The DOI matches its Crossref record; 61 of the 62 references it cites were found in a registry or an index.
Calcineurin-dependent regulation of Crz1p nuclear export requires Msn5p and a conserved calcineurin docking site
Open accessAbstract
Calcineurin, a conserved Ca 2+/calmodulin-regulated protein phosphatase, plays a crucial role in Ca 2+ signaling in a wide variety of cell types. In Saccharomyces cerevisiae, calcineurin positively regulates transcription in response to stress by dephosphorylating the transcription factor Crz1p/Tcn1p. Dephosphorylation promotes Crz1p nuclear localization in part by increasing the efficiency of its nuclear import. In this work, we show that calcineurin-dependent dephosphorylation of Crz1p also down-regulates its nuclear export. Using a genetic approach, we identify Msn5p as the exportin for Crz1p. In addition, we define the Crz1p nuclear export signal (NES) and show that it interacts with Msn5p in a phosphorylation-dependent manner. This indicates that calcineurin regulates Crz1p nuclear export by dephosphorylating and inactivating its NES. Finally, we define a motif in Crz1p, PIISIQ, similar to the PxIxIT docking site for calcineurin on the mammalian transcription factor NFAT, that mediates the in vivo interaction between calcineurin and Crz1p and is required for calcineurin-dependent regulation of Crz1p nuclear export and activity. Therefore, in yeast as in mammals, a docking site is required to target calcineurin to its substrate such that it can dephosphorylate it efficiently.
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“much likely the cell components involved in this nucleo-cytoplasmic shuffling, which have been already identified in S. cerevisiae (Polizotto and Cyert 2001;Boustany and Cyert 2002), are conserved in C. albicans.”
From Functional characterization of the Candida albicans CRZ1 gene encoding a calcineurin-regulated transcription factor (2005) · cites this paper as Boustany and Cyert 2002
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Metadata
- Authors
- Boustany, L. M., & Cyert, M. S.
- Affiliations
- Stanford University (US)
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2002-03-01
- Volume
- 16
- Issue
- 5
- Pages
- 608-619
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- PMC
- PMC155349
- OpenAlex
- W2110510554
- Cited by
- 115
- References
- 62
- Citations by year
- 2025: 1 · 2024: 1 · 2023: 1 · 2022: 2 · 2021: 3 · 2019: 1 · 2017: 3 · 2016: 7 · 2015: 4 · 2014: 6 · 2013: 5 · 2012: 6
- Type
- posted content
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes & Development (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (5 T32 GM07276, GM-48729, T32GM007276, R01GM048729)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Keywords
- calcineurin, nuclear export, nuclear export signal, protein dephosphorylation, NFAT, transcription factor regulation, Ca2+/calmodulin signaling, Saccharomyces cerevisiae, exportins
- MeSH terms
- Binding Sites, Carrier Proteins, Cell Nucleus, DNA-Binding Proteins, Mutation, Protein Binding, Saccharomyces cerevisiae, Transcription Factors, Trans-Activators, Conserved Sequence, Sequence Deletion, Calcineurin, Amino Acid Motifs, Protein Sorting Signals, Active Transport, Cell Nucleus, Karyopherins, Saccharomyces cerevisiae Proteins
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