<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Kang PJ</submitter><funding>NIGMS NIH HHS</funding><pagination>1218-26</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC3635463</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>126(Pt 5)</volume><pubmed_abstract>Cells of the budding yeast Saccharomyces cerevisiae select a site for polarized growth in a specific pattern that depends on their cell type. Haploid a and α cells bud in the axial budding pattern, which requires assembly of a landmark that includes the Bud4 protein. To understand how an axial bud site is established, we performed a structure-function analysis of Bud4. Bud4 contains DUF1709 (domain of unknown function), which is similar to a part of the anillin-homology domain, and a putative Pleckstrin homology (PH) domain near to its C terminus. Although its localization depends on septins, a conserved family of GTP-binding proteins, Bud4 is necessary for the stable inheritance of septin rings during cell division. Although some anillins interact directly with septins, we find that neith</pubmed_abstract><journal>Journal of cell science</journal><pubmed_title>Coupling of septins to the axial landmark by Bud4 in budding yeast.</pubmed_title><pmcid>PMC3635463</pmcid><funding_grant_id>R01 GM076375</funding_grant_id><funding_grant_id>R01-GM76375</funding_grant_id><pubmed_authors>Hood-DeGrenier JK</pubmed_authors><pubmed_authors>Kang PJ</pubmed_authors><pubmed_authors>Park HO</pubmed_authors></additional><is_claimable>false</is_claimable><name>Coupling of septins to the axial landmark by Bud4 in budding yeast.</name><description>Cells of the budding yeast Saccharomyces cerevisiae select a site for polarized growth in a specific pattern that depends on their cell type. Haploid a and α cells bud in the axial budding pattern, which requires assembly of a landmark that includes the Bud4 protein. To understand how an axial bud site is established, we performed a structure-function analysis of Bud4. Bud4 contains DUF1709 (domain of unknown function), which is similar to a part of the anillin-homology domain, and a putative Pleckstrin homology (PH) domain near to its C terminus. Although its localization depends on septins, a conserved family of GTP-binding proteins, Bud4 is necessary for the stable inheritance of septin rings during cell division. Although some anillins interact directly with septins, we find that neith</description><dates><release>2013-01-01T00:00:00Z</release><publication>2013 Mar</publication><modification>2025-04-19T09:07:25.996Z</modification><creation>2019-03-27T01:07:50Z</creation></dates><accession>S-EPMC3635463</accession><cross_references><pubmed>23345395</pubmed><doi>10.1242/jcs.118521</doi></cross_references></HashMap>