{"id":{"repo_id":"rutgers","oai_identifier":"oai:example.org:rutgers-lib:45448"},"canonical_url":"https://search.dev.ndltd.org/etd/rutgers/oai:example.org:rutgers-lib:45448","repository":{"repo_id":"rutgers","name":"Rutgers University","base_url":"https://rucore.libraries.rutgers.edu/api/oai-pmh/"},"display":{"title":"Identification and characterization of components of rab-6-mediated trafficking in caenorhabditus elegans","abstract":"Membrane trafficking in neurons is an important mechanism used to regulate signaling. Controlling the abundance of AMPA-type receptors at the synapse is important for synaptic plasticity and influences processes involved in learning, memory formation, and motor control (Greger and Esteban, 2007; Shepherd and Huganir, 2007). In Caenorhabditis elegans, recycling of the AMPA receptor subunit GLR-1 has been demonstrated to be one method by which synaptic signaling mechanisms can be controlled. Rab GTPases 6.1 and 6.2 have been profiled for their role in trafficking of GLR-1 in neurons. RAB-6.2 plays a role in the retrograde trafficking of the AMPA-type glutamate receptor GLR-1 (Zhang et al., 2012). Activated Rab GTPases regulate membrane trafficking by recruiting multiple effectors, including proteins that modify phospholipid membrane composition, motor proteins that tether membranes to the cytoskeleton, and scaffolding proteins that bind to specific proteins within membranes (Stenmark, 2009). In order to understand RAB-6.2 function, we used a yeast two-hybrid approach to screen for candidate effector molecules. Herein, we discuss the screen performed and detail candidates of interest. We identified one particularly compelling candidate, a phosphoinositol-5-phosphatase named SAC-2, which we hypothesize to be involved in vesicle uncoating and/or in modifying membrane phospholipids. SAC-2::GFP is localized to punctate structures along the ventral nerve cord and in the neuron soma. SAC-2::GFP localization to puncta in the soma is enhanced in rab-6.2(ok2254) null mutant animals, which is opposite to our expectation for RAB-6.2 retrograde cargo or effector molecules. Additionally, we assessed the overlap in functions between RAB-6.1 and RAB-6.2, and delineating their pathways. In agreement with previous data from our lab, our findings suggest that the two RAB-6 isoforms perform similar trafficking functions, but do so independently of each other.","abstract_html":"Membrane trafficking in neurons is an important mechanism used to regulate signaling. Controlling the abundance of AMPA-type receptors at the synapse is important for synaptic plasticity and influences processes involved in learning, memory formation, and motor control (Greger and Esteban, 2007; Shepherd and Huganir, 2007). In Caenorhabditis elegans, recycling of the AMPA receptor subunit GLR-1 has been demonstrated to be one method by which synaptic signaling mechanisms can be controlled. Rab GTPases 6.1 and 6.2 have been profiled for their role in trafficking of GLR-1 in neurons. RAB-6.2 plays a role in the retrograde trafficking of the AMPA-type glutamate receptor GLR-1 (Zhang et al., 2012). Activated Rab GTPases regulate membrane trafficking by recruiting multiple effectors, including proteins that modify phospholipid membrane composition, motor proteins that tether membranes to the cytoskeleton, and scaffolding proteins that bind to specific proteins within membranes (Stenmark, 2009). In order to understand RAB-6.2 function, we used a yeast two-hybrid approach to screen for candidate effector molecules. Herein, we discuss the screen performed and detail candidates of interest. We identified one particularly compelling candidate, a phosphoinositol-5-phosphatase named SAC-2, which we hypothesize to be involved in vesicle uncoating and/or in modifying membrane phospholipids. SAC-2::GFP is localized to punctate structures along the ventral nerve cord and in the neuron soma. SAC-2::GFP localization to puncta in the soma is enhanced in rab-6.2(ok2254) null mutant animals, which is opposite to our expectation for RAB-6.2 