Casein Kinases: An Atypical Class of Ubiquitous and Pleiotropic Protein Kinases

Pinna, Lorenzo A.; Meggio, Flavio; Marin, Oriano; Perich, John W.; Boldyreff, Brigitte; Issinger, O.-G.

doi:10.1007/978-3-0348-7315-4_24

Cited by 5 publications

(2 citation statements)

References 17 publications

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“…1). Six potential casein kinase I/II phosphorylation sites (D/E‐X‐X‐S/T and S/T‐X‐X‐D/E) (19–22) also were found at amino acid positions 57, 226, 253, 278, 292 and 293 (Fig. 1).…”

Section: Resultsmentioning

confidence: 99%

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A novel rat dentin mRNA coding only for dentin sialoprotein

Ritchie

2001

European J Oral Sciences

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Dentin sialoprotein (DSP) is a major glycoprotein present in the mineralized dentin matrix that is expressed mainly by young and mature odontoblasts. Mutations in the DSP coding regions are linked to Dentinogenesis imperfecta I and II. indicating the importance of DSP in tooth formation. Previous studies have identified multiple mRNA transcripts in dentin that code for both DSP and phosphophoryns (PPs). Using reverse transcriptase-polymerase chain reaction (RT-PCR) to characterize these mRNA transcripts, we have identified a cDNA that codes for DSP, but not PP. This cDNA codes for a protein with 324 amino acids, 303 amino acids being identical to the published rat DSP sequence. However, the subsequent 21 amino acids are unique to this cDNA. Based on the coding sequence, the core protein is predicted to have a pI=4.24, a net charge of -34, and to contain four potential N-glycosylation sites and six potential sites for phosphorylation by casein kinase. That the corresponding mRNA was present in day 5 molar tooth germs was confirmed using RNA protection assays. These data, therefore, identify a novel transcript in rat tooth germs that codes only for DSP (designated as DSPII).

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Section: Resultsmentioning

confidence: 99%

“…Four potential N‐glycosylation sites (i.e., Asn‐X‐Ser) (17, 18) are underlined and in bold font. Six potential casein kinase I and II phosphorylation sites (D/E‐X‐X‐S/T and S/T‐X‐X‐D/E) (19–22) are underlined and shaded. D: Asp, E: Glu, X: any amino acid, S: Ser, T: Thr.…”

Section: Resultsmentioning

confidence: 99%

A novel rat dentin mRNA coding only for dentin sialoprotein

Ritchie

2001

European J Oral Sciences

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Protein kinase CK2 (“casein kinase-2”) and its implication in cell division and proliferation

Pinna

Meggio

1997

Progress in Cell Cycle Research

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Protein kinase CK2 (also termed casein kinase-2 or -IT) is a ubiquitous Ser/Thr-specific protein kinase required for viability and for cell cycle progression. CK2 is especially elevated in proliferating tissues, either normal or transformed, and the expression of its catalytic subunit in transgenic mice is causative of lymphomas. CK2 is highly pleiotropic: more than 160 proteins phosphorylated by it at sites specified by multiple acidic residues are known. Despite its heterotetrameric structure generally composed by two catalytic (a and/or a') and two non catalytic ~-subunits, the regulation of CK2 is still enigmatic. A number of functional features of the ~-subunit which could cooperate to the modulation of CK2 targeting/activity will be discussed.

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Protein kinase

Springer Handbook of Enzymes

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Casein Kinases: An Atypical Class of Ubiquitous and Pleiotropic Protein Kinases

Cited by 5 publications

References 17 publications

A novel rat dentin mRNA coding only for dentin sialoprotein

A novel rat dentin mRNA coding only for dentin sialoprotein

Protein kinase CK2 (“casein kinase-2”) and its implication in cell division and proliferation

Protein kinase

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