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-49549
Methods Mol Biol 2021 Jan 01;2219:119-135. doi: 10.1007/978-1-0716-0974-3_7.
Show Gene links Show Anatomy links

Identification of SH2 Domain-Mediated Protein Interactions that Operate at Fertilization in the Sea Star Patiria miniata.

Bates L , Wiseman E , Kitson J , Carroll DJ .


Abstract
The signaling mechanisms controlling internal calcium release at fertilization in animals are still largely unknown. Echinoderms, such as the sea star Patiria miniata, produce abundant and easily accessible sperm and eggs. In addition, eggs are naturally synchronized at the same cell cycle stage, collectively making these animals an attractive model to study the signaling proteins controlling fertilization. However, the lack of antibodies to identify proteins in this model system has slowed progress in identifying key signaling molecules. With the advances in mass spectrometry, we present a method for identifying tyrosine phosphorylated proteins binding to GST-tagged SH2 domains in sea star cell lysates for downstream mass spectrometry analysis.

PubMed ID: 33074537
Article link: Methods Mol Biol
Grant support: [+]


References :
Stoica, The amino-terminal Src homology 2 domain of phospholipase C gamma 1 is essential for TCR-induced tyrosine phosphorylation of phospholipase C gamma 1. 1998, Pubmed