A novel &amp;lt;italic&amp;gt;Physarum polycephalum&amp;lt;/italic&amp;gt; SR protein kinase specifically phosphorylates the RS domain of the human SR protein, ASF/SF2

Liu, Shide; Kang, Kang; Zhang, Jianhua; Ouyang, Qiuling; Zhou, Zhuolong; Tian, Sijia; Xing, Miao

doi:10.1093/abbs/gmp054

Cited by 8 publications

(5 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…TcSRPK, the SR protein kinase of a protozoan, the parasite Trypanosoma cruzi , which displays trans‐ and cis‐splicing and was cloned and characterized in 2003, functions as a bona fide SR protein kinase, indicating that the general control of eukaryotic mRNA processing evolved early during evolution [22]. More recently, PSRPK, the SR protein kinase of Physarum polycephalum , a slime mold, has been cloned and characterized, especially with respect to its subcellular localization properties [23].…”

Section: History Of the Discovery Of The Serine‐arginine Protein Kinamentioning

confidence: 99%

Serine-arginine protein kinases: a small protein kinase family with a large cellular presence

et al. 2011

View full text Add to dashboard Cite

History of the discovery of the serine-arginine protein kinase (SPRK) familyThe first serine-arginine (SR) protein kinase to be purified and characterized was named SRPK1, for SR-protein-specific kinase 1 [1,2]. It was isolated during a search for the activity that phosphorylates SR splicing factors (also named SR proteins) during mitosis. SRPK1 was shown to phosphorylate SR proteins in a cell-cycle regulated manner, to affect SR protein localization and to inhibit splicing when added in large quantities to a cell-free splicing assay [1,2]. The SRPK1 cDNA was cloned, revealing that the Schizosaccharomyces pombe SRPK1 orthologue, Dsk1, had already been cloned and partially characterized as a kinase with cell cycle-dependent phosphorylation and subcellular localization [3]. The SRPK1 and Dsk1 nucleotide sequencing identified a domain interrupting the kinase catalytic site into two structural entities, Serine-arginine protein kinases (SPRKs) constitute a relatively novel subfamily of serine-threonine kinases that specifically phosphorylate serine residues residing in serine-arginine ⁄ arginine-serine dipeptide motifs. Fifteen years of research subsequent to the purification and cloning of human SRPK1 as a SR splicing factor-phosphorylating protein have lead to the accumulation of information on the function and regulation of the different members of this family, as well as on the genomic organization of SRPK genes in several organisms. Originally considered to be devoted to constitutive and alternative mRNA splicing, SRPKs are now known to expand their influence to additional steps of mRNA maturation, as well as to other cellular activities, such as chromatin reorganization in somatic and sperm cells, cell cycle and p53 regulation, and metabolic signalling. Similarly, SRPKs were considered to be constitutively active kinases, although several modes of regulation of their function have been demonstrated, implying an elaborate cellular control of their activity. Finally, SRPK gene sequence information from bioinformatics data reveals that SRPK gene homologs exist either in single or multiple copies in every single eukaryotic organism tested, emphasizing the importance of SRPK protein function for cellular life.Abbreviations CDK, cyclin dependent kinase; Clk, CDK-like kinase; CK2, casein kinase 2; FOXO1, forkhead box protein O1; HBV, hepatitis B virus; HP1, heterochromatin protein 1; Hsp, heat shock protein; LBR, lamin B receptor; NRF-1, nuclear respiratory factor-1; PGC-1, peroxisome proliferator activated receptor c coactivator-1; RS, arginine-serine; SAFB, scaffold attachment factor B; SR, serine-arginine; SRPK, serine-arginine protein kinase.

show abstract

Section: History Of the Discovery Of The Serine‐arginine Protein Kinamentioning

confidence: 99%

Serine-arginine protein kinases: a small protein kinase family with a large cellular presence

et al. 2011

View full text Add to dashboard Cite

show abstract

“…However, their functions were studied only in the fungal plant pathogens Fusarium graminearum, Physarum polycephalum, and Puccinia striiformis f. sp. Tritici (Liu et al, 2009;Cheng et al, 2015;Wang et al, 2018) and in the model yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe. Both model yeasts have only a single SRPK-like protein: Dsk1 in S.pombe regulates mitosis and pre-mRNA splicing (Takeuchi and Yanagida, 1993;Tang et al, 1998;Tang et al, 2007), whereas Sky1 in S. cerevisiae (ScSky1) broadly regulates cellular functions.…”

Section: Introductionmentioning

confidence: 99%

Candida albicans SR-Like Protein Kinases Regulate Different Cellular Processes: Sky1 Is Involved in Control of Ion Homeostasis, While Sky2 Is Important for Dipeptide Utilization

Brandt

Gerwien

Wagner

et al. 2022

Front. Cell. Infect. Microbiol.

