Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 2000 Nov 1;351(Pt 3):765–768.

Novel consensus sequence for the Golgi apparatus casein kinase, revealed using proline-rich protein-1 (PRP1)-derived peptide substrates.

A M Brunati 1, O Marin 1, A Bisinella 1, A Salviati 1, L A Pinna 1
PMCID: PMC1221417  PMID: 11042132

Abstract

Previous studies have shown that the Golgi apparatus casein kinase (G-CK) recognizes phosphoacceptor sites specified by the triplet SXE/Sp, which is found in several phosphoproteins, besides casein itself. In the present study, we report that G-CK can phosphorylate, with comparable efficiency, sequences surrounding Ser-22 of salivary proline-rich protein-1 (PRP1), which do not conform to the SXE/Sp motif. By using a series of peptide substrates derived from the PRP1 Ser-22 site, we also have shown that the optimal consensus sequence recognized by G-CK in this case was SXQXX(D/E)3, where the acidic residues at positions n+5 to n+7 and, to a lesser extent, the glutamine residue at position n+2 are the critical determinants.

Full Text

The Full Text of this article is available as a PDF (111.7 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Aitken A. 14-3-3 and its possible role in co-ordinating multiple signalling pathways. Trends Cell Biol. 1996 Sep;6(9):341–347. doi: 10.1016/0962-8924(96)10029-5. [DOI] [PubMed] [Google Scholar]
  2. Brunati A. M., Contri A., Muenchbach M., James P., Marin O., Pinna L. A. GRP94 (endoplasmin) co-purifies with and is phosphorylated by Golgi apparatus casein kinase. FEBS Lett. 2000 Apr 14;471(2-3):151–155. doi: 10.1016/s0014-5793(00)01378-8. [DOI] [PubMed] [Google Scholar]
  3. Drzymala L., Castle A., Cheung J. C., Bennick A. Cellular phosphorylation of an acidic proline-rich protein, PRP1, a secreted salivary phosphoprotein. Biochemistry. 2000 Feb 29;39(8):2023–2031. doi: 10.1021/bi9924213. [DOI] [PubMed] [Google Scholar]
  4. Fields G. B., Noble R. L. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids. Int J Pept Protein Res. 1990 Mar;35(3):161–214. doi: 10.1111/j.1399-3011.1990.tb00939.x. [DOI] [PubMed] [Google Scholar]
  5. Gross S. D., Anderson R. A. Casein kinase I: spatial organization and positioning of a multifunctional protein kinase family. Cell Signal. 1998 Nov;10(10):699–711. doi: 10.1016/s0898-6568(98)00042-4. [DOI] [PubMed] [Google Scholar]
  6. Guerra B., Issinger O. G. Protein kinase CK2 and its role in cellular proliferation, development and pathology. Electrophoresis. 1999 Feb;20(2):391–408. doi: 10.1002/(SICI)1522-2683(19990201)20:2<391::AID-ELPS391>3.0.CO;2-N. [DOI] [PubMed] [Google Scholar]
  7. Lasa-Benito M., Marin O., Meggio F., Pinna L. A. Golgi apparatus mammary gland casein kinase: monitoring by a specific peptide substrate and definition of specificity determinants. FEBS Lett. 1996 Mar 11;382(1-2):149–152. doi: 10.1016/0014-5793(96)00136-6. [DOI] [PubMed] [Google Scholar]
  8. Lasa M., Chang P. L., Prince C. W., Pinna L. A. Phosphorylation of osteopontin by Golgi apparatus casein kinase. Biochem Biophys Res Commun. 1997 Nov 26;240(3):602–605. doi: 10.1006/bbrc.1997.7702. [DOI] [PubMed] [Google Scholar]
  9. Lasa M., Marin O., Pinna L. A. Rat liver Golgi apparatus contains a protein kinase similar to the casein kinase of lactating mammary gland. Eur J Biochem. 1997 Feb 1;243(3):719–725. doi: 10.1111/j.1432-1033.1997.00719.x. [DOI] [PubMed] [Google Scholar]
  10. Meggio F., Boulton A. P., Marchiori F., Borin G., Lennon D. P., Calderan A., Pinna L. A. Substrate-specificity determinants for a membrane-bound casein kinase of lactating mammary gland. A study with synthetic peptides. Eur J Biochem. 1988 Nov 1;177(2):281–284. doi: 10.1111/j.1432-1033.1988.tb14374.x. [DOI] [PubMed] [Google Scholar]
  11. Meggio F., Perich J. W., Meyer H. E., Hoffmann-Posorske E., Lennon D. P., Johns R. B., Pinna L. A. Synthetic fragments of beta-casein as model substrates for liver and mammary gland casein kinases. Eur J Biochem. 1989 Dec 22;186(3):459–464. doi: 10.1111/j.1432-1033.1989.tb15229.x. [DOI] [PubMed] [Google Scholar]
  12. Mercier J. C. Phosphorylation of caseins, present evidence for an amino acid triplet code posttranslationally recognized by specific kinases. Biochimie. 1981 Jan;63(1):1–17. doi: 10.1016/s0300-9084(81)80141-1. [DOI] [PubMed] [Google Scholar]
  13. Moore A., Boulton A. P., Heid H. W., Jarasch E. D., Craig R. K. Purification and tissue-specific expression of casein kinase from the lactating guinea-pig mammary gland. Eur J Biochem. 1985 Nov 4;152(3):729–737. doi: 10.1111/j.1432-1033.1985.tb09254.x. [DOI] [PubMed] [Google Scholar]
  14. Murphy J. E., Hanover J. A., Froehlich M., DuBois G., Keen J. H. Clathrin assembly protein AP-3 is phosphorylated and glycosylated on the 50-kDa structural domain. J Biol Chem. 1994 Aug 19;269(33):21346–21352. [PubMed] [Google Scholar]
  15. Newman L. S., McKeever M. O., Okano H. J., Darnell R. B. Beta-NAP, a cerebellar degeneration antigen, is a neuron-specific vesicle coat protein. Cell. 1995 Sep 8;82(5):773–783. doi: 10.1016/0092-8674(95)90474-3. [DOI] [PubMed] [Google Scholar]
  16. Pinna L. A., Meggio F. Protein kinase CK2 ("casein kinase-2") and its implication in cell division and proliferation. Prog Cell Cycle Res. 1997;3:77–97. doi: 10.1007/978-1-4615-5371-7_7. [DOI] [PubMed] [Google Scholar]
  17. Pinna L. A., Ruzzene M. How do protein kinases recognize their substrates? Biochim Biophys Acta. 1996 Dec 12;1314(3):191–225. doi: 10.1016/s0167-4889(96)00083-3. [DOI] [PubMed] [Google Scholar]
  18. Plowman G. D., Sudarsanam S., Bingham J., Whyte D., Hunter T. The protein kinases of Caenorhabditis elegans: a model for signal transduction in multicellular organisms. Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):13603–13610. doi: 10.1073/pnas.96.24.13603. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Price P. A., Rice J. S., Williamson M. K. Conserved phosphorylation of serines in the Ser-X-Glu/Ser(P) sequences of the vitamin K-dependent matrix Gla protein from shark, lamb, rat, cow, and human. Protein Sci. 1994 May;3(5):822–830. doi: 10.1002/pro.5560030511. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Wong R. S., Bennick A. The primary structure of a salivary calcium-binding proline-rich phosphoprotein (protein C), a possible precursor of a related salivary protein A. J Biol Chem. 1980 Jun 25;255(12):5943–5948. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES