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.
Echinobase
ECB-ART-35657
Comp Biochem Physiol B Biochem Mol Biol 1995 Mar 01;1103:493-502. doi: 10.1016/0305-0491(94)00212-d.
Show Gene links Show Anatomy links

A diversity of enzymes involved in the regulation of reversible tyrosine phosphorylation in sea urchin eggs and embryos.

Wessel GM , Clark F , Berg L .


???displayArticle.abstract???
Reversible tyrosine phosphorylation is involved in the fertilization reaction and early embryogenesis of the sea urchin (Foltz and Shilling, 1993; Ramachandran et al., 1993). To determine the enzymes present that may be involved in this regulation, we used a PCR screen to identify sequences that encode protein tyrosine kinases (PTK) and protein tyrosine phosphatases (PTP). We identified five PTKs and eight PTPs using cDNA libraries from two sea urchin species at two different stages of development, and the similarities to known PTK and PTP amino acid sequences ranged from 70 to 95%. The cognate proteins represented both "receptor"-class and cytoplasmic enzymes. Using RNAse protection assays we found that the respective mRNAs showed many accumulation profiles that we have grouped into three basic patterns: (1) mRNA levels that do not vary by more than two to three times throughout development; (2) mRNA levels highest in eggs or ovaries; and (3) mRNA levels highest in gastrula or pluteus stages. mRNAs specific to adult somatic cells of the ovary were not found, nor were mRNAs that accumulated selectively at the blastula stage. The results show that a diversity of enzymes involved in the regulation of reversible tyrosine phosphorylation is present in eggs and embryos of the sea urchin and that the differential accumulation in development of each mRNA suggests specific functional responsibilities by members of these enzyme families.

???displayArticle.pubmedLink??? 7584825
???displayArticle.link??? Comp Biochem Physiol B Biochem Mol Biol
???displayArticle.grants??? [+]

Genes referenced: LOC100887844