Function and structure of Drosophila glycans

被引:57
作者
Seppo, A [1 ]
Tiemeyer, M [1 ]
机构
[1] Yale Univ, Sch Med, Dept Cell Biol, New Haven, CT 06510 USA
关键词
Drosophila; glycosaminoglycan; N-linked oligosaccharide; glycosphingolipid; lectin; glycosyltransferase; heparan sulfate; HRP-epitope;
D O I
10.1093/glycob/10.8.751
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Through the application of classic organismal genetic strategies, such as mutagenesis and interaction screens, Drosophila melanogaster provides opportunities to understand glycan function. For instance, screens for Drosophila genes that establish dorsal-ventral polarity in the embryo or that influence cellular differentiation through signal modulation have identified putative glycan modifying enzymes. Other genetic and molecular approaches have demonstrated the existence of phylogenetically conserved and novel oligosaccharide processing activities and carbohydrate binding proteins, While the structural characterization of Drosophila oligosaccharide diversity has lagged behind the elucidation of glycan function, landmarks are becoming apparent in the carbohydrate terrain, For instance, O-linked GlcNAc and mucins, spatially and temporally regulated N-linked oligosaccharide expression, glycosphingolipids, heparan sulfate, chondroitin sulfate and polysialic acid have all been described. A major challenge for Drosophila glycobiology is to expand the oligosaccharide structural database while endeavoring to link glycan characterization to functional analysis. The completion of the Drosophila genome sequencing project will yield a broad portfolio of glycosyltransferases, glycan modifiying enzymes and lectins requiring characterization. To this end, the great range of genetic tools that allow the controlled spatial and temporal expression of transgenes in Drosophila will permit unprecedented manipulation of glycosylation in a whole organism.
引用
收藏
页码:751 / 760
页数:10
相关论文
共 101 条
[1]   NCAM POLYSIALIC ACID CAN REGULATE BOTH CELL CELL AND CELL SUBSTRATE INTERACTIONS [J].
ACHESON, A ;
SUNSHINE, JL ;
RUTISHAUSER, U .
JOURNAL OF CELL BIOLOGY, 1991, 114 (01) :143-153
[2]   PROCESSING OF ASPARAGINE-LINKED OLIGOSACCHARIDES IN INSECT CELLS - N-ACETYLGLUCOSAMINYLTRANSFERASE I AND II ACTIVITIES IN CULTURED LEPIDOPTERAN CELLS [J].
ALTMANN, F ;
KORNFELD, G ;
DALIK, T ;
STAUDACHER, E ;
GLOSSL, J .
GLYCOBIOLOGY, 1993, 3 (06) :619-625
[3]   Heartless, a Drosophila FGF receptor homolog, is essential for cell migration and establishment of several mesodermal lineages [J].
Beiman, M ;
Shilo, BZ ;
Volk, T .
GENES & DEVELOPMENT, 1996, 10 (23) :2993-3002
[4]   Tout-velu is a Drosophila homologue of the putative tumour suppressor EXT-1 and is needed for Hh diffusion [J].
Bellaiche, Y ;
The, I ;
Perrimon, N .
NATURE, 1998, 394 (6688) :85-88
[5]   A conserved signaling pathway: The Drosophila Toll-Dorsal pathway [J].
Belvin, MP ;
Anderson, KV .
ANNUAL REVIEW OF CELL AND DEVELOPMENTAL BIOLOGY, 1996, 12 :393-416
[6]   A new member of the frizzled family from Drosophila functions as a Wingless receptor [J].
Bhanot, P ;
Brink, M ;
Samos, CH ;
Hsieh, JC ;
Wang, YS ;
Macke, JP ;
Andrew, D ;
Nathans, J ;
Nusse, R .
NATURE, 1996, 382 (6588) :225-230
[7]  
Binari RC, 1997, DEVELOPMENT, V124, P2623
[8]   ECTOPIC EXPRESSION IN DROSOPHILA [J].
BRAND, AH ;
MANOUKIAN, AS ;
PERRIMON, N .
METHODS IN CELL BIOLOGY, VOL 44, 1994, 44 :635-654
[9]   LECTIN-BINDING SITES DURING DROSOPHILA EMBRYOGENESIS [J].
CALLAERTS, P ;
VULSTEKE, V ;
PEUMANS, W ;
DELOOF, A .
ROUXS ARCHIVES OF DEVELOPMENTAL BIOLOGY, 1995, 204 (04) :229-243
[10]   Dual roles for patched in sequestering and transducing hedgehog [J].
Chen, Y ;
Struhl, G .
CELL, 1996, 87 (03) :553-563