PMID- 10531037
OWN - NLM
STAT- MEDLINE
DCOM- 19991206
LR  - 20161124
IS  - 0960-9822 (Print)
IS  - 0960-9822 (Linking)
VI  - 9
IP  - 20
DP  - 1999 Oct 21
TI  - A family of mammalian F-box proteins.
PG  - 1180-2
AB  - Ubiquitin-mediated destruction of regulatory proteins is a frequent means of
      controlling progression through signaling pathways [1]. F-box proteins [2] are
      components of modular E3 ubiquitin protein ligases called SCFs, which function in
      phosphorylation-dependent ubiquitination ([3] [4] [5], reviewed in [6] [7]).
      F-box proteins contain a carboxy-terminal domain that interacts with substrates
      and a 42-48 amino-acid F-box motif which binds to the protein Skp1 [2] [3] [4].
      Skp1 binding links the F-box protein with a core ubiquitin ligase composed of the
      proteins Cdc53/Cul1, Rbx1 (also called Hrt1 and Roc1) and the E2
      ubiquitin-conjugating enzyme Cdc34 [8] [9] [10] [11]. The genomes of the budding 
      yeast Saccharomyces cerevisiae and the nematode worm Caenorhabditis elegans
      contain, respectively, 16 and more than 60 F-box proteins [2] [7]; in S.
      cerevisiae, the F-box proteins Cdc4, Grr1 and Met30 target cyclin-dependent
      kinase inhibitors, G1 cyclins and transcriptional regulators for ubiquitination
      ([3] [4] [5] [8] [10], reviewed in [6] [7]). Only four mammalian F-box proteins
      (Cyclin F, Skp1, beta-TRCP and NFB42) have been identified so far [2] [12]. Here,
      we report the identification of a family of 33 novel mammalian F-box proteins.
      The large number of these proteins in mammals suggests that the SCF system
      controls a correspondingly large number of regulatory pathways in vertebrates.
      Four of these proteins contain a novel conserved motif, the F-box-associated
      (FBA) domain, which may represent a new protein-protein interaction motif. The
      identification of these genes will help uncover pathways controlled by
      ubiquitin-mediated proteolysis in mammals.
FAU - Winston, J T
AU  - Winston JT
AD  - Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor
      College of Medicine, One Baylor Plaza, Houston, Texas, 77030, USA.
FAU - Koepp, D M
AU  - Koepp DM
FAU - Zhu, C
AU  - Zhu C
FAU - Elledge, S J
AU  - Elledge SJ
FAU - Harper, J W
AU  - Harper JW
LA  - eng
SI  - GENBANK/AF176520
SI  - GENBANK/AF176521
SI  - GENBANK/AF176522
SI  - GENBANK/AF176706
GR  - AG-11085/AG/NIA NIH HHS/United States
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Research Support, U.S. Gov't, Non-P.H.S.
PT  - Research Support, U.S. Gov't, P.H.S.
PL  - England
TA  - Curr Biol
JT  - Current biology : CB
JID - 9107782
RN  - 0 (Proteins)
RN  - 0 (Ubiquitins)
RN  - EC 2.3.2.27 (SKP Cullin F-Box Protein Ligases)
RN  - EC 6.3.2.- (Peptide Synthases)
SB  - IM
SB  - S
MH  - Amino Acid Sequence
MH  - Animals
MH  - Conserved Sequence
MH  - Humans
MH  - Mice
MH  - Molecular Sequence Data
MH  - Peptide Synthases/metabolism
MH  - Phylogeny
MH  - Proteins/*chemistry/*classification/genetics
MH  - SKP Cullin F-Box Protein Ligases
MH  - Sequence Homology, Amino Acid
MH  - Two-Hybrid System Techniques
MH  - Ubiquitins/metabolism
EDAT- 1999/10/26 00:00
MHDA- 1999/10/26 00:01
CRDT- 1999/10/26 00:00
PHST- 1999/10/26 00:00 [pubmed]
PHST- 1999/10/26 00:01 [medline]
PHST- 1999/10/26 00:00 [entrez]
AID - S0960-9822(00)80021-4 [pii]
AID - 10.1016/S0960-9822(00)80021-4 [doi]
PST - ppublish
SO  - Curr Biol. 1999 Oct 21;9(20):1180-2. doi: 10.1016/S0960-9822(00)80021-4.