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Pregled bibliografske jedinice broj: 713202

Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues


Shi, Lei; Pigeonneau, Nathalie; Ravikumar, Vaishnavi; Dobrinic, Paula; Macek, Boris; Franjevic, Damjan; Noirot-gros, Marie-Françoise; Mijakovic, Ivan
Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues // Frontiers in Microbiology, 5 (2014), 495; 1-13 doi:10.3389/fmicb.2014.00495 (međunarodna recenzija, članak, znanstveni)


CROSBI ID: 713202 Za ispravke kontaktirajte CROSBI podršku putem web obrasca

Naslov
Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues

Autori
Shi, Lei ; Pigeonneau, Nathalie ; Ravikumar, Vaishnavi ; Dobrinic, Paula ; Macek, Boris ; Franjevic, Damjan ; Noirot-gros, Marie-Françoise ; Mijakovic, Ivan

Izvornik
Frontiers in Microbiology (1664-302X) 5 (2014), 495; 1-13

Vrsta, podvrsta i kategorija rada
Radovi u časopisima, članak, znanstveni

Ključne riječi
Protein phosphorylation; bacterial protein kinase; protein kinase cross-talk; phosphorylation cascade; kinase activation

Sažetak
Bacteria possess protein serine/threonine and tyrosine kinases which resemble eukaryal kinases in their capacity to phosphorylate multiple substrates. We hypothesized that the analogy might extend further, and bacterial kinases may also undergo mutual phosphorylation and activation, which is currently considered as a hallmark of eukaryal kinase networks. In order to test this hypothesis, we explored the capacity of all members of four different classes of serine/threonine and tyrosine kinases present in the firmicute model organism Bacillus subtilis to phosphorylate each other in vitro and interact with each other in vivo. The interactomics data suggested a high degree of connectivity among all types of kinases, while phosphorylation assays revealed equally wide-spread cross-phosphorylation events. Our findings suggest that the Hanks-type kinases PrkC, PrkD and YabT exhibit the highest capacity to phosphorylate other B. subtilis kinases, while the BY-kinase PtkA and the two- component-like kinases RsbW and SpoIIAB show the highest propensity to be phosphorylated by other kinases. Analysis of phosphorylated residues on several selected recipient kinases suggests that most cross-phosphorylation events concern key regulatory residues. Therefore, cross- phosphorylation events are very likely to influence the capacity of recipient kinases to phosphorylate substrates downstream in the signal transduction cascade. We therefore conclude that bacterial serine/threonine and tyrosine kinases probably engage in a network-type behavior previously described only in eukaryal cells.

Izvorni jezik
Engleski



POVEZANOST RADA


Profili:

Avatar Url Paula Dobrinić (autor)

Avatar Url Damjan Franjević (autor)

Avatar Url Ivan Mijaković (autor)

Poveznice na cjeloviti tekst rada:

doi http journal.frontiersin.org

Citiraj ovu publikaciju:

Shi, Lei; Pigeonneau, Nathalie; Ravikumar, Vaishnavi; Dobrinic, Paula; Macek, Boris; Franjevic, Damjan; Noirot-gros, Marie-Françoise; Mijakovic, Ivan
Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues // Frontiers in Microbiology, 5 (2014), 495; 1-13 doi:10.3389/fmicb.2014.00495 (međunarodna recenzija, članak, znanstveni)
Shi, L., Pigeonneau, N., Ravikumar, V., Dobrinic, P., Macek, B., Franjevic, D., Noirot-gros, M. & Mijakovic, I. (2014) Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues. Frontiers in Microbiology, 5 (495), 1-13 doi:10.3389/fmicb.2014.00495.
@article{article, author = {Shi, Lei and Pigeonneau, Nathalie and Ravikumar, Vaishnavi and Dobrinic, Paula and Macek, Boris and Franjevic, Damjan and Noirot-gros, Marie-Fran\c{c}oise and Mijakovic, Ivan}, year = {2014}, pages = {1-13}, DOI = {10.3389/fmicb.2014.00495}, keywords = {Protein phosphorylation, bacterial protein kinase, protein kinase cross-talk, phosphorylation cascade, kinase activation}, journal = {Frontiers in Microbiology}, doi = {10.3389/fmicb.2014.00495}, volume = {5}, number = {495}, issn = {1664-302X}, title = {Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues}, keyword = {Protein phosphorylation, bacterial protein kinase, protein kinase cross-talk, phosphorylation cascade, kinase activation} }
@article{article, author = {Shi, Lei and Pigeonneau, Nathalie and Ravikumar, Vaishnavi and Dobrinic, Paula and Macek, Boris and Franjevic, Damjan and Noirot-gros, Marie-Fran\c{c}oise and Mijakovic, Ivan}, year = {2014}, pages = {1-13}, DOI = {10.3389/fmicb.2014.00495}, keywords = {Protein phosphorylation, bacterial protein kinase, protein kinase cross-talk, phosphorylation cascade, kinase activation}, journal = {Frontiers in Microbiology}, doi = {10.3389/fmicb.2014.00495}, volume = {5}, number = {495}, issn = {1664-302X}, title = {Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues}, keyword = {Protein phosphorylation, bacterial protein kinase, protein kinase cross-talk, phosphorylation cascade, kinase activation} }

Časopis indeksira:


  • Web of Science Core Collection (WoSCC)
    • Science Citation Index Expanded (SCI-EXP)
    • SCI-EXP, SSCI i/ili A&HCI
  • Scopus


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  • BIOSIS Previews (Biological Abstracts)
  • Science Citation Index Expanded


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