Phosphorylation of CREB by CaM-Kinase IV Activated by CaM-Kinase IV Kinase

H. Enslen, H. Tokumitsu, Thomas Soderling

    Research output: Contribution to journalArticle

    68 Citations (Scopus)

    Abstract

    Previous reports have shown that CaM-kinase IV can phosphorylate the transcription factor CREB in vitro on Ser133. Furthermore, transfected CaM-kinase IV can activate CREB-dependent transcription, but at a lower efficiency than the cAMP-kinase. In this paper we examine the kinetics and site-specificity of CREB phosphorylation in vitro by CaM-kinase IV after its phosphorylation and activation by a newly discovered brain CaM-kinase IV kinase. Our results show that activated CaM-kinase IV has the same Km (1-5 μM) for CREB phosphorylation, but the Vmax is about 30-fold higher than with non-activated CaM-kinase IV. Activated CaM-kinase IV still shows specificity for phosphorylation of Ser133, the site necessary for transactivation by CREB. It is likely that the lower efficiency of transcriptional activation by transfected CaM-kinase IV in previous studies was due to the fact that the CaM-kinase IV was not activated by CaM-kinase IV kinase.

    Original languageEnglish (US)
    Pages (from-to)1038-1043
    Number of pages6
    JournalBiochemical and Biophysical Research Communications
    Volume207
    Issue number3
    DOIs
    StatePublished - Feb 27 1995

    Fingerprint

    Calcium-Calmodulin-Dependent Protein Kinase Type 4
    Phosphorylation
    Phosphotransferases
    Transcriptional Activation
    Chemical activation
    Transcription
    Brain

    ASJC Scopus subject areas

    • Molecular Biology
    • Cell Biology
    • Biophysics
    • Biochemistry

    Cite this

    Phosphorylation of CREB by CaM-Kinase IV Activated by CaM-Kinase IV Kinase. / Enslen, H.; Tokumitsu, H.; Soderling, Thomas.

    In: Biochemical and Biophysical Research Communications, Vol. 207, No. 3, 27.02.1995, p. 1038-1043.

    Research output: Contribution to journalArticle

    Enslen, H. ; Tokumitsu, H. ; Soderling, Thomas. / Phosphorylation of CREB by CaM-Kinase IV Activated by CaM-Kinase IV Kinase. In: Biochemical and Biophysical Research Communications. 1995 ; Vol. 207, No. 3. pp. 1038-1043.
    @article{735892af18d441a6a82e96dfd0f3493b,
    title = "Phosphorylation of CREB by CaM-Kinase IV Activated by CaM-Kinase IV Kinase",
    abstract = "Previous reports have shown that CaM-kinase IV can phosphorylate the transcription factor CREB in vitro on Ser133. Furthermore, transfected CaM-kinase IV can activate CREB-dependent transcription, but at a lower efficiency than the cAMP-kinase. In this paper we examine the kinetics and site-specificity of CREB phosphorylation in vitro by CaM-kinase IV after its phosphorylation and activation by a newly discovered brain CaM-kinase IV kinase. Our results show that activated CaM-kinase IV has the same Km (1-5 μM) for CREB phosphorylation, but the Vmax is about 30-fold higher than with non-activated CaM-kinase IV. Activated CaM-kinase IV still shows specificity for phosphorylation of Ser133, the site necessary for transactivation by CREB. It is likely that the lower efficiency of transcriptional activation by transfected CaM-kinase IV in previous studies was due to the fact that the CaM-kinase IV was not activated by CaM-kinase IV kinase.",
    author = "H. Enslen and H. Tokumitsu and Thomas Soderling",
    year = "1995",
    month = "2",
    day = "27",
    doi = "10.1006/bbrc.1995.1289",
    language = "English (US)",
    volume = "207",
    pages = "1038--1043",
    journal = "Biochemical and Biophysical Research Communications",
    issn = "0006-291X",
    publisher = "Academic Press Inc.",
    number = "3",

    }

    TY - JOUR

    T1 - Phosphorylation of CREB by CaM-Kinase IV Activated by CaM-Kinase IV Kinase

    AU - Enslen, H.

    AU - Tokumitsu, H.

    AU - Soderling, Thomas

    PY - 1995/2/27

    Y1 - 1995/2/27

    N2 - Previous reports have shown that CaM-kinase IV can phosphorylate the transcription factor CREB in vitro on Ser133. Furthermore, transfected CaM-kinase IV can activate CREB-dependent transcription, but at a lower efficiency than the cAMP-kinase. In this paper we examine the kinetics and site-specificity of CREB phosphorylation in vitro by CaM-kinase IV after its phosphorylation and activation by a newly discovered brain CaM-kinase IV kinase. Our results show that activated CaM-kinase IV has the same Km (1-5 μM) for CREB phosphorylation, but the Vmax is about 30-fold higher than with non-activated CaM-kinase IV. Activated CaM-kinase IV still shows specificity for phosphorylation of Ser133, the site necessary for transactivation by CREB. It is likely that the lower efficiency of transcriptional activation by transfected CaM-kinase IV in previous studies was due to the fact that the CaM-kinase IV was not activated by CaM-kinase IV kinase.

    AB - Previous reports have shown that CaM-kinase IV can phosphorylate the transcription factor CREB in vitro on Ser133. Furthermore, transfected CaM-kinase IV can activate CREB-dependent transcription, but at a lower efficiency than the cAMP-kinase. In this paper we examine the kinetics and site-specificity of CREB phosphorylation in vitro by CaM-kinase IV after its phosphorylation and activation by a newly discovered brain CaM-kinase IV kinase. Our results show that activated CaM-kinase IV has the same Km (1-5 μM) for CREB phosphorylation, but the Vmax is about 30-fold higher than with non-activated CaM-kinase IV. Activated CaM-kinase IV still shows specificity for phosphorylation of Ser133, the site necessary for transactivation by CREB. It is likely that the lower efficiency of transcriptional activation by transfected CaM-kinase IV in previous studies was due to the fact that the CaM-kinase IV was not activated by CaM-kinase IV kinase.

    UR - http://www.scopus.com/inward/record.url?scp=0028925179&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=0028925179&partnerID=8YFLogxK

    U2 - 10.1006/bbrc.1995.1289

    DO - 10.1006/bbrc.1995.1289

    M3 - Article

    C2 - 7864890

    AN - SCOPUS:0028925179

    VL - 207

    SP - 1038

    EP - 1043

    JO - Biochemical and Biophysical Research Communications

    JF - Biochemical and Biophysical Research Communications

    SN - 0006-291X

    IS - 3

    ER -