Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2010-12-2
pubmed:abstractText
Cilia are important sensory organelles, which are thought to be essential regulators of numerous signaling pathways. In Caenorhabditis elegans, defects in sensory cilium formation result in a small-body phenotype, suggesting the role of sensory cilia in body size determination. Previous analyses suggest that lack of normal cilia causes the small-body phenotype through the activation of a signaling pathway which consists of the EGL-4 cGMP-dependent protein kinase and the GCY-12 receptor-type guanylyl cyclase. By genetic suppressor screening of the small-body phenotype of a cilium defective mutant, we identified a chb-3 gene. Genetic analyses placed chb-3 in the same pathway as egl-4 and gcy-12 and upstream of egl-4. chb-3 encodes a novel protein, with a zf-MYND motif and ankyrin repeats, that is highly conserved from worm to human. In chb-3 mutants, GCY-12 guanylyl cyclase visualized by tagged GFP (GCY-12::GFP) fails to localize to sensory cilia properly and accumulates in cell bodies. Our analyses suggest that decreased GCY-12 levels in the cilia of chb-3 mutants may cause the suppression of the small-body phenotype of a cilium defective mutant. By observing the transport of GCY-12::GFP particles along the dendrites to the cilia in sensory neurons, we found that the velocities and the frequencies of the particle movement are decreased in chb-3 mutant animals. How membrane proteins are trafficked to cilia has been the focus of extensive studies in vertebrates and invertebrates, although only a few of the relevant proteins have been identified. Our study defines a new regulator, CHB-3, in the trafficking process and also shows the importance of ciliary targeting of the signaling molecule, GCY-12, in sensory-dependent body size regulation in C. elegans. Given that CHB-3 is highly conserved in mammal, a similar system may be used in the trafficking of signaling proteins to the cilia of other species.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1553-7404
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
e1001211
pubmed:dateRevised
2011-3-11
pubmed:meshHeading
pubmed-meshheading:21124861-Adaptor Proteins, Signal Transducing, pubmed-meshheading:21124861-Amino Acid Motifs, pubmed-meshheading:21124861-Animals, pubmed-meshheading:21124861-Behavior, Animal, pubmed-meshheading:21124861-Body Size, pubmed-meshheading:21124861-Caenorhabditis elegans, pubmed-meshheading:21124861-Caenorhabditis elegans Proteins, pubmed-meshheading:21124861-Cilia, pubmed-meshheading:21124861-Cyclic GMP, pubmed-meshheading:21124861-DNA Mutational Analysis, pubmed-meshheading:21124861-Dendrites, pubmed-meshheading:21124861-Genes, Helminth, pubmed-meshheading:21124861-Genes, Suppressor, pubmed-meshheading:21124861-Green Fluorescent Proteins, pubmed-meshheading:21124861-Guanylate Cyclase, pubmed-meshheading:21124861-Humans, pubmed-meshheading:21124861-Mutation, pubmed-meshheading:21124861-Phenotype, pubmed-meshheading:21124861-Protein Structure, Tertiary, pubmed-meshheading:21124861-Protein Transport, pubmed-meshheading:21124861-Recombinant Fusion Proteins, pubmed-meshheading:21124861-Sensory Receptor Cells, pubmed-meshheading:21124861-Signal Transduction, pubmed-meshheading:21124861-Zinc Fingers
pubmed:year
2010
pubmed:articleTitle
A novel zf-MYND protein, CHB-3, mediates guanylyl cyclase localization to sensory cilia and controls body size of Caenorhabditis elegans.
pubmed:affiliation
Department of Biology, Kyushu University, Hakozaki, Higashi-ku, Fukuoka, Japan. fujiwara.manabi.734@m.kyushu-u.ac.jp
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't