Journal article
Cdc42EP3-bound septin scaffolds promote actin polymerization
The Journal of biological chemistry, v 301(3), 108325
Mar 2025
PMID: 39971161
Abstract
Septins are cytoskeletal filament-forming proteins that typically associate with membranes and perform critical functions in a variety of cellular processes. Septins often colocalize with actin and microtubule structures, yet our understanding of all the ways that septins contribute mechanistically to actin- and microtubule-based functions is incomplete. The Cdc42 effector protein Cdc42EP3 (also known as BORG2) promotes septin localization to actin structures in vivo, but little else is known about how Cdc42EP3 influences the interactions of septins and F-actin. Here, using purified components, we show that Cdc42EP3 binds directly to septins, actin filaments and actin monomers. Moreover, septin-bound Cdc42EP3 accelerates actin filament polymerization. Thus, Cdc42EP3 is not merely a factor that crosslinks septins and F-actin, but one that promotes the formation of actin polymers along septin scaffolds.
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Details
- Title
- Cdc42EP3-bound septin scaffolds promote actin polymerization
- Creators
- Meagan R Tomasso - Drexel UniversityPrajakta D Mehetre - Drexel UniversityPriyashree Nagarajan - Drexel UniversityRoshni Ravi - Drexel UniversityJennifer Byrnett - Drexel UniversityEric Brinckman - Drexel UniversityJoseph Magliozzi - Brandeis UniversityBruce L Goode - Brandeis UniversityShae B Padrick - Drexel University
- Publication Details
- The Journal of biological chemistry, v 301(3), 108325
- Publisher
- Elsevier
- Number of pages
- 18
- Grant note
- College of Medicine, the Department of Biochemistry and Molecular BiologyPA Department of Health, 2018 Health Research CURE formula funds, SAP: 4100083087 NIH: R35 GM134895 NIGMS: F32 GM150204
Shae Padrick is supported by startup funds from the College of Medicine, the Department of Biochemistry and Molecular Biology and from the PA Department of Health, 2018 Health Research CURE formula funds, SAP#4100083087. Bruce Goode is supported by NIH (R35 GM134895) , and Joe Magliozzi by NIGMS (F32 GM150204) .
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Biochemistry and Molecular Biology
- Web of Science ID
- WOS:001448017800001
- Scopus ID
- 2-s2.0-86000510939
- Other Identifier
- 991022029670604721
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- Collaboration types
- Domestic collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology