PSKH1 kinase activity is differentially modulated via allosteric binding of Ca 2+ sensor proteins Article Swipe
Christopher R. Horne
,
Toby A. Dite
,
Samuel N. Young
,
Lucy J. Mather
,
Laura F. Dagley
,
Jared L. Johnson
,
Tomer M. Yaron
,
Emily M. Huntsman
,
Leonard A. Daly
,
Dominic P. Byrne
,
Antonia L. Cadell
,
Boaz H. Ng
,
Jumana Yousef
,
Dylan H. Multari
,
Lianju Shen
,
Luke M. McAloon
,
Gerard Manning
,
Mark A. Febbraio
,
Anthony R. Means
,
Lewis C. Cantley
,
Maria C. Tanzer
,
David R. Croucher
,
Claire E. Eyers
,
Patrick A. Eyers
,
John W. Scott
,
James M. Murphy
·
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1073/pnas.2420961122
YOU?
·
· 2025
· Open Access
·
· DOI: https://doi.org/10.1073/pnas.2420961122
Protein Serine Kinase H1 (PSKH1) was recently identified as a crucial factor in kidney development and is overexpressed in prostate, lung, and kidney cancers. However, little is known about PSKH1 regulatory mechanisms, leading to its classification as a “dark” kinase. Here, we used biochemistry and mass spectrometry to define PSKH1’s consensus substrate motif, protein interactors, and how interactors, including Ca 2+ sensor proteins, promote or suppress activity. Intriguingly, despite the absence of a canonical Calmodulin binding motif, Ca 2+ -Calmodulin activated PSKH1 while, in contrast, the ER-resident Ca 2+ sensor of the Cab45, Reticulocalbin, Erc55, Calumenin (CREC) family, Reticulocalbin-3, suppressed PSKH1 catalytic activity. In addition to antagonistic regulation of the PSKH1 kinase domain by Ca 2+ sensing proteins, we identified UNC119B as a protein interactor that activates PSKH1 via direct engagement of the kinase domain. Our findings identify complementary allosteric mechanisms by which regulatory proteins tune PSKH1’s catalytic activity and raise the possibility that different Ca 2+ sensors may act more broadly to tune kinase activities by detecting and decoding extremes of intracellular Ca 2+ concentrations.
Related Topics
Concepts
Allosteric regulation
Kinase
Calmodulin
Protein kinase domain
Protein kinase A
Chemistry
Cell biology
Biochemistry
Biology
Enzyme
Gene
Mutant
Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.1073/pnas.2420961122
- OA Status
- hybrid
- Cited By
- 3
- References
- 53
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4407695903
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4407695903Canonical identifier for this work in OpenAlex
- DOI
-
https://doi.org/10.1073/pnas.2420961122Digital Object Identifier
- Title
-
PSKH1 kinase activity is differentially modulated via allosteric binding of Ca 2+ sensor proteinsWork title
- Type
-
articleOpenAlex work type
- Language
-
enPrimary language
- Publication year
-
2025Year of publication
- Publication date
-
2025-02-18Full publication date if available
- Authors
-
Christopher R. Horne, Toby A. Dite, Samuel N. Young, Lucy J. Mather, Laura F. Dagley, Jared L. Johnson, Tomer M. Yaron, Emily M. Huntsman, Leonard A. Daly, Dominic P. Byrne, Antonia L. Cadell, Boaz H. Ng, Jumana Yousef, Dylan H. Multari, Lianju Shen, Luke M. McAloon, Gerard Manning, Mark A. Febbraio, Anthony R. Means, Lewis C. Cantley, Maria C. Tanzer, David R. Croucher, Claire E. Eyers, Patrick A. Eyers, John W. Scott, James M. MurphyList of authors in order
- Landing page
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https://doi.org/10.1073/pnas.2420961122Publisher landing page
- Open access
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YesWhether a free full text is available
- OA status
-
hybridOpen access status per OpenAlex
- OA URL
-
https://doi.org/10.1073/pnas.2420961122Direct OA link when available
- Concepts
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Allosteric regulation, Kinase, Calmodulin, Protein kinase domain, Protein kinase A, Chemistry, Cell biology, Biochemistry, Biology, Enzyme, Gene, MutantTop concepts (fields/topics) attached by OpenAlex
- Cited by
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3Total citation count in OpenAlex
- Citations by year (recent)
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2025: 3Per-year citation counts (last 5 years)
- References (count)
-
53Number of works referenced by this work
- Related works (count)
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10Other works algorithmically related by OpenAlex
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