View full text Add to dashboard Cite

Protein kinases play a crucial role in regulating cellular processes such as growth, proliferation, environmental adaptation and stress responses. Serine-arginine (SR) protein kinases are highly conserved in eukaryotes and regulate fundamental processes such as constitutive and alternative splicing, mRNA processing and ion homeostasis. The Candida albicans genome encodes two (Sky1, Sky2) and the Candida glabrata genome has one homolog (Sky1) of the human SR protein kinase 1, but their functions have not yet been investigated. We used deletion strains of the corresponding genes in both fungi to study their cellular functions. C. glabrata and C. albicans strains lacking SKY1 exhibited higher resistance to osmotic stress and toxic polyamine concentrations, similar to Saccharomyces cerevisiae sky1Δ mutants. Deletion of SKY2 in C. albicans resulted in impaired utilization of various dipeptides as the sole nitrogen source. Subsequent phosphoproteomic analysis identified the di- and tripeptide transporter Ptr22 as a potential Sky2 substrate. Sky2 seems to be involved in Ptr22 regulation since overexpression of PTR22 in the sky2Δ mutant restored the ability to grow on dipeptides and made the cells more susceptible to the dipeptide antifungals Polyoxin D and Nikkomycin Z. Altogether, our results demonstrate that C. albicans and C. glabrata Sky1 protein kinases are functionally similar to Sky1 in S. cerevisiae, whereas C. albicans Sky2, a unique kinase of the CTG clade, likely regulates dipeptide uptake via Ptr22.

show abstract

“…Interestingly, all mutation sites are observed in the kinase domains of PsSRPKL . Kinase domains in SRPKs are proven to be closely associated with phosphorylating their targets (SR proteins) (Liu et al ., ). Thus, we think that corresponding SR protein(s) may be altered in different Pst isolates due to the non‐synonymous substitutions.…”

Section: Discussionmentioning

confidence: 97%

Characterization of protein kinase PsSRPKL, a novel pathogenicity factor in the wheat stripe rust fungus

Cheng

Wang

Yao

et al. 2015

Environmental Microbiology

View full text Add to dashboard Cite

As in other eukaryotes, protein kinases (PKs) are generally evolutionarily conserved and play major regulatory roles in plant pathogenic fungi. Many PKs have been proven to be important for pathogenesis in model fungal plant pathogens, but little is currently known about their roles in the pathogenesis of cereal rust fungi, devastating pathogens in agriculture worldwide. Here, we report on an in planta highly induced PK gene PsSRPKL from the wheat stripe rust fungus Puccinia striiformis f. sp. tritici (Pst), one of the most important cereal rust fungi. PsSRPKL belongs to a group of PKs that are evolutionarily specific to cereal rust fungi. It shows a high level of intraspecies polymorphism in the kinase domains and directed green fluorescent protein chimers to plant nuclei. Overexpression of PsSRPKL in fission yeast induces aberrant cell morphology and a decreased resistance to environmental stresses. Most importantly, PsSRPKL is proven to be an important pathogenicity factor responsible for fungal growth and responses to environmental stresses, therefore contributing significantly to Pst virulence in wheat. We hypothesize that cereal rust fungi have developed specific PKs as pathogenicity factors for adaptation to their host species during evolution. Thus, our findings provide significant insights into pathogenicity and virulence evolution in cereal rust fungi.

show abstract

A novel <italic>Physarum polycephalum</italic> SR protein kinase specifically phosphorylates the RS domain of the human SR protein, ASF/SF2

Cited by 8 publications

References 29 publications

Serine-arginine protein kinases: a small protein kinase family with a large cellular presence

Serine-arginine protein kinases: a small protein kinase family with a large cellular presence

Candida albicans SR-Like Protein Kinases Regulate Different Cellular Processes: Sky1 Is Involved in Control of Ion Homeostasis, While Sky2 Is Important for Dipeptide Utilization

Characterization of protein kinase PsSRPKL, a novel pathogenicity factor in the wheat stripe rust fungus

Contact Info

Product

Resources

About