Function
CLR-1, a receptor protein tyrosine phosphatase (RPTP), exhibits intrinsic protein tyrosine phosphatase (PTPase) activity. It regulates egl-15 activity, crucial for hypodermis-mediated fluid homeostasis and muscle protein degradation. During larval neuromuscular junction formation, CLR-1 negatively regulates membrane protrusion from body wall muscles. Furthermore, it plays a role in nicotinic acetylcholine receptor (nAChR)-mediated nicotine sensitivity and regulates synaptic levels of the nAChR subunit LEV-1 in the nerve cord. CLR-1 promotes the outgrowth of PVD sensory neuron quaternary dendritic branches and, in parallel with the sax-7/mnr-1 pathway, controls PVD primary branch extension. It functions within the netrin/DCC pathway, mediating synapse formation between AVA interneurons and PHB sensory neurons, and is also required for synapse formation between AVA interneurons and VA10 motor neurons.
Tissue Specificity
Expressed in muscles, hypodermis and a subset of neurons. Expressed in the AVA neurons, with high expression in the anterior half of the preanal ganglion where AVA neurons contact the PHB neurons.