Molecular cloning of the human casein kinase II .alpha. subunit

Meisner, Herman; Heller-Harrison, Robin A.; Buxton, Joanne M.; Czech, Michael P.

doi:10.1021/bi00435a066

Cited by 112 publications

(69 citation statements)

References 29 publications

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“…Its properties were extremely reminiscent of CKII isolated from other species. This was somewhat expected, in view of the greater than 97 % identity in primary structures of the a-subunits from humans and chicken, and the complete amino acid identities in their fl-subunits (Meisner et al, 1989;Jakobi et al, 1989;Maridor et al, 1991). This implies that findings from the study of sea-star CKII may be of general significance.…”

Section: Phosphorylation Of Ckii With Other Protein Kinasesmentioning

confidence: 82%

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Purification and characterization of echinoderm casein kinase II. Regulation by protein kinase C

Sanghera

Charlton

Paddon

et al. 1992

Biochemical Journal

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Casein kinase II (CKII) is one of several protein kinases that become activated before germinal-vesicle breakdown in maturing sea-star oocytes. Echinoderm CKII was purified over 11000-fold with a recovery of -10% by sequential fractionation of the oocyte cytosol on tyrosine-agarose, heparin-agarose, casein-agarose and MonoQ. The purified enzyme contained 45, 38 and 28 kDa polypeptides, which corresponded to its a, c' and , subunits respectively. The ,3-subunit was autophosphorylated on one major tryptic peptide on serine residues, whereas the a'-subunit incorporated phosphate into at least two tryptic peptides primarily on threonine residues. Western-blotting analysis of sea-star oocyte extracts with two different anti-peptide antibodies that recognized conserved regions of the a-subunit indicated that the protein levels of the a-and a'-subunits of CKII were unchanged during oocyte maturation. The purified CKII was partly inactivated (by 25 %) by preincubation with protein-serine/threonine phosphatase 2A, but protein-tyrosine phosphatases had no effect. The f-subunit of CKII was phosphorylated on a serine residue(s) up to 0.54 mol of P/mol of fl-subunit by purified protein kinase C, and this correlated with a 1.5-fold enhancement of its phosphotransferase activity with phosvitin as a substrate. CKII was not a substrate for the maturation-activated myelin basic protein kinase p44mpk from sea-star oocytes, nor for cyclic-AMP-dependent protein kinase. These studies point to possible regulation of CKII by protein phosphorylation.

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Section: Phosphorylation Of Ckii With Other Protein Kinasesmentioning

confidence: 82%

“…There are five potential CKII phosphorylation sites that are highly conserved in both the a-and a'-subunits of CKII from various organisms. In the human ac-subunit sequence, these correspond to Thr-60, Thr-96, Thr-127, Thr-129 and Thr-314 (Meisner et al, 1989). Of these, Thr-129 is the most optimal.…”

Section: Phosphorylation Of Ckii With Other Protein Kinasesmentioning

confidence: 99%

Purification and characterization of echinoderm casein kinase II. Regulation by protein kinase C

Sanghera

Charlton

Paddon

et al. 1992

Biochemical Journal

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“…Two forms of a are known designated a (M 41,000-44,000) and a' (M, 37,000-42,000) . The a and a' subunits are thought to be the catalytic subunits based on their kinase activity in the absence of the ß subunit and sequences common to other protein kinases (Hathaway et al ., 1981; Cochet and Chambaz, 1983 ;Chen-wu et al ., 1988 ;Meisner et al, 1989;. The function of the ß subunit is unknown, and it shares no extensive homology to other known protein sequences (Jakobi et al ., 1989) .…”

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confidence: 99%

Immunocytochemical localization of casein kinase II during interphase and mitosis.

Spector

Bae

et al. 1991

The Journal of Cell Biology

119

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Abstract. We have developed specific antibodies to synthetic peptide antigens that react with the individual subunits of casein kinase 11 (CKII) . Using these antibodies, we studied the localization of CKII in asynchronous HeLa cells by immunofluorescence and immunoelectron microscopy. Further studies were done on HeLa cells arrested at the Gl/S transition by hydroxyurea treatment . Our results indicate that the CKII a and ß subunits are localized in the cytoplasm C ASEIN kinase II (CKII)' is a ubiquitous protein serlne/threonine kinase found in eukaryotic cells (Edelman et al . 1987 and highly conserved among eukaryotic organisms, including Drosophila, yeast, C. elegans, bovine, and human (Saxena et al ., 1987;Chen-Wu et al ., 1988;Hu and Rubin, 1990a ;Lozeman, 1990). Casein kinase II from several species share a common polypeptide subunit structure, a2ß2, with a of M 37,000-44,000 and ß of M 24,000-28,000 by electrophoresis (Edelman et al ., 1987) . Two forms of a are known designated a (M 41,000-44,000) and a' (M, 37,000-42,000) . The a and a' subunits are thought to be the catalytic subunits based on their kinase activity in the absence of the ß subunit and sequences common to other protein kinases (Hathaway et al ., 1981; Cochet and Chambaz, 1983 ;Chen-wu et al ., 1988 ;Meisner et al., 1989;. The function of the ß subunit is unknown, and it shares no extensive homology to other known protein sequences (Jakobi et al ., 1989) . The ß subunit has a high degree of polarity with clusters ofnegative charges in the amino-terminal region and positive charge clusters in the carboxy-terminal region (Takio et al., 1987) . The basic compounds, spermine, spermidine, and polylysine, stimulate activity by interacting at least in part with the ß subunit (Traugh et al ., 1990) . This subunit may have a regulatory role in the holoenzyme (Takio et al., 1987), and evidence supporting this has been found in A-431 cells (Ackerman et al ., 1990). The comparative studies using the native CKII holoenzyme and the bacterially expressed a subunit show that the expressed a is inhibited by heparin, but it is not stimulated by polyamines and has 9% of K t of the holoenzyme (Hu and Rubin, 1990b during interphase and are distributed throughout the cell during mitosis . Further electron microscopic investigation revealed that CKII a subunit is associated with spindle fibers during metaphase and anaphase. In contrast, the CKII a' subunit is localized in the nucleus during GI and in the cytoplasm during S. Taken together, our results suggest that CKII may play significant roles in cell division control by shifting its localization between the cytoplasm and nucleus .further suggests that CKII holoenzyme is stabilized by interaction with the ß subunit .

