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dc.contributor.author
Bauer, Angelika F.
dc.contributor.author
Sonzogni, Silvina Veronica
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dc.contributor.author
Meyer, Lucas
dc.contributor.author
Zeuzem, Stefan
dc.contributor.author
Piiper, Albrecht
dc.contributor.author
Biondi, Ricardo Miguel
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dc.contributor.author
Neimanis, Sonja
dc.date.available
2023-10-31T14:02:35Z
dc.date.issued
2012-06
dc.identifier.citation
Bauer, Angelika F.; Sonzogni, Silvina Veronica; Meyer, Lucas; Zeuzem, Stefan; Piiper, Albrecht; et al.; Regulation of protein kinase C-related Protein Kinase 2 (PRK2) by an intermolecular PRK2-PRK2 interaction mediated by its N-terminal domain; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 287; 24; 6-2012; 20590-20602
dc.identifier.issn
0021-9258
dc.identifier.uri
http://hdl.handle.net/11336/216618
dc.description.abstract
Protein kinase C-related protein kinases (PRKs) are effectors of the Rho family of small GTPases and play a role in the development of diseases such as prostate cancer and hepatitis C. Here we examined the mechanism underlying the regulation of PRK2 by its N-terminal region. We show that the N-terminal region of PRK2 prevents the interaction with its upstream kinase, the 3-phosphoinositide-dependent kinase 1 (PDK1), which phosphorylates the activation loop of PRK2. We confirm that the N-terminal region directly inhibits the kinase activity of PRK2. However, in contrast to previous models, our data indicate that this inhibition is mediated in trans through an intermolecular PRK2-PRK2 interaction. Our results also suggest that amino acids 487-501, located in the linker region between the N-terminal domains and the catalytic domain, contribute to the PRK2-PRK2 dimer formation. This dimerization is further supported by other N-terminal domains. Additionally, we provide evidence that the region C-terminal to the catalytic domain intramolecularly activates PRK2. Finally, we discovered that the catalytic domain mediates a cross-talk between the inhibitory N-terminal region and the activating C-terminal region. The results presented here describe a novel mechanism of regulation among AGC kinases and offer new insights into potential approaches to pharmacologically regulate PRK2.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society for Biochemistry and Molecular Biology
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dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
PRK2
dc.subject
REGULATION
dc.subject
DIMER
dc.subject
PDK1
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
Regulation of protein kinase C-related Protein Kinase 2 (PRK2) by an intermolecular PRK2-PRK2 interaction mediated by its N-terminal domain
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2023-04-19T17:26:02Z
dc.journal.volume
287
dc.journal.number
24
dc.journal.pagination
20590-20602
dc.journal.pais
Estados Unidos
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dc.journal.ciudad
Bethesda
dc.description.fil
Fil: Bauer, Angelika F.. Goethe Universitat Frankfurt; Alemania
dc.description.fil
Fil: Sonzogni, Silvina Veronica. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; Argentina. Goethe Universitat Frankfurt; Alemania
dc.description.fil
Fil: Meyer, Lucas. Goethe Universitat Frankfurt; Alemania
dc.description.fil
Fil: Zeuzem, Stefan. Goethe Universitat Frankfurt; Alemania
dc.description.fil
Fil: Piiper, Albrecht. Goethe Universitat Frankfurt; Alemania
dc.description.fil
Fil: Biondi, Ricardo Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria; Argentina. Goethe Universitat Frankfurt; Alemania
dc.description.fil
Fil: Neimanis, Sonja. Goethe Universitat Frankfurt; Alemania
dc.journal.title
Journal of Biological Chemistry (online)
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dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/287/24/20590.long
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.M111.327437
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