E3 ubiquitin ligase RNF2 interacts with the S6′ proteasomal ATPase subunit and increases the ATP hydrolysis activity of S6′

Sun Joo Lee, Dongwon Choi, Hyangshuk Rhim, Seong Man Kang

Research output: Contribution to journalArticle

17 Citations (Scopus)

Abstract

We reported previously that the human RNF2 (RING finger protein 2) protein is an E3 ubiquitin ligase that interacts with the human ubiquitin-conjugating enzyme Hip-2/hE2-25K. In the present study, we show that RNF2 interacts with S6′ ATPase, a subunit of the proteasomal 19 S regulatory complex. S6′ interacts with RNF2 through its N-terminal RING domain, and RNF2 interacts with S6′ through its C-terminal region. Interestingly, the RNF2-S6′ interaction increases the ATP hydrolysis activity of the S6′ protein. Moreover, S6′ ATPase activity is highly increased in the presence of ubiquitinated proteins. The present study suggests that the E3 ubiquitin ligase RNF2 might have a dual function: facilitating the ubiquitination of its target substrates and recruiting the substrates to the proteasome. Furthermore, ATP hydrolysis in the E3/proteasome complex might act as an important signal for the protein degradation pathway.

Original languageEnglish
Pages (from-to)457-463
Number of pages7
JournalBiochemical Journal
Volume389
Issue number2
DOIs
Publication statusPublished - 2005 Jul 15

Fingerprint

S 6
Ubiquitin-Protein Ligases
Fingers
Adenosine Triphosphatases
Hydrolysis
Adenosine Triphosphate
Proteins
Proteasome Endopeptidase Complex
RING Finger Domains
Ubiquitinated Proteins
Ubiquitin-Conjugating Enzymes
Ubiquitination
Ubiquitin
Proteolysis
Hip
Substrates
Degradation

Keywords

  • ATP hydrolysis
  • E3 ubiquitin ligase
  • Proteasomal 19 S regulatory complex
  • RING motifs
  • RNF2
  • S6′

ASJC Scopus subject areas

  • Biochemistry

Cite this

E3 ubiquitin ligase RNF2 interacts with the S6′ proteasomal ATPase subunit and increases the ATP hydrolysis activity of S6′. / Lee, Sun Joo; Choi, Dongwon; Rhim, Hyangshuk; Kang, Seong Man.

In: Biochemical Journal, Vol. 389, No. 2, 15.07.2005, p. 457-463.

Research output: Contribution to journalArticle

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