Calcineurin-dependent nuclear import of the transcription factor Crz1p requires Nmd5p
Open accessAbstract
Calcineurin is a conserved Ca2+/calmodulin-specific serine-threonine protein phosphatase that mediates many Ca2+-dependent signaling events. In yeast, calcineurin dephosphorylates Crz1p, a transcription factor that binds to the calcineurin-dependent response element, a 24-bp promoter element. Calcineurin-dependent dephosphorylation of Crz1p alters Crz1p nuclear localization. This study examines the mechanism by which calcineurin regulates the nuclear localization of Crz1p in more detail. We describe the identification and characterization of a novel nuclear localization sequence (NLS) in Crz1p, which requires both basic and hydrophobic residues for activity, and show that the karyopherin Nmd5p is required for Crz1p nuclear import. We also demonstrate that the binding of Crz1p to Nmd5p is dependent upon its phosphorylation state, indicating that nuclear import of Crz1p is regulated by calcineurin. Finally, we demonstrate that residues in both the NH2- and COOH-terminal portions of Crz1p are required for regulated Crz1p binding to Nmd5p, supporting a model of NLS masking for regulating Crz1p nuclear import.
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The cell components involved in nucleo-cytoplasmic shuffling, already identified in S. cerevisiae, are conserved in C. albicans.
“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 Polizotto and Cyert 2001
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- Authors
- Polizotto, R. S., & Cyert, M. S.
- Affiliations
- Department of Biological Sciences, Stanford University, Stanford, CA 94305
- Stanford University (US)
- ORCID
- Cyert, Martha S.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2001-09-03
- Volume
- 154
- Issue
- 5
- Pages
- 951-960
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2196176
- OpenAlex
- W1991532862
- Cited by
- 63
- References
- 46
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 3 · 2022: 5 · 2021: 2 · 2019: 1 · 2018: 1 · 2016: 3 · 2015: 2 · 2014: 2 · 2013: 5
- FWCI
- 1.63
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM-48728)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- calcineurin, nuclear import, nuclear localization signal, karyopherins, Ca2+/calmodulin signaling, Saccharomyces cerevisiae
- MeSH terms
- Amino Acid Sequence, Cell Nucleus, DNA-Binding Proteins, Fungal Proteins, Guanosine Triphosphate, Molecular Sequence Data, Nuclear Proteins, Protein Binding, Recombinant Fusion Proteins, Transcription Factors, Yeasts, Immunoblotting, Trans-Activators, Zinc Fingers, Protein Structure, Tertiary, Genes, Reporter, Calcineurin, Nuclear Localization Signals, Monomeric GTP-Binding Proteins, Protein Sorting Signals, Active Transport, Cell Nucleus, Saccharomyces cerevisiae Proteins
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