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Symbol report for FBXW7

HGNC data for FBXW7

Approved symbol
FBXW7
Approved name

F-box and WD repeat domain containing 7

Locus type
gene with protein product
HGNC ID
HGNC:16712
Symbol status
Approved
Previous names
F-box and WD-40 domain protein 7 (archipelago homolog, Drosophila)
F-box and WD repeat domain containing 7, E3 ubiquitin protein ligase
Alias symbols
AGO
FLJ11071
SEL-10
SEL10
FBW7
FBX30
CDC4
FBXW6
Alias names
archipelago homolog (Drosophila)
Chromosomal location
4q31.3
Bos taurus
FBXW7 VGNC:28926 VGNC
Canis familiaris
FBXW7 VGNC:40797 VGNC
Equus caballus
FBXW7 VGNC:17968 VGNC
Felis catus
FBXW7 VGNC:62204 VGNC
Macaca mulatta
FBXW7 VGNC:72516 VGNC
Mus musculus
Fbxw7 MGI:1354695 Curated
Pan troglodytes
FBXW7 VGNC:2989 VGNC
Rattus norvegicus
Fbxw7 RGD:2321145
Sus scrofa
FBXW7 VGNC:98925 VGNC
Functional interaction between SEL-10, an F-box protein, and the nuclear form of activated Notch1 receptor.
Gupta-Rossi N et al. J Biol Chem 2001 Sep;276(37)34371-34378
Gupta-Rossi N, Le Bail O, Gonen H, Brou C, Logeat F, Six E, Ciechanover A, Israël A.
J Biol Chem 2001 Sep;276(37)34371-34378
Abstract: The Notch signaling pathway is essential in many cell fate decisions in invertebrates as well as in vertebrates. After ligand binding, a two-step proteolytic cleavage releases the intracellular part of the receptor which translocates to the nucleus and acts as a transcriptional activator. Although Notch-induced transcription of genes has been reported extensively, its endogenous nuclear form has been seldom visualized. We report that the nuclear intracellular domain of Notch1 is stabilized by proteasome inhibitors and is a substrate for polyubiquitination in vitro. SEL-10, an F-box protein of the Cdc4 family, was isolated in a genetic screen for Lin12/Notch-negative regulators in Caenorhabditis elegans. We isolated human and murine counterparts of SEL-10 and investigated the role of a dominant-negative form of this protein, deleted of the F-box, on Notch1 stability and activity. This molecule could stabilize intracellular Notch1 and enhance its transcriptional activity but had no effect on inactive membrane-anchored forms of the receptor. We then demonstrated that SEL-10 specifically interacts with nuclear forms of Notch1 and that this interaction requires a phosphorylation event. Taken together, these data suggest that SEL-10 is involved in shutting off Notch signaling by ubiquitin-proteasome-mediated degradation of the active transcriptional factor after a nuclear phosphorylation event.
A family of mammalian F-box proteins.
Winston JT et al. Curr Biol 1999 Oct;9(20)1180-1182
Winston JT, Koepp DM, Zhu C, Elledge SJ, Harper JW.
Curr Biol 1999 Oct;9(20)1180-1182
Abstract: 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.