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Article

Phosphorylation of the cyclin CaPcl5 modulates both cyclin stability and specific recognition of the substrate.

Journal of molecular biology - 9 Sept 2013

Simon Einav, Gildor Tsvia, Kornitzer Daniel

Abstract excerpt

The Candida albicans cyclin CaPcl5 activates the cyclin-dependent kinase Pho85 and induces phosphorylation of the transcription factor CaGcn4, leading to its degradation. The high substrate specificity of the CaPcl5/Pho85 complex provides the opportunity to study the determinants of substrate selectivity of cyclins. Mutational analysis of CaPcl5 suggests that residues in a predicted α-helix at the N-terminal end...

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Source

Identifiers

PMID: 23763991
DOI: 10.1016/j.jmb.2013.06.004

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Phosphorylation of the cyclin CaPcl5 modulates both cyclin stability and specific recognition of the substrate.PMID 23763991Read ↗

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