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

Yijun Jin, Emily K. Blue, Shelley Dixon, Zhili Shao, Patricia Gallagher

Research output: Contribution to journalArticle

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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 languageEnglish
Pages (from-to)46980-46986
Number of pages7
JournalJournal of Biological Chemistry
Volume277
Issue number49
DOIs
StatePublished - Dec 6 2002

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Death-Associated Protein Kinases
Ubiquitin-Protein Ligases
Tumor Necrosis Factor-alpha
Apoptosis
Proteins
RING Finger Domains
Ubiquitination
Proteasome Endopeptidase Complex
Caspases
Ubiquitin
HeLa Cells
Protein Kinases
Degradation

ASJC Scopus subject areas

  • Biochemistry

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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 journalArticle

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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.

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