retrograde cargo or effector molecules. Additionally, we assessed the overlap in functions between RAB-6.1 and RAB-6.2, and delineating their pathways. In agreement with previous data from our lab, our findings suggest that the two RAB-6 isoforms perform similar trafficking functions, but do so independently of each other.","abstract_has_math":false,"creators":[],"institution":null,"degree_name":null,"degree_level":null,"degree_discipline":null,"degree_department":null,"school":null,"contributors":["Sanner, James William, 1987- (author)","Padgett, Richard (chair)","Firestein, Bonnie (internal member)","Grant, Barth (internal member)","Rongo, Christopher (internal member)","Rutgers University","Graduate School - New Brunswick"],"advisors":[],"committee_chairs":[],"committee_members":[],"year":2014,"date_issued":"2014","date_published":"2014","updated_at":"2026-07-27T20:49:29Z","subjects":["Microbiology and Molecular Genetics","Glutamic acid--Receptors"],"languages":["eng"],"rights":["The author owns the copyright to this work."],"rights_urls":[],"identifier_entries":[{"key":"dc:identifier","label":"Identifier","values":["rutgers-lib:45448","ETD_5715"],"render_values":[{"text":"rutgers-lib:45448","href":null,"code":true},{"text":"ETD_5715","href":null,"code":true}]}]},"links":{"outbound_url":null,"outbound_label":null,"outbound_source":null},"metadata_groups":[{"id":"people","label":"People","entries":[{"key":"dc:contributor","label":"Contributor","values":["Sanner, James William, 1987- (author)","Padgett, Richard (chair)","Firestein, Bonnie (internal member)","Grant, Barth (internal member)","Rongo, Christopher (internal member)","Rutgers University","Graduate School - New Brunswick"]}]},{"id":"academic_context","label":"Academic Context","entries":[{"key":"dc:date","label":"Dc Date","values":["2014","2014-10"]},{"key":"dc:relation","label":"Dc Relation","values":["Rutgers University Electronic Theses and Dissertations","ETD","Graduate School - New Brunswick Electronic Theses and Dissertations","rucore19991600001"]},{"key":"dc:type","label":"Dc Type","values":["Text","theses"]}]},{"id":"subjects_keywords","label":"Subjects and Keywords","entries":[{"key":"dc:subject","label":"Dc Subject","values":["Microbiology and Molecular Genetics","Glutamic acid--Receptors"]}]},{"id":"language_rights","label":"Language and Rights","entries":[{"key":"dc:language","label":"Dc Language","values":["eng"]},{"key":"dc:rights","label":"Dc Rights","values":["The author owns the copyright to this work."]}]},{"id":"identifiers","label":"Identifiers","entries":[{"key":"dc:identifier","label":"Identifier","values":["rutgers-lib:45448","ETD_5715"]}]},{"id":"additional","label":"Additional Metadata","entries":[{"key":"dc:description","label":"Description","values":["Membrane trafficking in neurons is an important mechanism used to regulate signaling. Controlling the abundance of AMPA-type receptors at the synapse is important for synaptic plasticity and influences processes involved in learning, memory formation, and motor control (Greger and Esteban, 2007; Shepherd and Huganir, 2007). In Caenorhabditis elegans, recycling of the AMPA receptor subunit GLR-1 has been demonstrated to be one method by which synaptic signaling mechanisms can be controlled. Rab GTPases 6.1 and 6.2 have been profiled for their role in trafficking of GLR-1 in neurons. RAB-6.2 plays a role in the retrograde trafficking of the AMPA-type glutamate receptor GLR-1 (Zhang et al., 2012). Activated Rab GTPases regulate membrane trafficking by recruiting multiple effectors, including proteins that modify phospholipid membrane composition, motor proteins that tether membranes to the cytoskeleton, and scaffolding proteins that bind to specific proteins within membranes (Stenmark, 2009). In order to understand RAB-6.2 function, we used a yeast two-hybrid approach to screen for candidate effector molecules. Herein, we discuss the screen performed and detail candidates of interest. We identified one particularly compelling candidate, a phosphoinositol-5-phosphatase