Control of mammalian G protein signaling by N-terminal acetylation and the N-end rule pathway
- Authors
- Park, Sang-Eun; Kim, Jeong-Mok; Seok, Ok-Hee; Cho, Hanna; Wadas, Brandon; Kim, Seon-Young; Varshavsky, Alexander; Hwang, Cheol-Sang
- Issue Date
- Mar-2015
- Publisher
- AMER ASSOC ADVANCEMENT SCIENCE
- Citation
- SCIENCE, v.347, no.6227, pp.1249 - 1252
- Indexed
- SCIE
SCOPUS
- Journal Title
- SCIENCE
- Volume
- 347
- Number
- 6227
- Start Page
- 1249
- End Page
- 1252
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/25619
- DOI
- 10.1126/science.aaa3844
- ISSN
- 0036-8075
- Abstract
- Rgs2, a regulator of G proteins, lowers blood pressure by decreasing signaling through G alpha(q). Human patients expressing Met-Leu-Rgs2 (ML-Rgs2) or Met-Arg-Rgs2 (MR-Rgs2) are hypertensive relative to people expressing wild-type Met-Gln-Rgs2 (MQ-Rgs2). We found that wild-type MQ-Rgs2 and its mutant, MR-Rgs2, were destroyed by the Ac/N-end rule pathway, which recognizes N-alpha-terminally acetylated (Nt-acetylated) proteins. The shortest-lived mutant, ML-Rgs2, was targeted by both the Ac/N-end rule and Arg/N-end rule pathways. The latter pathway recognizes unacetylated N-terminal residues. Thus, the Nt-acetylated Ac-MX-Rgs2 (X = Arg, Gln, Leu) proteins are specific substrates of the mammalian Ac/N-end rule pathway. Furthermore, the Ac/N-degron of Ac-MQ-Rgs2 was conditional, and Teb4, an endoplasmic reticulum (ER) membrane-embedded ubiquitin ligase, was able to regulate G protein signaling by targeting Ac-MX-Rgs2 proteins for degradation through their N-alpha-terminal acetyl group.
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