P2X Receptor Trafficking in Neurons Is Subunit Specific
P2X receptors within the CNS mediate excitatory synaptic transmission and also act presynaptically to modulate neurotransmitter release. We have studied the targeting and trafficking of P2X4 and P2X2 receptors heterologously expressed in cultured olfactory bulb neurons. Homomeric P2X4 receptors had...
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| Veröffentlicht in: | The Journal of neuroscience 2002-06, Vol.22 (12), p.4814-4824 |
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| creator | Bobanovic, Laura K Royle, Stephen J Murrell-Lagnado, Ruth D |
| description | P2X receptors within the CNS mediate excitatory synaptic transmission and also act presynaptically to modulate neurotransmitter release. We have studied the targeting and trafficking of P2X4 and P2X2 receptors heterologously expressed in cultured olfactory bulb neurons. Homomeric P2X4 receptors had a punctate distribution, and many of the puncta colocalized with early endosomes. In contrast, P2X2 receptors were primarily localized at the plasma membrane. By antibody-labeling of surface receptors in living neurons, we showed that P2X4 receptors undergo rapid constitutive internalization and subsequent reinsertion into the plasma membrane, whereas P2X2 receptors were not regulated in such a way. The internalization of P2X4 receptors was dynamin-dependent, and the binding of ATP enhanced the basal rate of retrieval in a Ca2+-independent manner. The presence of the P2X4 subunit in a P2X4/6 heteromer governed the trafficking properties of the receptor. P2X receptors acted presynaptically to enhance the release of glutamate, suggesting that the regulated cycling of P2X4-containing receptors might provide a mechanism for modulation of synaptic transmission. |
| doi_str_mv | 10.1523/jneurosci.22-12-04814.2002 |
| format | Article |
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We have studied the targeting and trafficking of P2X4 and P2X2 receptors heterologously expressed in cultured olfactory bulb neurons. Homomeric P2X4 receptors had a punctate distribution, and many of the puncta colocalized with early endosomes. In contrast, P2X2 receptors were primarily localized at the plasma membrane. By antibody-labeling of surface receptors in living neurons, we showed that P2X4 receptors undergo rapid constitutive internalization and subsequent reinsertion into the plasma membrane, whereas P2X2 receptors were not regulated in such a way. The internalization of P2X4 receptors was dynamin-dependent, and the binding of ATP enhanced the basal rate of retrieval in a Ca2+-independent manner. The presence of the P2X4 subunit in a P2X4/6 heteromer governed the trafficking properties of the receptor. 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We have studied the targeting and trafficking of P2X4 and P2X2 receptors heterologously expressed in cultured olfactory bulb neurons. Homomeric P2X4 receptors had a punctate distribution, and many of the puncta colocalized with early endosomes. In contrast, P2X2 receptors were primarily localized at the plasma membrane. By antibody-labeling of surface receptors in living neurons, we showed that P2X4 receptors undergo rapid constitutive internalization and subsequent reinsertion into the plasma membrane, whereas P2X2 receptors were not regulated in such a way. The internalization of P2X4 receptors was dynamin-dependent, and the binding of ATP enhanced the basal rate of retrieval in a Ca2+-independent manner. The presence of the P2X4 subunit in a P2X4/6 heteromer governed the trafficking properties of the receptor. P2X receptors acted presynaptically to enhance the release of glutamate, suggesting that the regulated cycling of P2X4-containing receptors might provide a mechanism for modulation of synaptic transmission.</description><subject>Adenosine Triphosphate - pharmacology</subject><subject>Animals</subject><subject>Cell Line</subject><subject>Cell Membrane - metabolism</subject><subject>Cells, Cultured</subject><subject>Dynamins</subject><subject>Endocytosis</subject><subject>Glutamic Acid - metabolism</subject><subject>GTP Phosphohydrolases - physiology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Neurons - drug effects</subject><subject>Neurons - metabolism</subject><subject>Olfactory Bulb - cytology</subject><subject>Olfactory Bulb - metabolism</subject><subject>Protein Subunits</subject><subject>Protein Transport</subject><subject>Purinergic P2 Receptor Agonists</subject><subject>Rats</subject><subject>Rats, Wistar</subject><subject>Receptors, Presynaptic - metabolism</subject><subject>Receptors, Purinergic P2 - analysis</subject><subject>Receptors, Purinergic P2 - metabolism</subject><subject>Receptors, Purinergic P2X2</subject><subject>Receptors, Purinergic P2X4</subject><subject>Synapses - metabolism</subject><subject>Synaptic