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The Journal of Experimental Biology 204, 2627-2635 (2001)
© 2001 The Company of Biologists Limited

The neuropeptide proctolin induces phosphorylation of a 30 kDa protein associated with the thin filament in crustacean muscle

Berit Brüstle1, Sabine Kreissl1,*, Donald L. Mykles2 and Werner Rathmayer1

1 Department of Biology, University of Konstanz, D-78457 Konstanz, Germany, and
2 Department of Biology, Colorado State University, Fort Collins, CO 80523, USA

*Author for correspondence (e-mail: s.kreissl{at}uni-konstanz.de)

Accepted May 14, 2001

In the isopod Idotea emarginata, the neuropeptide proctolin is contained in a single pair of motoneurones located in pereion ganglion 4. The two neurones supply dorsal extensor muscle fibres of all segments. Proctolin (1µmoll-1) potentiates the amplitude of contractures of single extensor muscle fibres elicited by 10mmoll-1 caffeine. In western blots of myofibrillar proteins isolated from single muscle fibres and treated with an anti-phosphoserine antibody, a protein with an apparent molecular mass of 30kDa was consistently found. The phosphorylation of this protein was significantly increased by treating the fibres with proctolin. After separation of myofibrillar filaments, a 30kDa protein was found only in the thin filament fraction. This protein is phosphorylated and detected by an antiserum against crustacean troponin I.

Key words: Idotea emarginata, nervous system, motoneurone, modulation, actin, myosin, troponin I, contraction, caffeine.




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© The Company of Biologists Ltd 2001