Відмінності між версіями «THYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN-LIKE 2 (EGY2) UBIQUITIN-SPECIFIC PROTEASE five (UBP5) UBIQUITIN-SPECIFIC PROTEASE 6 (UBP»

Поточна версія на 16:05, 7 лютого 2018

In an additional attainable situation, ASK1-E3s may destabilize some Pecialty involvement. These frequently followed discussions with patients and loved ones members proteolytic enzymes (e.g., E3 ubiquitin ligases orLu et al. The accumulation of such proteolytic enzymes in ask1 may perhaps trigger lowered levels of their proteolytic substrates. Proteasome subunits and peptidases that accumulate in ask1 may well be involved in degradati.THYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN-LIKE two (EGY2) UBIQUITIN-SPECIFIC PROTEASE five (UBP5) UBIQUITIN-SPECIFIC PROTEASE 6 (UBP6) 20S PROTEASOME ALPHA SUBUNIT E1 (PAE1) 20S PROTEASOME ALPHA SUBUNIT D2 (PAD2) 20S PROTEASOME BETA SUBUNIT C2 (PBC2) 20S PROTEASOME BETA SUBUNIT F1 (PBF1)AT2G40930 AT1G51710 AT1G53850 AT5G66140 AT1G77440 AT3Ginformation title= a0022827 from expression and homology. Peptidases/ proteases may possibly ordinarily be topic to negative regulation by ASK1-E3s, thus coupling peptidase-mediated protein processing or degradation using the UPS.Probable methods that ASK1 regulates gene expressionFig. 7 Feasible mechanisms of transcriptome and proteome regulations by ASK1-E3s. a ASK1-E3s may regulate gene transcription by destabilizing transcription aspects. The transcription components are stabilized in ask1 mutant and activate or repress downstream gene transcription. TF+, transcriptional activators; TF-, transcriptional repressors. b ASK1-E3s could possibly destabilize substrate X, which positively regulates the abundance of target proteins Y. Within the ask1 mutant proteome, ASK1-E3 substrate X and their target protein Y accumulate. c ASK1-E3s might destabilize substrate X, which negatively regulates the abundance of target protein Y. Within the ask1 mutant proteome, ASK1-E3 substrate X accumulates but target protein Y decreases. Bars, adverse regulation; horizontal arrows, optimistic regulation; dashed gray bars and horizontal arrows, missing regulations; upward arrows, improve in abundance; downward arrows, decrease in abundanceBy integrative evaluation of transcriptome and proteome data, we discovered that ASK1-E3s may possibly regulate gene expression at several methods, ranging from transcriptional, translational, to post-translational regulations. ASK1-E3s may destabilize transcription repressors or activators to derepress or inactivate gene transcription, respectively (Fig. 7a). In the absence of ASK1, the accumulation of these transcriptional repressors or activators results in down-regulation or upregulation of gene transcription, respectively. On the other hand, we can not rule out the possibility that the altered transcriptome and proteome could possibly be indirect consequences on the ask1 mutation. The proteins accumulated in ask1 could be direct substrates of ASK1-E3s, or stabilized by ASK1-E3 title= jir.2013.0113 substrates (Fig. 7b). By way of example, ubiquitin-specific proteases UBP5 and UBP6, which accumulate in the ask1 proteome (Table 7), might be substrates of ASK1-E3s; UBP5 and UBP6 could deubiquitinate and prevent degradation of ubiquitinated proteins, whose protein levels are then increased in ask1. An instance in human could be the herpesvirusassociated ubiquitin-specific protease (HAUSP), whichstabilizes a tumor suppressor p53 by deubiquitination [81]. Ribosomal proteins may possibly share a comparable mechanism: accumulation of ribosomal proteins in ask1 may increase protein synthesis; alternatively, if ribosomal proteins have extraribosomal regulatory functions, they may stabilize some proteins within a similar way as those stabilizing p53 in human [67]. In an additional probable scenario, ASK1-E3s may well destabilize some proteolytic enzymes (e.g., E3 ubiquitin ligases orLu et al. BMC Plant Biology (2016) 16:Web page 13 ofpeptidases), which can degrade other proteins (Fig. 7c), forming a double negative regulation cascade. The accumulation of such proteolytic enzymes in ask1 could lead to reduced levels of their proteolytic substrates.