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FUT8 (fucosyltransferase 8 (alpha (1,6) fucosyltransferase))

Written2010-08Hideyuki Ihara, Cong-xiao Gao, Yoshitaka Ikeda, Naoyuki Taniguchi
Division of Molecular Cell Biology, Department of Biomolecular Sciences, Saga University Faculty of Medicine, Saga, Japan (HI, YI); Department of Disease Glycomics, Institute of Scientific, Industrial Research, Osaka University, Osaka, Japan (CXG, NT); Disease Glycomics Team, Systems Glycobiology Research Group, Chemical Biology Department, Japan (NT)

(Note : for Links provided by Atlas : click)

Identity

Other aliasMGC26465
LocusID (NCBI) 2530
Atlas_Id 40649
Location 14q23.3  [Link to chromosome band 14q23]
Location_base_pair Starts at and ends at bp from pter
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
ATG14 (14q22.3) / FUT8 (14q23.3)FUT8 (14q23.3) / AGBL4 (1p33)FUT8 (14q23.3) / CCDC85C (14q32.2)
FUT8 (14q23.3) / CTNNA1 (5q31.2)FUT8 (14q23.3) / FNTB (14q23.3)FUT8 (14q23.3) / IFT52 (20q13.12)
FUT8 (14q23.3) / NUMB (14q24.2)FUT8 (14q23.3) / SIPA1L1 (14q24.2)FUT8 (14q23.3) / TDRP (8p23.3)
IFRD1 (7q31.1) / FUT8 (14q23.3)

DNA/RNA

 
  Figure 1. Genomic organization of human FUT8 gene. Exons are represented by vertical bars. Exons denoted by ATG or TAA contain start and stop codons, respectively. These exons also have a part of the noncoding region.
Description Human FUT8 gene is located on chromosome 14q23.3 (Yamaguchi et al., 1999). This gene encompasses approximately 333 kb and contains nine exons with coding regions and three 5'-untranslated exons (Yamaguchi et al., 2000; Martinez-Duncker et al., 2004).
Transcription Some splicing variants of the 5'-untranslated region arise in a developmental stage-specific and tissue-specific manner (Martinez-Duncker et al., 2004). At least three different promoters appear to be functional in regulating the expression of the FUT8 gene. Three transcripts with different 5'-untranslated regions have been identified. With respect to coding region, four variants were reported to encode polypeptides containing 575, 446, 308 and 169 amino acid residues. The 575 residue protein is a fully active alpha1,6-fucosyltransferase, which was first of the variants to be identified. The other variants have not yet been examined for enzymatic activity and biological function. The 308 amino acid variant is known to be expressed in the retina (Yamaguchi et al., 2000).

Protein

 
  Figure 2. Protein structure of FUT8. CT and TM denote the cytoplasmic tail and the transmembrane domain, respectively. I, II and III represent the conserved motifs in alpha1,2-, alpha1,6- and protein O-fucosyltransferases.
Description FUT8 was purified and cloned as a cDNA from porcine brain and a human gastric cancer cell line (Uozumi et al., 1996, Yanagidani et al., 1997). Human FUT8 is comprised of 575 amino acids, with a calculated molecular weight of 66516. FUT8 contains no N-glycosylation sites. This enzyme belongs to the GT23 family of the CaZY classification. The structual analysis of a transmembrane domain-truncated form of FUT8 showed that the enzyme consists of a catalytic domain, an N-terminal coiled-coil domain and a C-terminal SH3 domain (Ihara et al., 2007). The catalytic domain was structurally classfied as a member of the GT-B group of glycosylatransferases.
Expression FUT8 gene is widely expressed in human tissues (Martinez-Duncker et al., 2004). The FUT8 gene is expressed at relatively high levels in the brain, placenta, lung, stomach, small intestine and jejunum, while pancreas, uterus, kidney and urinary bladder exhibit moderate expression. The FUT8 gene is weakly expressed in the heart, ileum, colon and spleen. On the other hand, the expression is not detectable in the normal liver (Miyoshi et al., 1997).
Localisation FUT8 is a typical type II membrane protein and is localized in the Golgi apparatus.
 
