PMID- 10089879
OWN - NLM
STAT- MEDLINE
DCOM- 19990422
LR  - 20190705
IS  - 0092-8674 (Print)
IS  - 0092-8674 (Linking)
VI  - 96
IP  - 5
DP  - 1999 Mar 5
TI  - A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly.
PG  - 635-44
AB  - Proteins modified by multiubiquitin chains are the preferred substrates of the
      proteasome. Ubiquitination involves a ubiquitin-activating enzyme, E1, a
      ubiquitin-conjugating enzyme, E2, and often a substrate-specific
      ubiquitin-protein ligase, E3. Here we show that efficient multiubiquitination
      needed for proteasomal targeting of a model substrate requires an additional
      conjugation factor, named E4. This protein, previously known as UFD2 in yeast,
      binds to the ubiquitin moieties of preformed conjugates and catalyzes ubiquitin
      chain assembly in conjunction with E1, E2, and E3. Intriguingly, E4 defines a
      novel protein family that includes two human members and the regulatory protein
      NOSA from Dictyostelium required for fruiting body development. In yeast, E4
      activity is linked to cell survival under stress conditions, indicating that
      eukaryotes utilize E4-dependent proteolysis pathways for multiple cellular
      functions.
FAU - Koegl, M
AU  - Koegl M
AD  - Zentrum fur Molekulare Biologie, Universitat Heidelberg, Germany.
FAU - Hoppe, T
AU  - Hoppe T
FAU - Schlenker, S
AU  - Schlenker S
FAU - Ulrich, H D
AU  - Ulrich HD
FAU - Mayer, T U
AU  - Mayer TU
FAU - Jentsch, S
AU  - Jentsch S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Cell
JT  - Cell
JID - 0413066
RN  - 0 (Biopolymers)
RN  - 0 (Cell Cycle Proteins)
RN  - 0 (Fungal Proteins)
RN  - 0 (Macromolecular Substances)
RN  - 0 (Multienzyme Complexes)
RN  - 0 (Proteins)
RN  - 0 (Recombinant Fusion Proteins)
RN  - 0 (Saccharomyces cerevisiae Proteins)
RN  - 0 (Ubiquitins)
RN  - EC 2.3.2.23 (Ubiquitin-Conjugating Enzymes)
RN  - EC 3.4.22.- (Cysteine Endopeptidases)
RN  - EC 3.4.25.1 (Proteasome Endopeptidase Complex)
RN  - EC 3.6.1.- (Adenosine Triphosphatases)
RN  - EC 3.6.4.- (CDC48 protein, S cerevisiae)
RN  - EC 3.6.4.6 (Valosin Containing Protein)
RN  - EC 6.3.2.- (UFD2 protein, S cerevisiae)
SB  - IM
MH  - Adenosine Triphosphatases
MH  - Biopolymers/metabolism
MH  - Cell Cycle Proteins/physiology
MH  - Cell Survival
MH  - Cell-Free System
MH  - Cloning, Molecular
MH  - Cysteine Endopeptidases
MH  - Fungal Proteins/genetics/isolation & purification/*physiology
MH  - Humans
MH  - Macromolecular Substances
MH  - Multienzyme Complexes
MH  - Multigene Family
MH  - Proteasome Endopeptidase Complex
MH  - Protein Processing, Post-Translational
MH  - Proteins/metabolism
MH  - Recombinant Fusion Proteins/physiology
MH  - Saccharomyces cerevisiae/genetics/*physiology
MH  - *Saccharomyces cerevisiae Proteins
MH  - Stress, Physiological/metabolism
MH  - Ubiquitin-Conjugating Enzymes
MH  - Ubiquitins/*metabolism
MH  - Valosin Containing Protein
EDAT- 1999/03/25 00:00
MHDA- 1999/03/25 00:01
CRDT- 1999/03/25 00:00
PHST- 1999/03/25 00:00 [pubmed]
PHST- 1999/03/25 00:01 [medline]
PHST- 1999/03/25 00:00 [entrez]
AID - S0092-8674(00)80574-7 [pii]
AID - 10.1016/s0092-8674(00)80574-7 [doi]
PST - ppublish
SO  - Cell. 1999 Mar 5;96(5):635-44. doi: 10.1016/s0092-8674(00)80574-7.