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“…1). The major insert sequence is identical in all known mammalian sequences (Gupta and Singh, 1993;Litchfield et al, 1990;Meisner et al, 1989;Maridor et al, 1991) with only three conservative substitutions in the Drosophila sequence (Saxena et al, 1987). Similarly, the minor insert sequence is also highly conserved between species with 100% similarity existing between the human and the Drosophila sequences (Gupta and Singh, 1993;Litchfield et al, 1990 Enzyme.…”

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confidence: 98%

“…Protein kinase (EC 2.7.1.37). Meisner et al, 1989; Maridor et al, 1993;Saxena et al, 1987). The crystal structure of cell-cycle kinase (CDK2) (De Bondt et al., 1993) suggests that the major insert may be involved in subunit interactions.…”

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confidence: 99%

Insert Regions in Domain X of the Casein Kinase II Catalytic Subunit

Tiganis

House

Teh

et al. 1995

European Journal of Biochemistry

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Casein kinase 11, cyclin-dependent kinases, and glycogen synthase kinase-3 are members of the protein kinase subfamily with a prominent insert in domain X of their catalytic subunit sequence. The function of the insert sequence in casein kinase I1 was investigated utilising synthetic peptides corresponding to the insert, cross-linking experiments, and the generation of casein kinase 11 insert region mutants. The mutation of basic residues (R276+A, R278+A, R281+A, K277-+A) within the major insert sequence (PWHDILQRHSRKRWERFVHSDNQHL, positions 265 -290) did not affect alp subunit association, enzyme tetramerisation, thermal stability, and peptide (RRRDDDSDDD-NH,) phosphorylation. Similarly, replacement of residues 276-290 within the major insert with the corresponding residues from the cellcycle kinase cyclin-dependent kinase 2 (CDK2) (FPKWKPGSLASHVKN) had no significant effect. The mutation of charged residues (H232-+A, H234-+A, D235-+A) within a nearby minor insert sequence (HGHDNY, positions 232 -237), or replacement of residues 234-237 with the corresponding residues from CDK2 (DSEI) also did not affect alp subunit association and tetramerisation, but reduced enzyme thermal stability to more closely resemble the stability of the isolated a-subunit. In addition, mutations within the minor insert caused approximately a threefold increase in the apparent K,,, for peptide substrate. The results indicate that the major and minor inserts are not essential for dj3 subunit association, but the minor insert region influences substrate binding and thermal stability. Keywords. Casein kinase II; domain X; inserts.Casein kinase I1 is an essential ubiquitous serinehhreonine protein kinase that has been localised in eukaryotes to both the nucleus and the cytoplasm. The enzyme phosphorylates proteins important for cellular growth, differentiation, and metabolism. Casein kinase I1 is a heterotetramer and is typically comprised of two catalytic a (or a') subunits and two non-catalytic j3-subunits (Issinger, 1993 ;Pinna, 1990).Casein kinase I1 belongs to a subfamily of serine/threonine protein kinases including the cyclin-dependent kinases that contain insert sequences in domain X of their catalytic subunits Hanks and Quinn, 1991) (Fig. 1) Hanks and Quinn, 1991) (Fig. 1). The major insert sequence is identical in all known mammalian sequences (Gupta and Singh, 1993;Litchfield et al., 1990;Meisner et al., 1989;Maridor et al., 1991) with only three conservative substitutions in the Drosophila sequence (Saxena et al., 1987). Similarly, the minor insert sequence is also highly conserved between species with 100% similarity existing between the human and the Drosophila sequences (Gupta and Singh, 1993;Litchfield et al., 1990 Enzyme. Protein kinase (EC 2.7.1.37). Meisner et al., 1989; Maridor et al., 1993;Saxena et al., 1987). The crystal structure of cell-cycle kinase (CDK2) (De Bondt et al., 1993) suggests that the major insert may be involved in subunit interactions. In CDK2, the minor insert region forms part of the correspondin...

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Molecular cloning of the human casein kinase II .alpha. subunit

Cited by 112 publications

References 29 publications

Purification and characterization of echinoderm casein kinase II. Regulation by protein kinase C

Purification and characterization of echinoderm casein kinase II. Regulation by protein kinase C

Immunocytochemical localization of casein kinase II during interphase and mitosis.

Insert Regions in Domain X of the Casein Kinase II Catalytic Subunit

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