THE DROSOPHILA YOLKLESS GENE ENCODES A VITELLOGENIN RECEPTOR BELONGING TO THE LOW-DENSITY-LIPOPROTEIN RECEPTOR SUPERFAMILY

被引:162
作者
SCHONBAUM, CP
LEE, S
MAHOWALD, AP
机构
[1] Dept. Molec. Genet. and Cell Biol., University of Chicago, Chicago, IL 60637
[2] Dept. of Molec. and Cellular Biology, Harvard University, Cambridge, MA 02138
关键词
D O I
10.1073/pnas.92.5.1485
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Sequence comparisons of vitellogenins from a wide range of organisms have identified regions of similarity not only to each other but also to vertebrate apolipoproteins (e.g. apoB-100 and apoE). Furthermore, the chicken vitellogenin receptor, which also binds apolipoproteins, has been found to belong to the low density lipoprotein receptor (LDLR) superfamily [Bujo, H., Hermann, M., Kaderli, M. O., Jacobsen, L., Sugawara, S., Nimpf, J., Yamamoto, T. and Schneider, W. J. (1994) EMBO J. 13, 5165-5175]. The yolk proteins of higher dipterans are exceptional, however, and instead show similarity to lipoprotein lipases. The molecular characterization of the putative Drosophila melanogaster vitellogenin receptor gene, yolkless (yl), described in this report reveals that the protein it encodes (Yl), is also a member of the LDLR superfamily. The ovary-specific 6.5-kb yl RNA codes for a protein of approximate to 210 kDa which contains all three motifs common to the LDLR class of proteins. Within this superfamily, YI may be related more to the LDLR-related proteins (LRPs), which bind both apolipoproteins and lipoprotein lipases. The similarity of Yl to the other LDLR proteins is restricted to the putative extracellular domain. Most noticeably, the cytoplasmic domain of Yl lacks the typical NPXY sequence which is involved in receptor internalization.
引用
收藏
页码:1485 / 1489
页数:5
相关论文
共 54 条
[1]   BASIC LOCAL ALIGNMENT SEARCH TOOL [J].
ALTSCHUL, SF ;
GISH, W ;
MILLER, W ;
MYERS, EW ;
LIPMAN, DJ .
JOURNAL OF MOLECULAR BIOLOGY, 1990, 215 (03) :403-410
[2]  
Ausubel F, 2002, SHORT PROTOCOLS MOL
[4]   THE NPXY INTERNALIZATION SIGNAL OF THE LDL RECEPTOR ADOPTS A REVERSE-TURN CONFORMATION [J].
BANSAL, A ;
GIERASCH, LM .
CELL, 1991, 67 (06) :1195-1201
[5]   THE LDL RECEPTOR RELATED PROTEIN, LRP, IS AN APOLIPOPROTEIN-E-BINDING PROTEIN [J].
BEISIEGEL, U ;
WEBER, W ;
IHRKE, G ;
HERZ, J ;
STANLEY, KK .
NATURE, 1989, 341 (6238) :162-164
[6]   CHICKEN OOCYTE GROWTH IS MEDIATED BY AN 8 LIGAND-BINDING REPEAT MEMBER OF THE LDL RECEPTOR FAMILY [J].
BUJO, H ;
HERMANN, M ;
KADERLI, MO ;
JACOBSEN, L ;
SUGAWARA, S ;
NIMPF, J ;
YAMAMOTO, T ;
SCHNEIDER, WJ .
EMBO JOURNAL, 1994, 13 (21) :5165-5175
[7]   ANALYSIS OF MOSQUITO VITELLOGENIN CDNA - SIMILARITY WITH VERTEBRATE PHOSVITINS AND ARTHROPOD SERUM-PROTEINS [J].
CHEN, JS ;
CHO, WL ;
RAIKHEL, AS .
JOURNAL OF MOLECULAR BIOLOGY, 1994, 237 (05) :641-647
[8]  
CHEN WJ, 1990, J BIOL CHEM, V265, P3116
[9]   TRANSPLANTED LDL AND MANNOSE-6-PHOSPHATE RECEPTOR INTERNALIZATION SIGNALS PROMOTE HIGH-EFFICIENCY ENDOCYTOSIS OF THE TRANSFERRIN RECEPTOR [J].
COLLAWN, JF ;
KUHN, LA ;
LIU, LFS ;
TAINER, JA ;
TROWBRIDGE, IS .
EMBO JOURNAL, 1991, 10 (11) :3247-3253
[10]   CHARACTERIZATION OF THE SOLUBILIZED MOSQUITO VITELLOGENIN RECEPTOR [J].
DHADIALLA, TS ;
HAYS, AR ;
RAIKHEL, AS .
INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY, 1992, 22 (08) :803-816