July 1, 2000Journal of Biological ChemistryOpen Access

Truncation of a Mammalian Myosin I Results in Loss of Ca2+-sensitive Motility

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Population

In vitro model using baculovirus coexpression of calmodulin and an epitope-tagged 85-kDa fragment…

Comparison

Truncated mammalian myosin I (MI(1IQ)) vs Full-length 130-kDa myosin I (MI) from rat liver

Design

Preclinical

Authors

CPCynthia L. Perreault-MicaleHealthy Start ASAlexander D. ShushanBoston Biomedical Research Institute LCLynne M. ColuccioBoston University

Discussion

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Implication

Refines myosin I domain requirements for Ca2+ regulation; leaves open relevance to cardiac myocyte function in vivo.

Structured PICO

Population

In vitro model using baculovirus coexpression of calmodulin and an epitope-tagged 85-kDa fragment representing the amino-terminal catalytic 'motor' domain and the first calmodulin-binding IQ domain of rat myr-1

Intervention

Truncated mammalian myosin I (MI(1IQ))

Comparator

Full-length 130-kDa myosin I (MI(130)) from rat liver

Outcome

Actin filament translocation in vitro and its sensitivity to Ca2+ concentrationssurrogate

The study demonstrates that the calcium sensitivity of actin translocation by mammalian myosin I requires domains beyond the first IQ domain.

Cite This Study

Perreault-Micale et al. (2000) studied this question.

synapsesocial.com/papers/6a71470efebe604dd709f8be https://doi.org/10.1074/jbc.m000363200

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Truncation of a Mammalian Myosin I Results in Loss of Ca2+-sensitive Motility

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Truncation of a Mammalian Myosin I Results in Loss of Ca2+-sensitive Motility

Discussion

Member takes

Implication

Structured PICO

Cite This Study

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