<HashMap><database>biostudies-literature</database><scores/><additional><submitter>Pimm ML</submitter><funding>National Institutes of Health</funding><funding>NIH HHS</funding><funding>NIGMS NIH HHS</funding><pagination>e202305065</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC11117073</full_dataset_link><repository>biostudies-literature</repository><omics_type>Unknown</omics_type><volume>223(9)</volume><pubmed_abstract>Cell processes require precise regulation of actin polymerization that is mediated by plus-end regulatory proteins. Detailed mechanisms that explain plus-end dynamics involve regulators with opposing roles, including factors that enhance assembly, e.g., the formin mDia1, and others that stop growth (capping protein, CP). We explore IQGAP1's roles in regulating actin filament plus-ends and the consequences of perturbing its activity in cells. We confirm that IQGAP1 pauses elongation and interacts with plus ends through two residues (C756 and C781). We directly visualize the dynamic interplay between IQGAP1 and mDia1, revealing that IQGAP1 displaces the formin to influence actin assembly. Using four-color TIRF, we show that IQGAP1's displacement activity extends to formin-CP "decision comple</pubmed_abstract><journal>The Journal of cell biology</journal><pubmed_title>Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.</pubmed_title><pmcid>PMC11117073</pmcid><funding_grant_id>GM133485</funding_grant_id><funding_grant_id>R35 GM133485</funding_grant_id><pubmed_authors>Nobles AD</pubmed_authors><pubmed_authors>Haney LM</pubmed_authors><pubmed_authors>Henty-Ridilla JL</pubmed_authors><pubmed_authors>Pimm ML</pubmed_authors><pubmed_authors>Haarer BK</pubmed_authors><pubmed_authors>Marcin AG</pubmed_authors><pubmed_authors>Alcaide Eligio M</pubmed_authors></additional><is_claimable>false</is_claimable><name>Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.</name><description>Cell processes require precise regulation of actin polymerization that is mediated by plus-end regulatory proteins. Detailed mechanisms that explain plus-end dynamics involve regulators with opposing roles, including factors that enhance assembly, e.g., the formin mDia1, and others that stop growth (capping protein, CP). We explore IQGAP1's roles in regulating actin filament plus-ends and the consequences of perturbing its activity in cells. We confirm that IQGAP1 pauses elongation and interacts with plus ends through two residues (C756 and C781). We directly visualize the dynamic interplay between IQGAP1 and mDia1, revealing that IQGAP1 displaces the formin to influence actin assembly. Using four-color TIRF, we show that IQGAP1's displacement activity extends to formin-CP "decision comple</description><dates><release>2024-01-01T00:00:00Z</release><publication>2024 Sep</publication><modification>2026-06-03T06:51:25.895Z</modification><creation>2026-04-25T03:22:13.046Z</creation></dates><accession>S-EPMC11117073</accession><cross_references><pubmed>38787349</pubmed><doi>10.1083/jcb.202305065</doi></cross_references></HashMap>