The casein kinase 1 family: participation in multiple cellular processes in eukaryotes.
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The casein kinase 1 family: participation in multiple cellular processes in eukaryotes. / Knippschild, Uwe; Gocht, Andreas; Wolff, Sonja; Huber, Nadine; Löhler, Jürgen; Stöter, Martin.
in: CELL SIGNAL, Jahrgang 17, Nr. 6, 6, 2005, S. 675-689.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - The casein kinase 1 family: participation in multiple cellular processes in eukaryotes.
AU - Knippschild, Uwe
AU - Gocht, Andreas
AU - Wolff, Sonja
AU - Huber, Nadine
AU - Löhler, Jürgen
AU - Stöter, Martin
PY - 2005
Y1 - 2005
N2 - 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.
AB - 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.
M3 - SCORING: Zeitschriftenaufsatz
VL - 17
SP - 675
EP - 689
JO - CELL SIGNAL
JF - CELL SIGNAL
SN - 0898-6568
IS - 6
M1 - 6
ER -
