Abstract
A recently identified molecule C-terminus of Hsc70 interacting protein (CHIP) has been reported to be an E3 ubiquitin ligase collaborating with molecular chaperones for the degradation of misfolded or unfolded proteins. The physiological roles of CHIP in animal and plant development remain largely unknown. Here, we show that the knockdown of CeCHIP by RNAi and knockout by a deletion mutation arrests the development of the animal at the larval stage. CeCHIP expresses ubiquitously in all tissues but there are tissue specific variations of expression level. CeCHIP produces dose dependent phenotypes in vivo. Over expression of CHIP causes embryonic lethality, while a comparatively lower level of over expression causes locomotion and egg laying defects, and the CHIP over expressed animals form dauers at a higher temperature.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Animals
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Animals, Genetically Modified
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Caenorhabditis elegans / physiology*
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Caenorhabditis elegans Proteins / chemistry
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Caenorhabditis elegans Proteins / genetics*
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Caenorhabditis elegans Proteins / physiology*
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Cell Membrane / metabolism
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Crosses, Genetic
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DNA / chemistry
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Dose-Response Relationship, Drug
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Escherichia coli / metabolism
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Gene Deletion
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Models, Genetic
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Molecular Sequence Data
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Phenotype
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Protein Denaturation
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Protein Folding
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Protein Structure, Tertiary
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RNA Interference
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Recombinant Proteins / genetics
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Reverse Transcriptase Polymerase Chain Reaction
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Sequence Homology, Amino Acid
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Temperature
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Ubiquitin-Protein Ligases / genetics*
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Ubiquitin-Protein Ligases / physiology*
Substances
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Caenorhabditis elegans Proteins
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Recombinant Proteins
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DNA
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STUB1 protein, human
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Ubiquitin-Protein Ligases
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chn-1 protein, C elegans