The MAP kinase‐activated protein kinase 2 contains a proline‐rich SH3‐binding domain

FEBS Letters

Gaestel, Matthias¹  Plath, Kathrin¹  Engel, Katrin¹ 

[1] Max-Delbruck-Center of Molecular Medicine, R-Rössle-Str. 10, D-13122 Berlin, Germany

关键词: Protein kinase;    MAPKAP kinase 2;    Nnuclear targeting sequence;    Heat shock protein;    Proline-rich SH3-binding domain;    cDNA;    bp;    base pair(s);    Hsp25;    small mouse heat shock protein;    Hsp27;    small human heat shock protein;    ISPK1;    insulin-stimulated protein kinase 1;    MAP;    mitogen activated protein;    MAPKAP kinase;    MAP kinase-activated protein kinase;    NTS;    nuclear targeting sequence;    sHsp;    small heat shock protein;    RACE;    rapid amplification of cDNA ends;    RSKs;    ribosomal S6 kinases;    members of this kinase family are also referred as S6 kinase I;    S6 kinase II;    ISPK1 or MAPKAP kinase 1;    SH3;    src homology 3;   

DOI  :  10.1016/0014-5793(93)81628-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The protein sequence of MAP kinase-activated protein kinase 2 (MAPKAP kinase 2) deduced from mouse cDNA sequence reveals structural features of the enzyme, which could be of importance for its function: a proline-rich SH3-binding domain N-terminal to the catalytic region, a MAP kinase phosphorylation site and a bipartite nuclear targeting sequence located C-terminal to the catalytic region. The catalytic domain itself has the strongest homology to calcium/calmodulin-dependent protein kinase II. Northern blot analysis demonstrates a 3.5 kb MAPKAP kinase 2 transcript which is ubiquitously expressed and, hence, co-expressed with the mRNA of the recently identified substrate Hsp25 in all tissues analysed. However, the functional consequences of the nuclear targeting sequence present in MAPKAP kinase 2 suggest the existence of further substrates for the enzyme in the nucleus.

【 授权许可】

Unknown