Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans

被引:156
作者
Blelloch, R
Kimble, J [1 ]
机构
[1] Univ Wisconsin, Howard Hughes Med Inst, Madison, WI 53706 USA
[2] Univ Wisconsin, Cell & Mol Biol Program, Madison, WI 53706 USA
[3] Univ Wisconsin, Dept Biochem, Madison, WI 53706 USA
[4] Univ Wisconsin, Dept Med Genet, Madison, WI 53706 USA
[5] Univ Wisconsin, Mol Biol Lab, Madison, WI 53706 USA
关键词
D O I
10.1038/21196
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
The molecular controls governing organ shape are poorly understood. In the nematode Caenorhabditis elegans, the gonad acquires a U-shape by the directed migration of a specialized 'leader' cell, which is located at the tip of the growing gonadal 'arm'(1). The gon-1 gene is essential for gonadal morphogenesis: in gon-1 mutants, no arm elongation occurs and somatic gonadal structures are severely malformed(2). Here we report that gon-1 encodes a secreted protein with a metalloprotease domain and multiple thrombospondin type-1-like repeats. This motif architecture is typical of a small family of genes that include bovine procollagen I N-protease (P1NP), which cleaves collagen(3), and murine ADAMTS-1, the expression of which correlates with tumour cell progression(4). We find that gon-1 is expressed in two sites, leader cells and muscle, and that expression in each site has a unique role in forming the gonad. We speculate that GON-1 controls morphogenesis by remodelling basement membranes and that regulation of its activity is crucial for achieving organ shape.
引用
收藏
页码:586 / 590
页数:5
相关论文
共 24 条
  • [1] Adams J. C., 1995, THROMBOSPONDIN GENE
  • [2] ANDERSON P, 1997, C ELEGANS, V2, P185
  • [3] BLELLOCH R, GON 1 GENE REGULATES
  • [4] Genome sequence of the nematode C-elegans:: A platform for investigating biology
    不详
    [J]. SCIENCE, 1998, 282 (5396) : 2012 - 2018
  • [5] Site-directed mutagenesis of the active site glutamate in human matrilysin: Investigation of its role in catalysis
    Cha, J
    Auld, DS
    [J]. BIOCHEMISTRY, 1997, 36 (50) : 16019 - 16024
  • [6] CHARACTERIZATION AND PARTIAL AMINO-ACID SEQUENCING OF A 107-KDA PROCOLLAGEN-I N-PROTEINASE PURIFIED BY AFFINITY-CHROMATOGRAPHY ON IMMOBILIZED TYPE-XIV COLLAGEN
    COLIGE, A
    BESCHIN, A
    SAMYN, B
    GOEBELS, Y
    VANBEEUMEN, J
    NUSGENS, BV
    LAPIERE, CM
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 1995, 270 (28) : 16724 - 16730
  • [7] cDNA cloning and expression of bovine procollagen I N-proteinase: A new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components
    Colige, A
    Li, SW
    Sieron, AL
    Nusgens, BV
    Prockop, DJ
    Lapiere, CM
    [J]. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1997, 94 (06) : 2374 - 2379
  • [8] Potent and specific genetic interference by double-stranded RNA in Caenorhabditis elegans
    Fire, A
    Xu, SQ
    Montgomery, MK
    Kostas, SA
    Driver, SE
    Mello, CC
    [J]. NATURE, 1998, 391 (6669) : 806 - 811
  • [9] HENDERSON ST, 1994, DEVELOPMENT, V120, P2913
  • [10] Matrix metalloproteinases regulate neovascularization by acting as pericellular fibrinolysins
    Hiraoka, N
    Allen, E
    Apel, IJ
    Gyetko, MR
    Weiss, SJ
    [J]. CELL, 1998, 95 (03) : 365 - 377