Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.
IQGAP1
actin
capping protein
formin
Journal
bioRxiv : the preprint server for biology
Titre abrégé: bioRxiv
Pays: United States
ID NLM: 101680187
Informations de publication
Date de publication:
05 May 2023
05 May 2023
Historique:
pubmed:
19
5
2023
medline:
19
5
2023
entrez:
19
5
2023
Statut:
epublish
Résumé
Cell processes require precise regulation of actin polymerization at filament plus ends to execute normal functions. The detailed mechanisms used to control filament assembly at plus ends in the presence of diverse and often opposing regulators is not clear. Here we explore and identify residues important for the plus-end related activities of IQGAP1. In multi-wavelength TIRF assays, we directly visualize dimers of IQGAP1, mDia1, and CP on filament ends alone and as a multicomponent end binding complex. IQGAP1 promotes the turnover of end-binding proteins reducing the dwell times of CP, mDia1, or mDia1-CP 'decision complexes' by 8-18-fold. Loss of these activities in cells disrupts actin filament arrays, morphology, and migration. Together, our results reveal a role for IQGAP1 in promoting protein turnover on filament ends and provide new insights into how actin assembly is regulated in cells.
Identifiants
pubmed: 37205555
doi: 10.1101/2023.05.04.539490
pmc: PMC10187324
pii:
doi:
Types de publication
Preprint
Langues
eng
Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM133485
Pays : United States
Déclaration de conflit d'intérêts
Declaration of interests The authors declare that they have no known competing financial or personal interests relevant to this work.
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