TY  - GEN
T1  - Caspar SUMOylation regulates Drosophila lifespan
AU  - Kaduskar, Bhagyashree
AU  - Trivedi, Deepti
AU  - Ratnaparkhi, Girish S
DO  - 10.17912/micropub.biology.000288
UR  - http://beta.micropublication.org/journals/biology/micropub-biology-000288/
AB  - Conjugation of Small ubiquitin-like modifier (SUMO) to a protein substrate (also called SUMOylation) is achieved by a specialized cellular machinery that includes a SUMO maturing enzyme (Ulp1, Ubiquitin-like protease 1) which also doubles as a de-conjugase, heterodimeric activation enzymes (Aos1 & Uba2), a single E2 conjugase (Ubc9), and multiple E3 ligases (Hay, 2005). Loss of function ubc9 mutants shows activated immune signaling (Chiu et al., 2005; Paddibhatla et al., 2010), with Toll signaling attenuated by SUMO conjugation (Bhaskar et al., 2002; Chiu et al., 2005; Paddibhatla et al., 2010). Although multiple studies have confirmed the role of SUMOylation in the regulation of Drosophila innate immune signaling (Bhaskar et al., 2000); Bhaskar et al., 2002; Chiu et al., 2005), only a handful of proteins have been identified as direct targets of SUMOylation. Validated direct targets include Dorsal (Bhaskar et al., 2002), and IRD5 (Fukuyama et al., 2013), critical proteins in the Toll/NFkB and IMD/NFkB cascades, respectively. Previously, to gain a more elaborate understanding of the SUMO conjugation in the immune response, we performed a quantitative proteomic analysis and identified proteins whose SUMOylation status is altered in response to crude LPS, which activates both Toll/NFkB and IMD/NFkB signaling in Drosophila macrophage-like S2 cells. This analysis identified ~700 SUMO targets of which 5% were known to have immune function (Handu et al., 2015).
PY  - 2020
JO  - microPublication Biology
ER  -