October 1, 1996The Journal of Cell BiologyOpen Access

Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides.

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Population

In vitro models using purified capping proteins and actin

Comparison

Polyphosphoinositides and proposed regulators vs Control conditions without polyphosphoinositides…

Design

Preclinical

Authors

DSDorothy A. SchaferUniversity of North Carolina at Chapel Hill PJPaul B. JenningsMonmouth Medical Center JCJohn A. CooperNorthwestern University

Discussion

Member takes

Implication

PIP2/PIP may stimulate actin polymerization via uncapping; leaves open in vivo relevance and any cardiovascular implications.

Structured PICO

Population

In vitro models using purified capping proteins (CP-beta1 from chicken skeletal muscle, CP-beta2 from chicken kidney and brain) and actin (alpha-actin from chicken skeletal muscle, beta-actin from bovine erythrocytes, beta/gamma-actin from chicken brain)

Intervention

Polyphosphoinositides (PIP2, PIP, PIP3) and proposed regulators (Hsc70, S100)

Comparator

Control conditions without polyphosphoinositides or regulators

Outcome

Kinetics of capping protein binding to and dissociating from actin filament barbed ends (on-rate, off-rate, dissociation constants)

PIP2 and PIP rapidly uncap actin filament barbed ends in vitro, suggesting a potential mechanism for stimulating actin polymerization in vivo.

Cite This Study

Schafer et al. (1996) studied this question.

synapsesocial.com/papers/6a88539f2c11edba2ecf20ef https://doi.org/10.1083/jcb.135.1.169

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Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides.

Discussion

Member takes

Implication

Structured PICO

Cite This Study

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Also Consider