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Chapter category: Development

Actin and Arthrin

This chapter appears in the following book:

Nature's Versatile Engine: Insect Flight Muscle Inside and Out

Edited by: Jim O. Vigoreaux
ISBN: 0-387-25798-5
» Get more information about this book at landesbioscience.com «

Chapter authors:
John C. Sparrow

Filamentous actin forms the core of all muscle thin filaments and is an integral part of the acto-myosin motor system that powers muscle contraction. Muscle actin isoforms show considerable sequence conservation compared to all actins, but insect actins form a distinct group. Within insect actins the flight muscle actin sequences do not form a statistically distinct group. The flight muscle actins have biochemical properties and post-translational modifications almost indistinguishable from those of vertebrate muscle actins. The major exception is the specific mono-ubiquitination of some flight muscle-specific actins through a single isopeptide bond at a specific actin lysine residue to form arthrin. Though the ability to carry out this modification seems to have arisen de novo at least twice in insect evolution it is not required for flight and a specific function remains elusive. The close conservation of insect actins with all other actins, the presence of a single indirect flight muscle-specific isoform encoded by the Act88F gene in Drosophila, that is not required for any other vital functions (and thus does not affect viability), has allowed this particular insect flight muscle actin to play a major role in the molecular genetic study of actin function.

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Additional chapters from this book:

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