Ubiquitin C-Terminal Hydrolase Is an Immediate-Early Gene Essential for Long-Term Facilitation in Aplysia
The switch from short-term to long-term facilitation of the synapses between sensory and motor neurons mediating gill and tail withdrawal reflexes in Aplysia requires CREB-mediated transcription and new protein synthesis. We isolated several downstream genes, one of which encodes a neuron-specific u...
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| Veröffentlicht in: | Cell 1997-04, Vol.89 (1), p.115-126 |
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| container_title | Cell |
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| creator | Hegde, Ashok N. Inokuchi, Kaoru Pei, Wanzheng Casadio, Andrea Ghirardi, Mirella Chain, Daniel G. Martin, Kelsey C. Kandel, Eric R. Schwartz, James H. |
| description | The switch from short-term to long-term facilitation of the synapses between sensory and motor neurons mediating gill and tail withdrawal reflexes in Aplysia requires CREB-mediated transcription and new protein synthesis. We isolated several downstream genes, one of which encodes a neuron-specific ubiquitin C-terminal hydrolase. This rapidly induced gene encodes an enzyme that associates with the proteasome and increases its proteolytic activity. This regulated proteolysis is essential for long-term facilitation. Inhibiting the expression or function of the hydrolase blocks induction of long-term but not short-term facilitation. We suggest that the enhanced proteasome activity increases degradation of substrates that normally inhibit long-term facilitation. Thus, through induction of the hydrolase and the resulting up-regulation of the ubiquitin pathway, learning recruits a regulated form of proteolysis that removes inhibitory constraints on long-term memory storage. |
| doi_str_mv | 10.1016/S0092-8674(00)80188-9 |
| format | Article |
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We isolated several downstream genes, one of which encodes a neuron-specific ubiquitin C-terminal hydrolase. This rapidly induced gene encodes an enzyme that associates with the proteasome and increases its proteolytic activity. This regulated proteolysis is essential for long-term facilitation. Inhibiting the expression or function of the hydrolase blocks induction of long-term but not short-term facilitation. We suggest that the enhanced proteasome activity increases degradation of substrates that normally inhibit long-term facilitation. 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Thus, through induction of the hydrolase and the resulting up-regulation of the ubiquitin pathway, learning recruits a regulated form of proteolysis that removes inhibitory constraints on long-term memory storage.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies - pharmacology</subject><subject>Aplysia</subject><subject>Aplysia - physiology</subject><subject>Base Sequence</subject><subject>Blotting, Northern</subject><subject>Cells, Cultured - drug effects</subject><subject>Cells, Cultured - enzymology</subject><subject>Cyclic AMP - pharmacology</subject><subject>Cyclic AMP-Dependent Protein Kinases - metabolism</subject><subject>Ganglia, Invertebrate - cytology</subject><subject>Genes, Immediate-Early - physiology</subject><subject>Long-Term Potentiation - genetics</subject><subject>Marine</subject><subject>Memory - physiology</subject><subject>Microinjections</subject><subject>Molecular Sequence Data</subject><subject>Nerve Tissue Proteins - genetics</subject><subject>Nerve Tissue Proteins - immunology</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurons, Afferent - drug effects</subject><subject>Neurons, Afferent - enzymology</subject><subject>Oligonucleotides, Antisense - pharmacology</subject><subject>Proteins - metabolism</subject><subject>RNA, Messenger - analysis</subject><subject>Serotonin - pharmacology</subject><subject>Substrate Specificity</subject><subject>Thiolester Hydrolases - genetics</subject><subject>Thiolester Hydrolases - immunology</subject><subject>Thiolester Hydrolases - metabolism</subject><subject>Ubiquitin Thiolesterase</subject><subject>Ubiquitins - metabolism</subject><issn>0092-8674</issn><issn>1097-4172</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFr3DAQhUVpSDdpf0JAp9Ic3IxsS7ZOJSybZGGhhyZnMZLHQcGWN5K3sP8-yu6Sa05zmO-9B-8xdiXgtwChbv4B6LJoVVP_ArhuQbRtob-whQDdFLVoyq9s8YF8YxcpvQBAK6U8Z-cadN2UsGD-yfrXnZ994MvikeLoAw78Yd_FacBEfJ04Br4eR-o8zlSsMA57fk-B-ColCrPPeD9FvpnC88GA36Hzg59x9lPg2fd2O-yTx-_srMch0Y_TvWRPd6vH5UOx-Xu_Xt5uCielmguLpFH0tmwr0cvGOQUlKFdb6VwlS6vKFnpL5FSFDpV1uu5QIgkpqOp6W12yn0ffbZxed5RmM_rkaBgw0LRLpml11ehGfQqKnCwAZAblEXRxSilSb7bRjxj3RoB538IctjDvRRsAc9jC6Ky7OgXsbO7vQ3UqP___HP-U6_jvKZrkPAWXq47kZtNN_pOEN4uWmhU</recordid><startdate>19970404</startdate><enddate>19970404</enddate><creator>Hegde, Ashok N.</creator><creator>Inokuchi, Kaoru</creator><creator>Pei, Wanzheng</creator><creator>Casadio, Andrea</creator><creator>Ghirardi, Mirella</creator><creator>Chain, Daniel G.</creator><creator>Martin, Kelsey C.</creator><creator>Kandel, Eric R.</creator><creator>Schwartz, James H.