named SAC-2, which we hypothesize to be involved in vesicle uncoating and/or in modifying membrane phospholipids. SAC-2::GFP is localized to punctate structures along the ventral nerve cord and in the neuron soma. SAC-2::GFP localization to puncta in the soma is enhanced in rab-6.2(ok2254) null mutant animals, which is opposite to our expectation for RAB-6.2 retrograde cargo or effector molecules. Additionally, we assessed the overlap in functions between RAB-6.1 and RAB-6.2, and delineating their pathways. In agreement with previous data from our lab, our findings suggest that the two RAB-6 isoforms perform similar trafficking functions, but do so independently of each other.","M.S.","Includes bibliographical references","by James William Sanner"]},{"key":"dc:format","label":"Dc Format","values":["1 online resource (vii, 41 p. : ill.)","electronic resource","application/pdf"]},{"key":"dc:title","label":"Title","values":["Identification and characterization of components of rab-6-mediated trafficking in caenorhabditus elegans"]}]}],"canonical_facts":{"dc:contributor":["Sanner, James William, 1987- (author)","Padgett, Richard (chair)","Firestein, Bonnie (internal member)","Grant, Barth (internal member)","Rongo, Christopher (internal member)","Rutgers University","Graduate School - New Brunswick"],"dc:date":["2014","2014-10"],"dc:description":["Membrane trafficking in neurons is an important mechanism used to regulate signaling. Controlling the abundance of AMPA-type receptors at the synapse is important for synaptic plasticity and influences processes involved in learning, memory formation, and motor control (Greger and Esteban, 2007; Shepherd and Huganir, 2007). In Caenorhabditis elegans, recycling of the AMPA receptor subunit GLR-1 has been demonstrated to be one method by which synaptic signaling mechanisms can be controlled. Rab GTPases 6.1 and 6.2 have been profiled for their role in trafficking of GLR-1 in neurons. RAB-6.2 plays a role in the retrograde trafficking of the AMPA-type glutamate receptor GLR-1 (Zhang et al., 2012). Activated Rab GTPases regulate membrane trafficking by recruiting multiple effectors, including proteins that modify phospholipid membrane composition, motor proteins that tether membranes to the cytoskeleton, and scaffolding proteins that bind to specific proteins within membranes (Stenmark, 2009). In order to understand RAB-6.2 function, we used a yeast two-hybrid approach to screen for candidate effector molecules. Herein, we discuss the screen performed and detail candidates of interest. We identified one particularly compelling candidate, a phosphoinositol-5-phosphatase named SAC-2, which we hypothesize to be involved in vesicle uncoating and/or in modifying membrane phospholipids. SAC-2::GFP is localized to punctate structures along the ventral nerve cord and in the neuron soma. SAC-2::GFP localization to puncta in the soma is enhanced in rab-6.2(ok2254) null mutant animals, which is opposite to our expectation for RAB-6.2 retrograde cargo or effector molecules. Additionally, we assessed the overlap in functions between RAB-6.1 and RAB-6.2, and delineating their pathways. In agreement with previous data from our lab, our findings suggest that the two RAB-6 isoforms perform similar trafficking functions, but do so independently of each other.","M.S.","Includes bibliographical references","by James William Sanner"],"dc:format":["1 online resource (vii, 41 p. : ill.)","electronic resource","application/pdf"],"dc:identifier":["rutgers-lib:45448","ETD_5715"],"dc:language":["eng"],"dc:relation":["Rutgers University Electronic Theses and Dissertations","ETD","Graduate School - New Brunswick Electronic Theses and Dissertations","rucore19991600001"],"dc:rights":["The author owns the copyright to this work."],"dc:subject":["Microbiology and Molecular Genetics","Glutamic acid--Receptors"],"dc:title":["Identification and characterization of components of rab-6-mediated trafficking in caenorhabditus elegans"],"dc:type":["Text","theses"]},"updated_at":"2026-07-27T20:49:29Z"}