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Phosphorylation of axonemal 21 kDa and 26 kDa proteins modulates activation of sperm motility in the ascidian, Ciona intestinalis

Published online by Cambridge University Press:  16 July 2018

Mamoru Nomura
Affiliation:
Misaki Marine Biological Station, Graduate School of Science, University of Tokyo, Misaki, Miura, Kanagawa 238-0225, Japan
Kazuo Inaba
Affiliation:
Asamushi Marine Biological Station, Faculty of Science, Tohoku University, Asamushi, Aomori 039-3501, Japan
Masaaki Morisawa
Affiliation:
Misaki Marine Biological Station, Graduate School of Science, University of Tokyo, Misaki, Miura, Kanagawa 238-0225, Japan

Extract

Protein phosphorylation is highly coupled with sperm motility activation in several animal species. The micro-tubule based flagellar motor protein, dynein, is a candidate for a phosphoprotein related to sperm activation in many animal species (Morisawa & Hayashi, 1985; Hayashi et al., 1987; Dey & Brokaw, 1991; Stephens & Prior, 1992; Inaba et al., 1998, 1999). Sperm motility of the ascidians Ciona intestinalis and C. savignyi is activated by a factor derived from unfertilised eggs named sperm activating and attracting factor (SAAF). SAAF elevates the intracellular cyclic AMP (cAMP) level by a mechanism dependent on membrane hyperpolarisation and extracellular Ca2+ (Yoshida et al., 1994; Izumi et al., 1999). Experiments using demembranated Ciona sperm showed that cAMP is required prior to ATP for the activation of axonemal movement (Opreska & Brokaw, 1983; Morisawa et al., 1984; Brokaw, 1985; Dey & Brokaw, 1991; Chaudhry et al., 1995) and that many sperm flagellar proteins including dynein light chain are phosphorylated during incubation of demembranated sperm with ATP and cAMP (Dey & Brokaw, 1991). However, there is no evidence of which proteins are phosphorylated during the SAAF-dependent activation of Ciona sperm motility.

Type
Special Lecture for Citizens
Copyright
Copyright © Cambridge University Press 1999

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