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><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>7TM</scope><scope>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>L.G</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19970404</creationdate><title>Ubiquitin C-Terminal Hydrolase Is an Immediate-Early Gene Essential for Long-Term Facilitation in Aplysia</title><author>Hegde, Ashok N. ; Inokuchi, Kaoru ; Pei, Wanzheng ; Casadio, Andrea ; Ghirardi, Mirella ; Chain, Daniel G. ; Martin, Kelsey C. ; Kandel, Eric R. ; Schwartz, James H.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c556t-bae9a1fb2831f57cc60206c4b5cc352b6280fbeec63aca6bc94da5ae151e3dfb3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies - pharmacology</topic><topic>Aplysia</topic><topic>Aplysia - physiology</topic><topic>Base Sequence</topic><topic>Blotting, Northern</topic><topic>Cells, Cultured - drug effects</topic><topic>Cells, Cultured - enzymology</topic><topic>Cyclic AMP - pharmacology</topic><topic>Cyclic AMP-Dependent Protein Kinases - metabolism</topic><topic>Ganglia, Invertebrate - cytology</topic><topic>Genes, Immediate-Early - physiology</topic><topic>Long-Term Potentiation - genetics</topic><topic>Marine</topic><topic>Memory - physiology</topic><topic>Microinjections</topic><topic>Molecular Sequence Data</topic><topic>Nerve Tissue Proteins - genetics</topic><topic>Nerve Tissue Proteins - immunology</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurons, Afferent - drug effects</topic><topic>Neurons, Afferent - enzymology</topic><topic>Oligonucleotides, Antisense - pharmacology</topic><topic>Proteins - metabolism</topic><topic>RNA, Messenger - analysis</topic><topic>Serotonin - pharmacology</topic><topic>Substrate Specificity</topic><topic>Thiolester Hydrolases - genetics</topic><topic>Thiolester Hydrolases - immunology</topic><topic>Thiolester Hydrolases - metabolism</topic><topic>Ubiquitin Thiolesterase</topic><topic>Ubiquitins - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hegde, Ashok N.</creatorcontrib><creatorcontrib>Inokuchi, Kaoru</creatorcontrib><creatorcontrib>Pei, Wanzheng</creatorcontrib><creatorcontrib>Casadio, Andrea</creatorcontrib><creatorcontrib>Ghirardi, Mirella</creatorcontrib><creatorcontrib>Chain, Daniel G.</creatorcontrib><creatorcontrib>Martin, Kelsey C.</creatorcontrib><creatorcontrib>Kandel, Eric R.</creatorcontrib><creatorcontrib>Schwartz, James H.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Nucleic Acids Abstracts</collection><collection>Technology Research Database</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Engineering Research Database</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hegde, Ashok N.</au><au>Inokuchi, Kaoru</au><au>Pei, Wanzheng</au><au>Casadio, Andrea</au><au>Ghirardi, Mirella</au><au>Chain, Daniel G.</au><au>Martin, Kelsey C.</au><au>Kandel, Eric R.</au><au>Schwartz, James H.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ubiquitin C-Terminal Hydrolase Is an Immediate-Early Gene Essential for Long-Term Facilitation in Aplysia</atitle><jtitle>Cell</jtitle><addtitle>Cell</addtitle><date>1997-04-04</date><risdate>1997</risdate><volume>89</volume><issue>1</issue><spage>115</spage><epage>126</epage><pages>115-126</pages><issn>0092-8674</issn><eissn>1097-4172</eissn><abstract>The switch from short-term to long-term facilitation of the synapses between sensory and motor neurons mediating gill and tail withdrawal reflexes in Aplysia requires CREB-mediated transcription and new protein synthesis. We isolated several downstream genes, one of which encodes a neuron-specific ubiquitin C-terminal hydrolase. This rapidly induced gene encodes an enzyme that associates with the proteasome and increases its proteolytic activity. This regulated proteolysis is essential for long-term facilitation. Inhibiting the expression or function of the hydrolase blocks induction of long-term but not short-term facilitation. We suggest that the enhanced proteasome activity increases degradation of substrates that normally inhibit long-term facilitation. Thus, through induction of the hydrolase and the resulting up-regulation of the ubiquitin pathway, learning recruits a regulated form of proteolysis that removes inhibitory constraints on long-term memory storage.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>9094720</pmid><doi>10.1016/S0092-8674(00)80188-9</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Cell, 1997-04, Vol.89 (1), p.115-126 |
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| subjects | Amino Acid Sequence Animals Antibodies - pharmacology Aplysia Aplysia - physiology Base Sequence Blotting, Northern Cells, Cultured - drug effects Cells, Cultured - enzymology Cyclic AMP - pharmacology Cyclic AMP-Dependent Protein Kinases - metabolism Ganglia, Invertebrate - cytology Genes, Immediate-Early - physiology Long-Term Potentiation - genetics Marine Memory - physiology Microinjections Molecular Sequence Data Nerve Tissue Proteins - genetics Nerve Tissue Proteins - immunology Nerve Tissue Proteins - metabolism Neurons, Afferent - drug effects Neurons, Afferent - enzymology Oligonucleotides, Antisense - pharmacology Proteins - metabolism RNA, Messenger - analysis Serotonin - pharmacology Substrate Specificity Thiolester Hydrolases - genetics Thiolester Hydrolases - immunology Thiolester Hydrolases - metabolism Ubiquitin Thiolesterase Ubiquitins - metabolism |
| title | Ubiquitin C-Terminal Hydrolase Is an Immediate-Early Gene Essential for Long-Term Facilitation in Aplysia |
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