<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Citron YR</submitter><funding>Intramural NIH HHS</funding><funding>Howard Hughes Medical Institute</funding><funding>National Heart, Lung, and Blood Institute</funding><funding>National Institutes of Health</funding><funding>David and Lucile Packard Foundation</funding><funding>NIGMS NIH HHS</funding><funding>NIH HHS</funding><pagination>e0190530</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC5760045</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>13(1)</volume><pubmed_abstract>The centrosome serves as the main microtubule-organizing center in metazoan cells, yet despite its functional importance, little is known mechanistically about the structure and organizational principles that dictate protein organization in the centrosome. In particular, the protein-protein interactions that allow for the massive structural transition between the tightly organized interphase centrosome and the highly expanded matrix-like arrangement of the mitotic centrosome have been largely uncharacterized. Among the proteins that undergo a major transition is the Drosophila melanogaster protein centrosomin that contains a conserved carboxyl terminus motif, CM2. Recent crystal structures have shown this motif to be dimeric and capable of forming an intramolecular interaction with a centr</pubmed_abstract><journal>PloS one</journal><pubmed_title>The centrosomin CM2 domain is a multi-functional binding domain with distinct cell cycle roles.</pubmed_title><pmcid>PMC5760045</pmcid><funding_grant_id>ZIA HL006104</funding_grant_id><funding_grant_id>GM031627</funding_grant_id><funding_grant_id>T32 GM008284</funding_grant_id><funding_grant_id>DP2 OD008479</funding_grant_id><funding_grant_id>DP2OD008479</funding_grant_id><funding_grant_id>R01 GM031627</funding_grant_id><funding_grant_id>1ZIAHL006104</funding_grant_id><funding_grant_id>R35GM118099</funding_grant_id><funding_grant_id>R35 GM118099</funding_grant_id><pubmed_authors>Rusan NM</pubmed_authors><pubmed_authors>Citron YR</pubmed_authors><pubmed_authors>Agard DA</pubmed_authors><pubmed_authors>Fagerstrom CJ</pubmed_authors><pubmed_authors>Keszthelyi B</pubmed_authors><pubmed_authors>Huang B</pubmed_authors><pubmed_authors>Kelly MJS</pubmed_authors></additional><is_claimable>false</is_claimable><name>The centrosomin CM2 domain is a multi-functional binding domain with distinct cell cycle roles.</name><description>The centrosome serves as the main microtubule-organizing center in metazoan cells, yet despite its functional importance, little is known mechanistically about the structure and organizational principles that dictate protein organization in the centrosome. In particular, the protein-protein interactions that allow for the massive structural transition between the tightly organized interphase centrosome and the highly expanded matrix-like arrangement of the mitotic centrosome have been largely uncharacterized. Among the proteins that undergo a major transition is the Drosophila melanogaster protein centrosomin that contains a conserved carboxyl terminus motif, CM2. Recent crystal structures have shown this motif to be dimeric and capable of forming an intramolecular interaction with a centr</description><dates><release>2018-01-01T00:00:00Z</release><publication>2018</publication><modification>2026-04-07T18:54:56.937Z</modification><creation>2019-03-26T23:49:42Z</creation></dates><accession>S-EPMC5760045</accession><cross_references><pubmed>29315319</pubmed><doi>10.1371/journal.pone.0190530</doi></cross_references></HashMap>