Transmission</subject><issn>0270-6474</issn><issn>1529-2401</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFP2zAUgK0JNDq2vzBFO8Ap5b0Xx044IKGqY0UIJgrSbpZrnNYsTYqdUPHv59JqsNNOPrzvfbb1MfYNYYg5ZSePje19G4wbEqVIKfAC-ZAA6AMbRKJMiQPusQGQhFRwyQ_YpxAeAUACyo_sAAmkRFkMmPxJv5Jba-yqa31y53VVOfPbNfPENcn15p4mJJOQTPtZ37guma6scRH5zPYrXQf7ZXcesvvv47vRj_Tq5mIyOr9KjYCiS21WiRkSIvFScF0QVXmZ62yGBrgWnKzWUBalMBAHEgRYwCpDU5Lh-MCzQ3a29a762dI-GNt0Xtdq5d1S-xfVaqf-nTRuoebtsxIylzIvouBoJ_DtU29Dp5YuGFvXurFtH5TEIhM54H9BLGSGUkIET7egiRGCt9Xf1yCoTSB1eT2-v72ZjiaKSCGp10BqEyguf33_n7fVXZEIHG-BhZsv1s5bFZa6riOOar1eb4UbX_YHM0Sawg</recordid><startdate>20020615</startdate><enddate>20020615</enddate><creator>Bobanovic, Laura K</creator><creator>Royle, Stephen J</creator><creator>Murrell-Lagnado, Ruth D</creator><general>Soc Neuroscience</general><general>Society for Neuroscience</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TK</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20020615</creationdate><title>P2X Receptor Trafficking in Neurons Is Subunit Specific</title><author>Bobanovic, Laura K ; Royle, Stephen J ; Murrell-Lagnado, Ruth D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c608t-e3f6b121124964a822f595a3b1c04a642eaa09896c0f597060e01f31c92c41d43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Adenosine Triphosphate - pharmacology</topic><topic>Animals</topic><topic>Cell Line</topic><topic>Cell Membrane - metabolism</topic><topic>Cells, Cultured</topic><topic>Dynamins</topic><topic>Endocytosis</topic><topic>Glutamic Acid - metabolism</topic><topic>GTP Phosphohydrolases - physiology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Neurons - drug effects</topic><topic>Neurons - metabolism</topic><topic>Olfactory Bulb - cytology</topic><topic>Olfactory Bulb - metabolism</topic><topic>Protein Subunits</topic><topic>Protein Transport</topic><topic>Purinergic P2 Receptor Agonists</topic><topic>Rats</topic><topic>Rats, Wistar</topic><topic>Receptors, Presynaptic - metabolism</topic><topic>Receptors, Purinergic P2 - analysis</topic><topic>Receptors, Purinergic P2 - metabolism</topic><topic>Receptors, Purinergic P2X2</topic><topic>Receptors, Purinergic P2X4</topic><topic>Synapses - metabolism</topic><topic>Synaptic Transmission</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bobanovic, Laura K</creatorcontrib><creatorcontrib>Royle, Stephen J</creatorcontrib><creatorcontrib>Murrell-Lagnado, Ruth D</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Neurosciences Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of neuroscience</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bobanovic, Laura K</au><au>Royle, Stephen J</au><au>Murrell-Lagnado, Ruth D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>P2X Receptor Trafficking in Neurons Is Subunit Specific</atitle><jtitle>The Journal of neuroscience</jtitle><addtitle>J Neurosci</addtitle><date>2002-06-15</date><risdate>2002</risdate><volume>22</volume><issue>12</issue><spage>4814</spage><epage>4824</epage><pages>4814-4824</pages><issn>0270-6474</issn><eissn>1529-2401</eissn><abstract>P2X receptors within the CNS mediate excitatory synaptic transmission and also act presynaptically to modulate neurotransmitter release. We have studied the targeting and trafficking of P2X4 and P2X2 receptors heterologously expressed in cultured olfactory bulb neurons. Homomeric P2X4 receptors had a punctate distribution, and many of the puncta colocalized with early endosomes. In contrast, P2X2 receptors were primarily localized at the plasma membrane. By antibody-labeling of surface receptors in living neurons, we showed that P2X4 receptors undergo rapid constitutive internalization and subsequent reinsertion into the plasma membrane, whereas P2X2 receptors were not regulated in such a way. The internalization of P2X4 receptors was dynamin-dependent, and the binding of ATP enhanced the basal rate of retrieval in a Ca2+-independent manner. The presence of the P2X4 subunit in a P2X4/6 heteromer governed the trafficking properties of the receptor. P2X receptors acted presynaptically to enhance the release of glutamate, suggesting that the regulated cycling of P2X4-containing receptors might provide a mechanism for modulation of synaptic transmission.</abstract><cop>United States</cop><pub>Soc Neuroscience</pub><pmid>12077178</pmid><doi>10.1523/jneurosci.22-12-04814.2002</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenosine Triphosphate - pharmacology Animals Cell Line Cell Membrane - metabolism Cells, Cultured Dynamins Endocytosis Glutamic Acid - metabolism GTP Phosphohydrolases - physiology Humans Kinetics Neurons - drug effects Neurons - metabolism Olfactory Bulb - cytology Olfactory Bulb - metabolism Protein Subunits Protein Transport Purinergic P2 Receptor Agonists Rats Rats, Wistar Receptors, Presynaptic - metabolism Receptors, Purinergic P2 - analysis Receptors, Purinergic P2 - metabolism Receptors, Purinergic P2X2 Receptors, Purinergic P2X4 Synapses - metabolism Synaptic Transmission |
| title | P2X Receptor Trafficking in Neurons Is Subunit Specific |
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