Abstract
Death-associated protein kinase (DAPK) is a multi-domain Ser/Thr protein kinase with an important role in apoptosis regulation. In these studies we have identified a DAPK-interacting protein called DIP-1, which is a novel multi-RING finger protein. The RING finger motifs of DIP-1 have E3 ligase activity that can auto-ubiquitinate DIP-1 in vitro. In vivo, DIP-1 is detected as a polyubiquitinated protein, suggesting that the intracellular levels of DIP-1 are regulated by the ubiquitin-proteasome system. Transient expression of DIP-1 in HeLa cells antagonizes the anti-apoptotic function of DAPK to promote a caspase-dependent apoptosis. These studies also demonstrate that DAPK is an in vitro and in vivo target for ubiquitination by DIP-1, thereby providing a mechanism by which DAPK activities can be regulated through proteasomal degradation.
| Original language | English |
|---|---|
| Pages (from-to) | 46980-46986 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 277 |
| Issue number | 49 |
| DOIs | |
| State | Published - Dec 6 2002 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
A death-associated protein kinase (DAPK)-interacting protein, DIP-1, is an E3 ubiquitin ligase that promotes tumor necrosis factor-induced apoptosis and regulates the cellular levels of DAPK. / Jin, Yijun; Blue, Emily K.; Dixon, Shelley; Shao, Zhili; Gallagher, Patricia.
In: Journal of Biological Chemistry, Vol. 277, No. 49, 06.12.2002, p. 46980-46986.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A death-associated protein kinase (DAPK)-interacting protein, DIP-1, is an E3 ubiquitin ligase that promotes tumor necrosis factor-induced apoptosis and regulates the cellular levels of DAPK
AU - Jin, Yijun
AU - Blue, Emily K.
AU - Dixon, Shelley
AU - Shao, Zhili
AU - Gallagher, Patricia
PY - 2002/12/6
Y1 - 2002/12/6
N2 - Death-associated protein kinase (DAPK) is a multi-domain Ser/Thr protein kinase with an important role in apoptosis regulation. In these studies we have identified a DAPK-interacting protein called DIP-1, which is a novel multi-RING finger protein. The RING finger motifs of DIP-1 have E3 ligase activity that can auto-ubiquitinate DIP-1 in vitro. In vivo, DIP-1 is detected as a polyubiquitinated protein, suggesting that the intracellular levels of DIP-1 are regulated by the ubiquitin-proteasome system. Transient expression of DIP-1 in HeLa cells antagonizes the anti-apoptotic function of DAPK to promote a caspase-dependent apoptosis. These studies also demonstrate that DAPK is an in vitro and in vivo target for ubiquitination by DIP-1, thereby providing a mechanism by which DAPK activities can be regulated through proteasomal degradation.
AB - Death-associated protein kinase (DAPK) is a multi-domain Ser/Thr protein kinase with an important role in apoptosis regulation. In these studies we have identified a DAPK-interacting protein called DIP-1, which is a novel multi-RING finger protein. The RING finger motifs of DIP-1 have E3 ligase activity that can auto-ubiquitinate DIP-1 in vitro. In vivo, DIP-1 is detected as a polyubiquitinated protein, suggesting that the intracellular levels of DIP-1 are regulated by the ubiquitin-proteasome system. Transient expression of DIP-1 in HeLa cells antagonizes the anti-apoptotic function of DAPK to promote a caspase-dependent apoptosis. These studies also demonstrate that DAPK is an in vitro and in vivo target for ubiquitination by DIP-1, thereby providing a mechanism by which DAPK activities can be regulated through proteasomal degradation.
UR - http://www.scopus.com/inward/record.url?scp=0037033026&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0037033026&partnerID=8YFLogxK
U2 - 10.1074/jbc.M208585200
DO - 10.1074/jbc.M208585200
M3 - Article
C2 - 12351649
AN - SCOPUS:0037033026
VL - 277
SP - 46980
EP - 46986
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 49
ER -