  Figure 3. The reaction catalysed by FUT8.
Function FUT8 catalyzes the transfer of a fucose residue from GDP-fucose to the reducing terminal GlcNAc of Asn-linked oligosaccharide (N-glycan) via an alpha1.6-linkage (Figure 3). The resulting fucosyl residue is often refered to as a core fucose. The reaction does not require any divalent cations or cofactors. The deletion of the FUT8 gene in mice leads to severe phenotypes that exhibit growth retardation, lung emphysema and death during postnatal development (Wang et al., 2005). As has been clearly shown in studies using knockout mice, the lack of core fucosylation resulted in the biological activities of various proteins to be perturbed (Taniguchi et al., 2006; Takahashi et al., 2009). Examples of this include the TGF-beta1 receptor (Wang et al., 2005), EGF receptor (Wang et al., 2006), VEGF receptor-2 (Wang et al., 2009), LRP-1 (Lee et al., 2006), E-cadherin (Osumi et al., 2009), alpha3beta1 integrin (Zhao et al., 2006), VCAM and alpha4beta1 integrin (Li et al., 2008). The binding affinity of the core fucose-deleted TGF-beta receptor to TGF-beta 1 is diminished in fut8-null mice, resulting in the downregulation of TGF-beta 1 signaling (Wang et al., 2005). The unusual overexpression of matrix metalloproteinases such as MMP-12 and MMP-13 is associated with the impaired receptor function, and has been proposed to cause the lung-destructive phenotypes. The EGF receptor in fut8 null mice is also affected in terms of its binding affinity to EGF and EGF-induced phoshorylation (Wang et al., 2006). These studies strongly suggest that FUT8 and core fucose structures regulate the receptor function.
In addition, core fucosylation was reported to be involved in antibodydependent cellular cytotoxicity (ADCC) (Shields et al., 2002; Shinkawa et al., 2003). The lack of core fucose of N-glycan in the Fc region of the IgG1 molecule enhances ADCC activity up to 50-100-fold. This discorvery promises to be useful in the development of antibody therapy in cancer treatment.
Homology The sequence identities between human FUT8 and other organisms are as follows :
Chimpangee (100%), Dog (97.7%), Cow (97.5%), Pig (95.6%), Rat (96.6%), Mouse (96.5%), Chicken (93.9%), Clawed frog (90.3%), Zebrafish (79.5%), Takifugu (80.2%), Tetraodon (79.8%), Sea squirt (23.2%), Fruit fly (43.7%), C. elegans (34.8%).
Eight cysteine residues in the catalytic domain are conserved among these species, except for ciona (Ihara et al., 2007).
FUT8 contains three short regions that are highly conserved in FUT8, alpha1,2-, bacterial alpha1,6-, and protein O-fucosyltransferases (Oriol et al., 1999; Takahashi et al., 2000a; Chazalet et al., 2001; Martinez-Duncker et al., 2003). The structual analysis has shown that these regions are located adjacent to one another in the Rossmann fold of FUT8 (Ihara et al., 2007). In addition, the C-terminal SH3 domain of FUT8 is structually similar to the typical SH3 domain that is found in many proteins.

Mutations

Note One frame-shit mutation and 4 substitution mutants have been identified to date in various SNPs of the FUT8 gene. The frame shift mutant is due to the insertion of a T at position 2 of the codon for Val-85, resulting in 85-VLEEQLVK-92 being change to 85-VFRRAACter-92. The four substitution mutants are K101Q, L153V, E181G and T267K. These mutants are due to A being substituted by C at position 1 of codon 101, C to G at position 1 of codon 153, A to G at position 2 of codon 181, and C to A at posision 2 of codon 267, respectively. Effects of these substitutions on enzymatic activity are not currently known.

