Відмінності між версіями «THYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN-LIKE two (EGY2) UBIQUITIN-SPECIFIC PROTEASE 5 (UBP5) UBIQUITIN-SPECIFIC PROTEASE 6 (UBP»

Поточна версія на 10:09, 30 січня 2018

a ASK1-E3s may possibly LY2510924 site regulate gene transcription by destabilizing transcription factors. An instance in human could be the herpesvirusassociated ubiquitin-specific protease (HAUSP), whichstabilizes a tumor suppressor p53 by deubiquitination [81]. Ribosomal proteins may well share a related mechanism: accumulation of ribosomal proteins in ask1 may perhaps improve protein synthesis; alternatively, if ribosomal proteins have extraribosomal regulatory functions, they may stabilize some proteins inside a similar way as those stabilizing p53 in human [67]. In yet another doable situation, ASK1-E3s may perhaps 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 trigger reduced levels of their proteolytic substrates. Proteasome subunits and peptidases that accumulate in ask1 may possibly be involved in degradati.THYLENE-DEPENDENT GRAVITROPISM-DEFICIENT AND YELLOW-GREEN-LIKE 2 (EGY2) UBIQUITIN-SPECIFIC PROTEASE 5 (UBP5) UBIQUITIN-SPECIFIC PROTEASE six (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 generally be topic to damaging regulation by ASK1-E3s, therefore coupling peptidase-mediated protein processing or degradation with all the UPS.Attainable strategies that ASK1 regulates gene expressionFig. 7 Achievable mechanisms of transcriptome and proteome regulations by ASK1-E3s. a ASK1-E3s could regulate gene transcription by destabilizing transcription components. The transcription variables are stabilized in ask1 mutant and activate or repress downstream gene transcription. TF+, transcriptional activators; TF-, transcriptional repressors. b ASK1-E3s may 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 could possibly 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, negative regulation; horizontal arrows, positive regulation; dashed gray bars and horizontal arrows, missing regulations; upward arrows, enhance in abundance; downward arrows, reduce in abundanceBy integrative evaluation of transcriptome and proteome information, we identified that ASK1-E3s could regulate gene expression at multiple measures, ranging from transcriptional, translational, to post-translational regulations. ASK1-E3s may well destabilize transcription repressors or activators to derepress or inactivate gene transcription, respectively (Fig. 7a). Within the absence of ASK1, the accumulation of these transcriptional repressors or activators benefits in down-regulation or upregulation of gene transcription, respectively. However, we can't rule out the possibility that the altered transcriptome and proteome could possibly be indirect consequences from the ask1 mutation. The proteins accumulated in ask1 could possibly be direct substrates of ASK1-E3s, or stabilized by ASK1-E3 title= jir.2013.0113 substrates (Fig. 7b). For instance, ubiquitin-specific proteases UBP5 and UBP6, which accumulate inside the ask1 proteome (Table 7), could possibly be substrates of ASK1-E3s; UBP5 and UBP6 could deubiquitinate and avert degradation of ubiquitinated proteins, whose protein levels are then improved in ask1. An instance in human is definitely the herpesvirusassociated ubiquitin-specific protease (HAUSP), whichstabilizes a tumor suppressor p53 by deubiquitination [81].