Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Echinobase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
Cell Motil Cytoskeleton 2000 Jun 01;462:129-36. doi: 10.1002/1097-0169(200006)46:2<129::AID-CM5>3.0.CO;2-C.
Show Gene links Show Anatomy links

Effect of calyculin A on the surface structure of unfertilized sea urchin eggs.

Tosuji H , Miyaji K , Fusetani N , Nakazawa T .

Calyculin A, a potent inhibitor of type 1 and type 2A protein phosphatases, induces contractile ring formation when applied to unfertilized sea urchin eggs [Tosuji et al., 1992: Proc. Natl. Acad. Sci. USA 89:10613-10617]. We report here the elongation of microvilli in the unfertilized eggs exposed to calyculin A. The elongated microvilli and associated sperm-egg binding sites (egg receptor for sperm) then became concentrated into a constriction site corresponding to the cleavage furrow. The egg receptor for sperm was also in close connection to the microfilaments. Okadaic acid is another known inhibitor of protein phosphatase type-1 and type-2A. Its effect, however, is about a hundredfold feebler for type-1 phosphatase than type-2A. Even after treatment with okadaic acid, no change was observed, suggesting that these morphological changes were induced by calyculin A solely though its inhibitory effect on the type-1 protein phosphatase.

PubMed ID: 10891858
Article link: Cell Motil Cytoskeleton

Genes referenced: LOC100887844 LOC100893523 LOC575557