TY  - GEN
T1  - Inner Nuclear Membrane Asi Ubiquitin Ligase Catalytic Subunits Asi1p and Asi3p, but not Asi2p, confer resistance to aminoglycoside hygromycin B in Saccharomyces cerevisiae
AU  - Woodruff, Kelsey A
AU  - Richards, Kyle A
AU  - Evans, Melissa D
AU  - Scott, Abigail R
AU  - Voas, Brian M
AU  - Irelan, Courtney Broshar
AU  - Olesen, James B
AU  - Smaldino, Philip J
AU  - Rubenstein, Eric M
DO  - 10.17912/micropub.biology.000403
UR  - http://beta.micropublication.org/journals/biology/micropub-biology-000403/
AB  - Organelle proteome maintenance is essential for eukaryotic life. Several dedicated proteolytic systems promote organelle-specific turnover of misfolded or excess proteins. Inner nuclear membrane (INM) proteins are targeted for proteasomal destruction via INM-associated degradation (INMAD). At least three ubiquitin ligases mediate INMAD in the budding yeast Saccharomyces cerevisiae. These include the Asi complex, Doa10p, and the anaphase promoting complex (Deng and Hochstrasser, 2006; Foresti et al., 2014; Khmelinskii et al., 2014; Koch et al., 2019). Asi is composed of three subunits, Asi1p, Asi2p, and Asi3p (Foresti et al., 2014; Khmelinskii et al., 2014). Asi1p and Asi3p possess catalytic Really Interesting New Gene (RING) domains, while Asi2p serves as an adaptor for a subset of Asi substrates (Foresti et al., 2014; Khmelinskii et al., 2014; Natarajan et al., 2020).
PY  - 2021
JO  - microPublication Biology
ER  -