A structural basis for substrate specificities of protein Ser/Thr kinases: Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1

Z. Songyang, Kun Ping Lu, Young T. Kwon, Li Huei Tsai, Odile Filhol, Claude Cochet, Debra A. Brickey, Thomas Soderling, Cheryl Bartleson, Donald J. Graves, Anthony J. Demaggio, Merl F. Hoekstra, John Blenis, Tony Hunter, Lewis C. Cantley

    Research output: Contribution to journalArticle

    454 Citations (Scopus)

    Abstract

    We have developed a method to study the primary sequence specificities of protein kinases by using an oriented degenerate peptide library. We report here the substrate specificities of eight protein Ser/Thr kinases. All of the kinases studied selected distinct optimal substrates. The identified substrate specificities of these kinases, together with known crystal structures of protein kinase A, CDK2, Erk2, twitchin, and casein kinase I, provide a structural basis for the substrate recognition of protein Ser/Thr kinases. In particular, the specific selection of amino acids at the +1 and - 3 positions to the substrate serine/threonine can be rationalized on the basis of sequences of protein kinases. The identification of optimal peptide substrates of CDK5, casein kinases I and II, NIMA, calmodulin-dependent kinases, Erk1, and phosphorylase kinase makes it possible to predict the potential in vivo targets of these kinases.

    Original languageEnglish (US)
    Pages (from-to)6486-6493
    Number of pages8
    JournalMolecular and Cellular Biology
    Volume16
    Issue number11
    StatePublished - 1996

    Fingerprint

    Casein Kinase I
    Phosphorylase Kinase
    Casein Kinase II
    Calcium-Calmodulin-Dependent Protein Kinases
    Substrate Specificity
    Phosphotransferases
    Proteins
    Protein Kinases
    Peptide Library
    Threonine
    Cyclic AMP-Dependent Protein Kinases
    Serine
    Amino Acids
    Peptides

    ASJC Scopus subject areas

    • Molecular Biology
    • Genetics
    • Cell Biology

    Cite this

    A structural basis for substrate specificities of protein Ser/Thr kinases : Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1. / Songyang, Z.; Lu, Kun Ping; Kwon, Young T.; Tsai, Li Huei; Filhol, Odile; Cochet, Claude; Brickey, Debra A.; Soderling, Thomas; Bartleson, Cheryl; Graves, Donald J.; Demaggio, Anthony J.; Hoekstra, Merl F.; Blenis, John; Hunter, Tony; Cantley, Lewis C.

    In: Molecular and Cellular Biology, Vol. 16, No. 11, 1996, p. 6486-6493.

    Research output: Contribution to journalArticle

    Songyang, Z, Lu, KP, Kwon, YT, Tsai, LH, Filhol, O, Cochet, C, Brickey, DA, Soderling, T, Bartleson, C, Graves, DJ, Demaggio, AJ, Hoekstra, MF, Blenis, J, Hunter, T & Cantley, LC 1996, 'A structural basis for substrate specificities of protein Ser/Thr kinases: Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1', Molecular and Cellular Biology, vol. 16, no. 11, pp. 6486-6493.
    Songyang, Z. ; Lu, Kun Ping ; Kwon, Young T. ; Tsai, Li Huei ; Filhol, Odile ; Cochet, Claude ; Brickey, Debra A. ; Soderling, Thomas ; Bartleson, Cheryl ; Graves, Donald J. ; Demaggio, Anthony J. ; Hoekstra, Merl F. ; Blenis, John ; Hunter, Tony ; Cantley, Lewis C. / A structural basis for substrate specificities of protein Ser/Thr kinases : Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1. In: Molecular and Cellular Biology. 1996 ; Vol. 16, No. 11. pp. 6486-6493.
    @article{3423e3f8c9bc40199572f3c98f3a3d6a,
    title = "A structural basis for substrate specificities of protein Ser/Thr kinases: Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1",
    abstract = "We have developed a method to study the primary sequence specificities of protein kinases by using an oriented degenerate peptide library. We report here the substrate specificities of eight protein Ser/Thr kinases. All of the kinases studied selected distinct optimal substrates. The identified substrate specificities of these kinases, together with known crystal structures of protein kinase A, CDK2, Erk2, twitchin, and casein kinase I, provide a structural basis for the substrate recognition of protein Ser/Thr kinases. In particular, the specific selection of amino acids at the +1 and - 3 positions to the substrate serine/threonine can be rationalized on the basis of sequences of protein kinases. The identification of optimal peptide substrates of CDK5, casein kinases I and II, NIMA, calmodulin-dependent kinases, Erk1, and phosphorylase kinase makes it possible to predict the potential in vivo targets of these kinases.",
    author = "Z. Songyang and Lu, {Kun Ping} and Kwon, {Young T.} and Tsai, {Li Huei} and Odile Filhol and Claude Cochet and Brickey, {Debra A.} and Thomas Soderling and Cheryl Bartleson and Graves, {Donald J.} and Demaggio, {Anthony J.} and Hoekstra, {Merl F.} and John Blenis and Tony Hunter and Cantley, {Lewis C.}",
    year = "1996",
    language = "English (US)",
    volume = "16",
    pages = "6486--6493",
    journal = "Molecular and Cellular Biology",
    issn = "0270-7306",
    publisher = "American Society for Microbiology",
    number = "11",

