| Autor: |
Müller, Jan Paul, Klempnauer, Karl‐Heinz, Gray, Nicola |
| Předmět: |
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| Zdroj: |
FEBS Letters; Jun2021, Vol. 595 Issue 11, p1559-1568, 10p |
| Abstrakt: |
Homeodomain‐interacting protein kinase 2 (HIPK2) is a highly conserved, constitutively active Ser/Thr protein kinase that is involved in various important biological processes. HIPK2 activates itself by auto‐phosphorylation during its synthesis, and its activity is mainly controlled through modulation of its expression by ubiquitin‐dependent degradation. By comparing the expression of wild‐type and kinase‐defective HIPK2, we have recently described a novel mechanism of HIPK2 regulation that is based on preferential co‐translational degradation of kinase‐defective versus wild‐type HIPK2. Here, we have addressed this novel regulatory mechanism in more detail by focusing on the possible involvement of chaperones. Our work shows that HIPK2 is a client of the CDC37‐HSP90 chaperone complex and points to a novel role of CDC37 in the co‐translational degradation of a client protein. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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