Document Detail


Prodomain-dependent tissue targeting of an ADAMTS protease controls cell migration in Caenorhabditis elegans.
MedLine Citation:
PMID:  17491590     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Members of the ADAMTS (a disintegrin and metalloprotease with thrombospondin motifs) family of secreted proteins play important roles in animal development and pathogenesis. However, the lack of in vivo models has hampered elucidation of the mechanisms by which these enzymes are recruited to specific target tissues and the timing of their activation during development. Using transgenic worms and primary cell cultures, here we show that MIG-17, an ADAMTS family protein required for gonadal leader cell migration in Caenorhabditis elegans, is recruited to the gonadal basement membrane in a prodomain-dependent manner. The activation of MIG-17 to control leader cell migration requires prodomain removal, which is suggested to occur autocatalytically in vitro. Although the prodomains of ADAMTS proteases have been implicated in maintaining enzymatic latency, polypeptide folding and secretion, our findings demonstrate that the prodomain has an unexpected function in tissue-specific targeting of MIG-17; this prodomain targeting function may be shared by other ADAMTSs including those in vertebrates.
Authors:
Shinji Ihara; Kiyoji Nishiwaki
Publication Detail:
Type:  Comparative Study; Journal Article     Date:  2007-05-10
Journal Detail:
Title:  The EMBO journal     Volume:  26     ISSN:  0261-4189     ISO Abbreviation:  EMBO J.     Publication Date:  2007 Jun 
Date Detail:
Created Date:  2007-06-07     Completed Date:  2008-03-06     Revised Date:  2009-11-18    
Medline Journal Info:
Nlm Unique ID:  8208664     Medline TA:  EMBO J     Country:  England    
Other Details:
Languages:  eng     Pagination:  2607-20     Citation Subset:  IM    
Affiliation:
RIKEN Center for Developmental Biology, Kobe, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Animals
Animals, Genetically Modified
Basement Membrane / metabolism*
Blotting, Western
Caenorhabditis elegans / physiology*
Caenorhabditis elegans Proteins / metabolism*
Cell Movement / physiology*
Disintegrins / metabolism*
Enzyme Activation / physiology
Gonads / metabolism*,  physiology
Metalloendopeptidases / metabolism*
Microscopy, Fluorescence
Molecular Sequence Data
Morphogenesis / genetics,  physiology*
Protein Structure, Tertiary / genetics
Chemical
Reg. No./Substance:
0/Caenorhabditis elegans Proteins; 0/Disintegrins; 0/MIG-17 protein, C elegans; EC 3.4.24.-/Metalloendopeptidases
Comments/Corrections

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