
_version_ 1612093656084250624

Similar Items