# Actin filament mechanics and branched network turnover

> **NIH NIH R35** · YALE UNIVERSITY · 2020 · $41,503

## Abstract

SUMMARY
The assembly of actin filaments into Arp2/3 complex-branched filament networks powers numerous
fundamental eukaryotic cellular processes, including motility, endocytosis, and cytokinesis. Members of the
actin depolymerization factor homology (ADF-H)-domain protein family, which includes cofilin and glial
maturation factor (GMF), accelerate branched actin filament network reorganization and turnover. Cofilin and
GMF accelerate network remodeling by debranching Arp 2/3 complex. Cofilin accelerates network turnover by
fragmenting filaments and increasing the concentration of filament ends where subunits add and dissociate.
This MIRA proposal integrates biochemical and biophysical approaches, including electron cryo-microscopy,
microfluidics, and a recently developed microscopic magnetic cylinders assay, to develop predictive models of
actin filament and filament network mechanics, remodeling and fragmentation. General principles regarding the
relationship between actin filament elasticity, conformation and regulatory protein occupancy will emerge from
this work.

## Key facts

- **NIH application ID:** 10147485
- **Project number:** 3R35GM136656-01S1
- **Recipient organization:** YALE UNIVERSITY
- **Principal Investigator:** ENRIQUE M DE LA CRUZ
- **Activity code:** R35 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2020
- **Award amount:** $41,503
- **Award type:** 3
- **Project period:** 2020-04-06 → 2025-01-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10147485

## Citation

> US National Institutes of Health, RePORTER application 10147485, Actin filament mechanics and branched network turnover (3R35GM136656-01S1). Retrieved via AI Analytics 2026-05-23 from https://api.ai-analytics.org/grant/nih/10147485. Licensed CC0.

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