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RPM-1 suppressors Act in synapse formation and axon termination in Caenorhabditis elegans

Abstract

One prevailing question in developmental neurobiology is how neurons form precise connections with their targets. The PHR (Pam/Highwire/RPM-1) protein family is highly conserved from mammals to zebrafish and is important for both axon termination and synapse formation. Caenorhabditis elegans RPM-1 (Regulator of Presynaptic Morphology) is a large protein with multiple domains. One role of RPM-1 is to negatively regulate a mitogen- activated protein kinase (MAPK) cascade via proteasomal degradation. To learn more about the RPM-1 signaling pathway, a genetic suppressor screen was utilized to identify additional molecules downstream of RPM-1. Suppressors were initially tested by non-complementation against known rpm-1 suppressors to identify novel suppressors. One prevailing question in developmental neurobiology is how neurons form precise connections with their targets. The PHR (Pam/Highwire/RPM-1) protein family is highly conserved from mammals to zebrafish and is important for both axon termination and synapse formation. Caenorhabditis elegans RPM-1 (Regulator of Presynaptic Morphology) is a large protein with multiple domains. One role of RPM-1 is to negatively regulate a mitogen- activated protein kinase (MAPK) cascade via proteasomal degradation. To learn more about the RPM-1 signaling pathway, a genetic suppressor screen was utilized to identify additional molecules downstream of RPM-1. Suppressors were initially tested by non-complementation against known rpm-1 suppressors to identify novel suppressors. One prevailing question in developmental neurobiology is how neurons form precise connections with their targets. The PHR (Pam/Highwire/RPM-1) protein family is highly conserved from mammals to zebrafish and is important for both axon termination and synapse formation. Caenorhabditis elegans RPM-1 (Regulator of Presynaptic Morphology) is a large protein with multiple domains. One role of RPM-1 is to negatively regulate a mitogen- activated protein kinase (MAPK) cascade via proteasomal degradation. To learn more about the RPM-1 signaling pathway, a genetic suppressor screen was utilized to identify additional molecules downstream of RPM-1. Suppressors were initially tested by non-complementation against known rpm-1 suppressors to identify novel suppressors. My dissertation provides characterization of a novel protein involved in synaptogenesis and the addition of mapping information for additional proteins important in synapse formation downstream of RPM-1

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