Plant Peroxisomal Protein Kinases Implicated in Stress‐Related Responses

Kataya, Amr R.A.; Hu, Jianping; Muench, Douglas G.; Moorhead, Greg B. G.

doi:10.1002/9781119541578.ch22

Cited by 1 publication

(2 citation statements)

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“…In addition, several kinase transcripts are found either induced or suppressed in response to external perturbations such as biotic and abiotic stresses ( Supplementary Figure 12 ). Peroxisomes are now known to be involved in several stress response pathways through the synthesis of a jasmonic acid (JA) precursor via 12-oxophytodienoate reductase isoform 3 (OPR3) and β-oxidation, and salicylic acid (SA) signaling and antifungal defense through the peroxisomal enzyme PEN2 myrosinase (reviewed in ( Kataya et al, 2020b )). Several protein kinases (K11, K12, K14, and K15) show higher expression, not only under fungal and bacterial infections, but also when plants are exposed to different elicitors such as FLG22 and GST-NPP1 and to SA ( Supplementary Figure 12 ), suggesting these kinases are involved in peroxisome-dependent defense responses.…”

Section: Resultsmentioning

confidence: 99%

“…The CTR1 PTD may normally be masked letting the enzyme reside in the ER, then under certain conditions, it is exposed to allow peroxisome import. Indeed, CTR1 was suggested to be quarantined in peroxisomes under stress, which could be an alternative strategy for the cell to regulate stress responses ( Sorhagen et al, 2013 ; Kataya et al, 2020b ). K6 (CDKB2-1), a soluble cyclin-dependent protein kinase, partially targets peroxisomes and is annotated to be involved in the regulation of cell division ( Gutierrez, 2009 ).…”

Section: Discussionmentioning

confidence: 99%

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Identification of Arabidopsis Protein Kinases That Harbor Functional Type 1 Peroxisomal Targeting Signals

Kataya

Gautam

Jamshed

et al. 2022

Front. Cell Dev. Biol.

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Peroxisomes are eukaryotic specific organelles that perform diverse metabolic functions including fatty acid β-oxidation, reactive species metabolism, photorespiration, and responses to stress. However, the potential regulation of these functions by post-translational modifications, including protein phosphorylation, has had limited study. Recently, we identified and catalogued a large number of peroxisomal phosphorylated proteins, implicating the presence of protein kinases in this organelle. Here, we employed available prediction models coupled with sequence conservation analysis to identify 31 protein kinases from the Arabidopsis kinome (all protein kinases) that contain a putative, non-canonical peroxisomal targeting signal type 1 (PTS1). From this, twelve C-terminal domain-PTS1s were demonstrated to be functional in vivo, targeting enhanced yellow fluorescent protein to peroxisomes, increasing the list of presumptive peroxisomal protein kinases to nineteen. Of the twelve protein kinases with functional PTS1s, we obtained full length clones for eight and demonstrated that seven target to peroxisomes in vivo. Screening homozygous mutants of the presumptive nineteen protein kinases revealed one candidate (GPK1) that harbors a sugar-dependence phenotype, suggesting it is involved in regulating peroxisomal fatty acid β-oxidation. These results present new opportunities for investigating the regulation of peroxisome functions.

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Section: Resultsmentioning

confidence: 99%