UBIQUITIN-SPECIFIC PROTEASE16 interacts with a HEAVY METAL ASSOCIATED ISOPRENYLATED PLANT PROTEIN27 and modulates cadmium tolerance
UBIQUITIN-SPECIFIC PROTEASE16 interacts with a HEAVY METAL ASSOCIATED ISOPRENYLATED PLANT PROTEIN27 and modulates cadmium tolerance
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DOI:
10.4161/psb.25680
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发表时间:
2013-07
影响因子:
2.9
通讯作者:
Jinfeng Zhao;Huapeng Zhou;Xueyong Li
中科院分区:
文献类型:
--
作者:
Jinfeng Zhao;Huapeng Zhou;Xueyong Li
Protein ubiquitination and deubiquitination are two reversible processes catalyzed by ubiquitin ligases and deubiquitinating enzymes, respectively. In Arabidopsis, lots of substrates of ubiquitin ligases were found, whereas only a few targets of deubiquitinating enzymes were identified. Recently, we reported that a functional UBIQUITIN-SPECIFIC PROTEASE16 (UBP16) was involved in salt tolerance through positively regulating plasma membrane Na+/H+ antiport activity and at least partially modulating SERINE HYDROXYMETHYLTRANSFERASE1 (SHM1) stability and activity. Here, we report that UBP16 interacts with HEAVY METAL ASSOCIATED ISOPRENYLATED PLANT PROTEIN27 (HIPP27), a metallochaperone containing a predicted heavy-metal-associated domain, which has been reported to play an important role in cadmium detoxification. Meanwhile, the ubp16 mutant showed more sensitive to cadmium than wild-type. Taken together, HIPP27 may be another target of UBP16 in cadmium response.