The DH-PH Region of the Giant Protein UNC-89 Activates RHO-1 GTPase in Caenorhabditis elegans Body Wall Muscle
Journal of Molecular Biology, ISSN: 0022-2836, Vol: 383, Issue: 4, Page: 747-752
2008
- 34Citations
- 16Captures
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Metrics Details
- Citations34
- Citation Indexes34
- CrossRef34
- 34
- Captures16
- Readers16
- 16
Article Description
Mutation of the Caenorhabditis elegans gene unc-89 results in disorganization of muscle A-bands. unc-89 encodes a giant polypeptide (900 kDa) containing a DH domain followed by a PH domain at its N terminus, which is characteristic of guanine nucleotide exchange factor proteins for Rho GTPases. To obtain evidence that the DH-PH region has activity toward specific Rho family small GTPases, we conducted an experiment using the yeast three-hybrid system. The DH-PH region of UNC-89 has exchange activity for RHO-1 ( C. elegans RhoA), but not for CED-10 ( C. elegans Rac), MIG-2 ( C. elegans RhoG), or CDC-42 ( C. elegans Cdc42). The DH domain alone has similar activity for RHO-1. An in vitro binding assay demonstrates interaction between the DH-PH region of UNC-89 and each of the C. elegans Rho GTPases. Partial knockdown of rho-1 in C. elegans adults showed a pattern of disorganization of myosin thick filaments similar to the phenotype caused by unc-89 (su75), a mutant allele in which all of the isoforms containing the DH-PH region are missing. Taken together, we propose a model in which the DH-PH region of UNC-89 activates RHO-1 GTPase for organization of myosin filaments in C. elegans muscle cells.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S002228360801098X; http://dx.doi.org/10.1016/j.jmb.2008.08.083; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=53149141697&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/18801371; https://linkinghub.elsevier.com/retrieve/pii/S002228360801098X
Elsevier BV
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