Home LiteratureArticle Details
PMID: 11042132 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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

The Biochemical journal ·Vol. 351 Pt 3 ·2000-11-01 ·Pages 765-8

Brunati AM, Marin O, Bisinella A, Salviati A, Pinna LA

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.

MeSH Terms
Amino Acid Sequence Casein Kinases Consensus Sequence Golgi Apparatus/enzymology Kinetics Molecular Sequence Data Peptides/metabolism Proline-Rich Protein Domains Protein Kinases/chemistry,isolation & purification,metabolism Substrate Specificity
Chemicals
Peptides Protein Kinases Casein Kinases
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Brunati A M
Dipartimento di Chimica Biologica, Centro per lo Studio delle Biomembrane del CNR and CRIBI, Università degli Studi di Padova, Viale G. Colombo 3, 35121 Padova, Italy.
Marin O
Bisinella A
Salviati A
Pinna L A
References (20)
20 references, click to expand
  1. Protein kinase CK2 and its role in cellular proliferation, development and pathology.
    Electrophoresis. 1999 Feb;20(2):391-408 PMID: 10197447
  2. 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):5943-8 PMID: 7380845
  3. 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):149-52 PMID: 8612738
  4. Purification and tissue-specific expression of casein kinase from the lactating guinea-pig mammary gland.
    Eur J Biochem. 1985 Nov 4;152(3):729-37 PMID: 3863754
  5. Phosphorylation of caseins, present evidence for an amino acid triplet code posttranslationally recognized by specific kinases.
    Biochimie. 1981 Jan;63(1):1-17 PMID: 7011421
  6. Synthetic fragments of beta-casein as model substrates for liver and mammary gland casein kinases.
    Eur J Biochem. 1989 Dec 22;186(3):459-64 PMID: 2606100
  7. Clathrin assembly protein AP-3 is phosphorylated and glycosylated on the 50-kDa structural domain.
    J Biol Chem. 1994 Aug 19;269(33):21346-52 PMID: 8063760
  8. 14-3-3 and its possible role in co-ordinating multiple signalling pathways.
    Trends Cell Biol. 1996 Sep;6(9):341-7 PMID: 15157431
  9. 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):13603-10 PMID: 10570119
  10. Phosphorylation of osteopontin by Golgi apparatus casein kinase.
    Biochem Biophys Res Commun. 1997 Nov 26;240(3):602-5 PMID: 9398611
  11. Solid phase peptide synthesis utilizing 9-fluorenylmethoxycarbonyl amino acids.
    Int J Pept Protein Res. 1990 Mar;35(3):161-214 PMID: 2191922
  12. Cellular phosphorylation of an acidic proline-rich protein, PRP1, a secreted salivary phosphoprotein.
    Biochemistry. 2000 Feb 29;39(8):2023-31 PMID: 10684652
  13. 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):822-30 PMID: 8061611
  14. Casein kinase I: spatial organization and positioning of a multifunctional protein kinase family.
    Cell Signal. 1998 Nov;10(10):699-711 PMID: 9884021
  15. Protein kinase CK2 ("casein kinase-2") and its implication in cell division and proliferation.
    Prog Cell Cycle Res. 1997;3:77-97 PMID: 9552408
  16. How do protein kinases recognize their substrates?
    Biochim Biophys Acta. 1996 Dec 12;1314(3):191-225 PMID: 8982275
  17. 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):719-25 PMID: 9057837
  18. Beta-NAP, a cerebellar degeneration antigen, is a neuron-specific vesicle coat protein.
    Cell. 1995 Sep 8;82(5):773-83 PMID: 7671305
  19. 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):281-4 PMID: 3191919
  20. GRP94 (endoplasmin) co-purifies with and is phosphorylated by Golgi apparatus casein kinase.
    FEBS Lett. 2000 Apr 14;471(2-3):151-5 PMID: 10767412
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
2000-11-01
Pages
765-8
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1221417
Subset
IM
External Links
PubMed source PMC Full Text View journal details
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: product@genelibs.com

Copyright © 2026.Genelibs Jinan Honghui Biotechnology Co., Ltd. 鲁ICP备20007159号-2