Cited by 601Protein Kinase Regulation and GTPase SignalingCancer Mechanisms and TherapyCircadian rhythm and melatonin

The casein kinase 1 family: participation in multiple cellular processes in eukaryotes

Knippschild, Uwe, Gocht, Andreas, Wolff, Sonja, Huber, Nadine, Löhler, Jürgen, Stöter, Martin·2005·Cellular Signalling

Abstract

Phosphorylation of serine, threonine and tyrosine residues by cellular protein kinases plays an important role in the regulation of various cellular processes. The serine/threonine specific casein kinase 1 and 2 protein kinase families--(CK1 and CK2)--were among the first protein kinases that had been described. In recent years our knowledge of the regulation and function of mammalian CK1 kinase family members has rapidly increased. Extracellular stimuli, the subcellular localization of CK1 isoforms, their interaction with various cellular structures and proteins, as well as autophosphorylation and proteolytic cleavage of their C-terminal regulatory domains influence CK1 kinase activity. Mammalian CK1 isoforms phosphorylate many different substrates among them key regulatory proteins involved in the control of cell differentiation, proliferation, chromosome segregation and circadian rhythms. Deregulation and/or the incidence of mutations in the coding sequence of CK1 isoforms have been linked to neurodegenerative diseases and cancer. This review will summarize our current knowledge about the function and regulation of mammalian CK1 isoforms.

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Crossref · 10.1016/j.cellsig.2004.12.011

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  • PER and CRY proteins are phosphorylated by Casein Kinase I ε and δ and Glycogen Synthase Kinase 3β, leading to changes in their stability, association, and nuclear entry.

    “The PER and CRY proteins are translated in the cytoplasm, and are phosphorylated by Casein Kinase I ε and δ (CK1) and Glycogen Synthase Kinase 3β (GSK3β), leading to changes in their stability, association, and nuclear entry (Harms et al., 2003; Iitaka et al., 2005; Knippschild et al., 2005; Kurabayashi et al., 2006).”

    From Circadian genes, rhythms and the biology of mood disorders (2007) · cites this paper as Knippschild et al., 2005

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Authors
Knippschild, U., Gocht, A., Wolff, S., Huber, N., Löhler, J., & Stöter, M.
Affiliations
  • Universität Ulm (DE)
  • University Medical Center Hamburg-Eppendorf (DE)
  • Leibniz Institute of Virology (LIV) (DE)
Corresponding author
Knippschild, Uwe
Venue
Cellular Signalling
Publisher
Elsevier BV
Published
2005-06
Volume
17
Issue
6
Pages
675-689
ISSN
0898-6568 (ISSN-L)
OpenAlex
W2028867134
Cited by
601
References
235
Citations by year
2026: 21 · 2025: 25 · 2024: 40 · 2023: 20 · 2022: 27 · 2021: 34 · 2020: 35 · 2019: 25 · 2018: 21 · 2017: 23 · 2016: 29 · 2015: 28 · 2014: 36 · 2013: 25 · 2012: 24
FWCI
2.19
Type
journal article
Language
en
Open access
closed
Locations
  • Cellular Signalling (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Deutsche Forschungsgemeinschaft
  • Deutsche Krebshilfe
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Health Sciences › Medicine › Pathology and Forensic Medicine › Cancer Mechanisms and Therapy
  • Life Sciences › Neuroscience › Endocrine and Autonomic Systems › Circadian rhythm and melatonin
Keywords
casein kinase 1, casein kinase 2, serine/threonine kinase, protein phosphorylation, kinase regulation, autophosphorylation, C-terminal regulatory domain, subcellular localization, cell differentiation, cell proliferation, chromosome segregation, circadian rhythm, neurodegenerative diseases, cancer, kinase substrates
MeSH terms
Amino Acid Sequence, Animals, Cell Division, Circadian Rhythm, Humans, Mammals, Molecular Sequence Data, Nuclear Proteins, Proto-Oncogene Proteins, Signal Transduction, Tumor Suppressor Protein p53, Apoptosis, Intercellular Signaling Peptides and Proteins, Casein Kinase I, Wnt Proteins, Proto-Oncogene Proteins c-mdm2

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