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Gene Expr Patterns 2014 Jul 01;152:135-41. doi: 10.1016/j.gep.2014.06.002.
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Protein degradation machinery is present broadly during early development in the sea urchin.

Zazueta-Novoa V , Wessel GM .

Ubiquitin-dependent proteosome-mediated proteolysis is an important pathway of degradation that controls the timed destruction of cellular proteins in all tissues. All intracellular proteins and many extracellular proteins are continually being hydrolyzed to their constituent amino acids as a result of their recognition by E3 ligases for specific targeting of ubiquitination. Gustavus is a member of an ECS-type E3 ligase which interacts with Vasa, a DEAD-box RNA helicase, to regulate its localization during sea urchin embryonic development, and Gustavus mRNA accumulation is highly localized and dynamic during development. We tested if the core complex for Gustavus function was present in the embryo and if other SOCS box proteins also had restricted expression profiles that would inform future research. Expression patterns of the key members of the proteasomal function, such as the E3 core complex which interacts with Gustavus, and other E3-SOCS box proteins, are widely spread and dynamic in early development of the embryo suggesting broad core complex availability in the proteasome degradation pathway and temporal/spatial enrichments of various E3 ligase dependent targeting mechanisms.

PubMed ID: 24963879
PMC ID: PMC4125525
Article link: Gene Expr Patterns
Grant support: [+]

Genes referenced: ddx4 LOC100887844 LOC105441782 LOC578749 LOC587482 psmg1

References [+] :
Amemiya, Autoubiquitination of BCA2 RING E3 ligase regulates its own stability and affects cell migration. 2008, Pubmed