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Functional and Ecological Effects of Isoform Variation in Insect Flight Muscle

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:
James H. Marden


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Nearly all of the known structural molecules in insect flight muscles exist as multiple isoforms. Both post-transcriptional and post-translational mechanisms are responsible for this variability. Among these mechanisms, alternative splicing is noteworthy for the ability to create a large number of combinatorial arrangements of alternative exons. For example there are over 1K possible distinct combinations of the characterized isoforms of troponin-T and projectin, which are just two of the many alternatively spliced proteins in insect muscle. The potential number of combinatorial possibilities for larger suites of insect muscle proteins is exponentially larger, i.e., numbers that far exceed the total number of coding genes in the insect genome. Thus, isoform variation is a potent source of variation in insect flight muscle and other tissue types, and the control of alternative splicing and other mechanisms that generate protein isoforms is a likely target of natural selection. Presently we know very little about the realized extent of this potential to generate protein variation, and no studies have yet examined constraints such as coordinate regulation of isoform expression of multiple protein species within insect flight muscles.

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