- Information
- Symbol: MHZ3
- MSU: LOC_Os06g02480
- RAPdb: Os06g0115200
- Publication
- Membrane protein MHZ3 stabilizes OsEIN2 in rice by interacting with its Nramp-like domain., 2018, Proc Natl Acad Sci U S A.
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Genbank accession number
- Key message
- The association of MHZ3 with the Nramp-like domain is crucial for OsEIN2 accumulation, demonstrating the significance of the OsEIN2 transmembrane domains in ethylene signaling
- Together, these results suggest that ethylene-induced MHZ3 stabilizes OsEIN2 likely by binding to its Nramp-like domain and impeding protein ubiquitination to facilitate ethylene signal transduction
- Connection
- MHZ3, OsEIN2, Membrane protein MHZ3 stabilizes OsEIN2 in rice by interacting with its Nramp-like domain., Membrane protein MHZ3 stabilizes OsEIN2 in rice by interacting with its Nramp-like domain.
- MHZ3, OsEIN2, Membrane protein MHZ3 stabilizes OsEIN2 in rice by interacting with its Nramp-like domain., MHZ3 physically interacts with OsEIN2, and both the N- and C-termini of MHZ3 specifically associate with the OsEIN2 Nramp-like domain
- MHZ3, OsEIN2, Membrane protein MHZ3 stabilizes OsEIN2 in rice by interacting with its Nramp-like domain., Loss ofmhz3function reduces OsEIN2 abundance and attenuates ethylene-induced OsEIN2 accumulation, whereasMHZ3overexpression elevates the abundance of both wild-type and mutated OsEIN2 proteins, suggesting that MHZ3 is required for proper accumulation of OsEIN2 protein
- MHZ3, OsEIN2, Membrane protein MHZ3 stabilizes OsEIN2 in rice by interacting with its Nramp-like domain., The association of MHZ3 with the Nramp-like domain is crucial for OsEIN2 accumulation, demonstrating the significance of the OsEIN2 transmembrane domains in ethylene signaling
- MHZ3, OsEIN2, Membrane protein MHZ3 stabilizes OsEIN2 in rice by interacting with its Nramp-like domain., Moreover, MHZ3 negatively modulates OsEIN2 ubiquitination, protecting OsEIN2 from proteasome-mediated degradation
- MHZ3, OsEIN2, Membrane protein MHZ3 stabilizes OsEIN2 in rice by interacting with its Nramp-like domain., Together, these results suggest that ethylene-induced MHZ3 stabilizes OsEIN2 likely by binding to its Nramp-like domain and impeding protein ubiquitination to facilitate ethylene signal transduction
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