Implicated in

Note
  
Entity Hepatocellular carcinoma (HCC)
Note It is well known that the core fucosylation of alpha-fetoprotein (AFP) is implicated in the development of HCC. AFP is a major fetal plasma protein, and its expression is elevated in hepatic diseases such as HCC, hepatitis and liver cirrhosis (Alpert et al., 1968; Ruoslahti et al., 1974). The AFP-L3 fraction was identified as the core-fucosylated isoform of AFP. The elevation in serum and liver tissue was found to be specific to HCC, but was not observed in other liver diseases (Taketa, 1990; Aoyagi, 1995; Miyoshi et al., 1999).
Thus, it appears that AFP-L3 could be used as a marker for HCC. The FUT8 gene is not expressed in the normal adult liver, but is highly expressed in HCC tissue. Surprisingly, however, such an elevation was also observed in liver cirrhosis in spite of the absence of a concomitant increase in AFP-L3 levels (Noda et al., 1998). This discrepancy can be attributed to the difference in the synthesis of GDP-fucose, a glycosyl donor substrate for fucosyltransferases, including FUT8, and by the altered intracellular sorting of fucosylated glycoproteins in hepatic cells. Because the intracellular concentration of GDP-fucose is higher in HCC, as compared to a normal liver, chronic hepatitis and liver cirrhosis, this increase would be expected to facilitate core fucosyltion of AFP (Noda et al., 2003). Core fucosylation appears to serve as a sorting signal for a glycoprotein to be directed to the bile, as revealed by the predominant distribution of fucosylated glycoproteins in bile rather than serum (Nakagawa et al., 2006). In fact, the levels of alpha-antitrypsin and alpha1-acid glycoprotein, both of which are fucosylated glycoproteins, are quite low in the bile of Fut8-null mice. The loss of polarity in cancer cells is likely to impair the regulated sorting, thus allowing abnormal secretion into the serum.
Prognosis AFP-L3-positive HCC patients were reported to show a poor prognosis (Yamashita et al., 1996).
  
  
Entity Ovarian cancer
Note FUT8 activity and mRNA levels are highly and specifically elavated in cases of ovarian serous adenocarcinoma, as compared to nomal ovary and other types of epithelial ovarian carcinoma (Takahashi et al., 2000b). In addition, core fucosylation levels in glycoproteins is also significantlly increased in cases of serous adenocarcinoma tissues.
  
  
Entity Thyroid cancer
Note The overexpression of FUT8 occurs in 33.3% of cases of papillary carcinoma of the thyroid (Ito et al., 2003), although FUT8 was not expressed in normal follicular cells. This overexpression was also shown to be correlated with tumor size and lymph node metastasis. These phenomena were not observed in cases of follicular carcinoma and anaplastic carcinoma.
  
  
Entity Pancreatic cancer
Note Haptoglobin was identified as a highly fucosylated glycoprotein in the serum of patients with pancreatic cancer (Okuyama et al., 2006). The increment of fucosylated haptoglobin was observed in pancreatic cancer rather than other diseases such as HCC, liver cirrhosis, gastric cancer and colon cancer, and also appeared to be correlated with the clinical stage. Structural analyses using lectin blotting and mass spectrometry showed that core fucosylation as well as alpha1,3/4-fucosylation is increased in haptoglobin from the serum of such patients. In addition, it was shown that interleukin 6 expressed in pancreatic cancer is a possible inducing factor for increasing the production of fucosylated haptoglobin in the liver (Narisada et al., 2008).
  
  
Entity Colorectal cancer
Note The enzymatic activity and protein expression of FUT8 were increased in tumor tissues of human colorectal carcinoma, but not in healthy tissues (Muinelo-Romay et al., 2008). This increment was well observed in cases of male, polypoid growth, no regional lymph node metastasis and early clinical stage. In addition, immunohistochemical examination has demonstrated that FUT8 is expressed at higher levels in tumor tissues of colorectal carcinoma than in healthy and transitional tissues.
  
  
Entity Cystic fibrosis
Note Fucosylation is known to be increased in cystic fibrosis. The alpha1,6-fucosylation of a membrane glycoprotein is elevated in cystic fibrosis fibroblast (Wang et al., 1990).
  

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Citation

This paper should be referenced as such :
Ihara, H ; Gao, CX ; Ikeda, Y ; Taniguchi, N
FUT8 (fucosyltransferase 8 (alpha (1,6) fucosyltransferase))
Atlas Genet Cytogenet Oncol Haematol. 2011;15(5):410-414.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/FUT8ID40649ch14q23.html


Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 5 ]
  t(1;14)(p33;q23) FUT8/AGBL4
t(14;14)(q22;q23) ATG14/FUT8
FUT8/FNTB (14q23)
t(14;14)(q23;q24) FUT8/SIPA1L1
t(14;14)(q23;q32) FUT8/CCDC85C


External links

Nomenclature
Cards
AtlasFUT8ID40649ch14q23.txt
Aliases
Genomic and cartography
Gene and transcription
RefSeq transcript (Entrez)
RefSeq genomic (Entrez)
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
BioGPS (Tissue expression)2530
Protein : pattern, domain, 3D structure
Domain families : Pfam (Sanger)
Domain families : Pfam (NCBI)
Protein Interaction databases
Ontologies - Pathways
Clinical trials, drugs, therapy
Miscellaneous
canSAR (ICR) (select the gene name)
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