<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Liu H</submitter><funding>MEXT | Japan Society for the Promotion of Science</funding><pagination>e202201714</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC9998277</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>6(5)</volume><pubmed_abstract>CAMSAPs are proteins that show microtubule minus-end-specific localization, decoration, and stabilization. Although the mechanism for minus-end recognition via their C-terminal CKK domain has been well described in recent studies, it is unclear how CAMSAPs stabilize microtubules. Our several binding assays revealed that the D2 region of CAMSAP3 specifically binds to microtubules with the expanded lattice. To investigate the relationship between this preference and the stabilization effect of CAMSAP3, we precisely measured individual microtubule lengths and found that D2 binding expanded the microtubule lattice by ∼3%. Consistent with the notion that the expanded lattice is a common feature of stable microtubules, the presence of D2 slowed the microtubule depolymerization rate to ∼1/20, sug</pubmed_abstract><journal>Life science alliance</journal><pubmed_title>Preference of CAMSAP3 for expanded microtubule lattice contributes to stabilization of the minus end.</pubmed_title><pmcid>PMC9998277</pmcid><funding_grant_id>18K06147</funding_grant_id><funding_grant_id>19H05379</funding_grant_id><funding_grant_id>21H00387</funding_grant_id><pubmed_authors>Liu H</pubmed_authors><pubmed_authors>Shima T</pubmed_authors></additional><is_claimable>false</is_claimable><name>Preference of CAMSAP3 for expanded microtubule lattice contributes to stabilization of the minus end.</name><description>CAMSAPs are proteins that show microtubule minus-end-specific localization, decoration, and stabilization. Although the mechanism for minus-end recognition via their C-terminal CKK domain has been well described in recent studies, it is unclear how CAMSAPs stabilize microtubules. Our several binding assays revealed that the D2 region of CAMSAP3 specifically binds to microtubules with the expanded lattice. To investigate the relationship between this preference and the stabilization effect of CAMSAP3, we precisely measured individual microtubule lengths and found that D2 binding expanded the microtubule lattice by ∼3%. Consistent with the notion that the expanded lattice is a common feature of stable microtubules, the presence of D2 slowed the microtubule depolymerization rate to ∼1/20, sug</description><dates><release>2023-01-01T00:00:00Z</release><publication>2023 May</publication><modification>2025-04-22T06:51:39.623Z</modification><creation>2025-04-05T21:55:31.007Z</creation></dates><accession>S-EPMC9998277</accession><cross_references><pubmed>36894175</pubmed><doi>10.26508/lsa.202201714</doi></cross_references></HashMap>