cDNA Cloning and Expression Analysis of New Members of the Mammalian F-Box Protein Family

F-box proteins are critical components of the SCF ubiquitin–protein ligase complex and are involved in substrate recognition and recruitment for ubiquitination and consequent degradation by the proteasome. We have isolated cDNAs encoding a further 10 mammalian F-box proteins. Five of them (FBL3 to F...

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Bibliographic Details
Published in:Genomics (San Diego, Calif.) Calif.), 2000-07, Vol.67 (1), p.40-47
Main Authors: Ilyin, Gennady P., Rialland, Mickael, Pigeon, Christelle, Guguen-Guillouzo, Christiane
Format: Article
Language:English
Subjects:
Amino Acid Motifs
Amino Acid Sequence
Animals
Biological and medical sciences
Caenorhabditis elegans
Cloning, Molecular
Databases, Factual
Fundamental and applied biological sciences. Psychology
Genes. Genome
Humans
Leucine Zippers
Molecular and cellular biology
Molecular genetics
Molecular Sequence Data
Multigene Family - genetics
Multigene Family - physiology
Peptide Synthases - classification
Peptide Synthases - genetics
Peptide Synthases - metabolism
Proteins - chemistry
Proteins - classification
Proteins - genetics
Rats
Reverse Transcriptase Polymerase Chain Reaction
Sequence Homology, Amino Acid
Tissue Distribution
Ubiquitins - metabolism
Yeasts
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Summary:F-box proteins are critical components of the SCF ubiquitin–protein ligase complex and are involved in substrate recognition and recruitment for ubiquitination and consequent degradation by the proteasome. We have isolated cDNAs encoding a further 10 mammalian F-box proteins. Five of them (FBL3 to FBL7) share structural similarities with Skp2 and contain C-terminal leucine-rich repeats. The other 5 proteins have different putative protein–protein interaction motifs. Specifically, FBS and FBWD4 proteins contain Sec7 and WD40-repeat domains, respectively. The C-terminal region of FBA shares similarity with bacterial protein ApaG while FBG2 shows homology with the F-box protein NFB42. The marked differences in F-box gene expression in human tissues suggest their distinct role in ubiquitin-dependent protein degradation.
ISSN:0888-7543
1089-8646
DOI:10.1006/geno.2000.6211