    }

    TY - JOUR

    T1 - A structural basis for substrate specificities of protein Ser/Thr kinases

    T2 - Primary sequence preference of casein kinases I and II, NIMA, phosphorylase kinase, calmodulin-dependent kinase II, CDK5, and Erk1

    AU - Songyang, Z.

    AU - Lu, Kun Ping

    AU - Kwon, Young T.

    AU - Tsai, Li Huei

    AU - Filhol, Odile

    AU - Cochet, Claude

    AU - Brickey, Debra A.

    AU - Soderling, Thomas

    AU - Bartleson, Cheryl

    AU - Graves, Donald J.

    AU - Demaggio, Anthony J.

    AU - Hoekstra, Merl F.

    AU - Blenis, John

    AU - Hunter, Tony

    AU - Cantley, Lewis C.

    PY - 1996

    Y1 - 1996

    N2 - We have developed a method to study the primary sequence specificities of protein kinases by using an oriented degenerate peptide library. We report here the substrate specificities of eight protein Ser/Thr kinases. All of the kinases studied selected distinct optimal substrates. The identified substrate specificities of these kinases, together with known crystal structures of protein kinase A, CDK2, Erk2, twitchin, and casein kinase I, provide a structural basis for the substrate recognition of protein Ser/Thr kinases. In particular, the specific selection of amino acids at the +1 and - 3 positions to the substrate serine/threonine can be rationalized on the basis of sequences of protein kinases. The identification of optimal peptide substrates of CDK5, casein kinases I and II, NIMA, calmodulin-dependent kinases, Erk1, and phosphorylase kinase makes it possible to predict the potential in vivo targets of these kinases.

    AB - We have developed a method to study the primary sequence specificities of protein kinases by using an oriented degenerate peptide library. We report here the substrate specificities of eight protein Ser/Thr kinases. All of the kinases studied selected distinct optimal substrates. The identified substrate specificities of these kinases, together with known crystal structures of protein kinase A, CDK2, Erk2, twitchin, and casein kinase I, provide a structural basis for the substrate recognition of protein Ser/Thr kinases. In particular, the specific selection of amino acids at the +1 and - 3 positions to the substrate serine/threonine can be rationalized on the basis of sequences of protein kinases. The identification of optimal peptide substrates of CDK5, casein kinases I and II, NIMA, calmodulin-dependent kinases, Erk1, and phosphorylase kinase makes it possible to predict the potential in vivo targets of these kinases.

    UR - http://www.scopus.com/inward/record.url?scp=0343177223&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=0343177223&partnerID=8YFLogxK

    M3 - Article

    C2 - 8887677

    AN - SCOPUS:0343177223

    VL - 16

    SP - 6486

    EP - 6493

    JO - Molecular and Cellular Biology

    JF - Molecular and Cellular Biology

    SN - 0270-7306

    IS - 11

    ER -