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Updated: Jul 17, 2026

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Aip1p Dynamics Are Altered by the R256H Mutation in Actin

Published on: July 30, 2014

Caspase-11 regulates cell migration by promoting Aip1-Cofilin-mediated actin depolymerization.

Juying Li¹, William M Brieher, M Lucila Scimone

¹Department of Cell Biology, Harvard Medical School, 240 Longwood Ave, Boston, MA 02115, USA.

Nature Cell Biology

|February 13, 2007

Summary

Caspase-11 regulates cell migration during inflammation by interacting with Aip1 to control actin dynamics. This discovery reveals a new caspase-mediated pathway essential for cell movement in mammals.

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Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry

Measuring Caspase Activity Using a Fluorometric Assay or Flow Cytometry

Published on: March 24, 2023

Area of Science:

Immunology
Cell Biology
Biochemistry

Background:

Inflammatory responses require coordinated regulation of cell migration, cytokine maturation, and apoptosis.
Caspases, cysteine proteases, are key regulators of cytokine maturation and apoptosis.
The role of specific caspases in cell migration during inflammation remains incompletely understood.

Purpose of the Study:

To investigate the role of caspase-11 in regulating mammalian cell migration during inflammation.
To elucidate the molecular mechanism by which caspase-11 influences cell migration.
To identify novel interacting partners of caspase-11 involved in cytoskeletal regulation.

Main Methods:

Generation and analysis of caspase-11-deficient lymphocytes.
In vitro and in vivo migration assays.
Co-immunoprecipitation and biochemical assays to study protein-protein interactions.
Actin depolymerization assays.
Analysis of actin dynamics in cells deficient for caspase-11 or Aip1.

Main Results:

Caspase-11-deficient lymphocytes exhibit impaired cell migration both in vitro and in vivo.
Caspase-11 physically and functionally interacts with actin interacting protein 1 (Aip1).
The CARD domain of caspase-11 binds to the WD40 propeller domain of Aip1, promoting cofilin-mediated actin depolymerization.
Deficiency in either caspase-11 or Aip1 leads to defects in actin dynamics.
Caspase-11 and Aip1 cooperate to enhance cofilin-mediated actin depolymerization.

Conclusions:

Caspase-11 plays a crucial, cell-autonomous role in regulating mammalian cell migration during inflammation.
A novel caspase-mediated pathway involving caspase-11 and Aip1 controls actin dynamics and cell migration.
This mechanism is distinct from the known receptor-mediated Rho-Rac-Cdc42 pathway.