The mechanism of activation of protein kinase FA (the activator of type-1 protein phosphatase) in brain synaptosomes
The ATP.Mg-dependent type-1 protein phosphatase and its activating factor (protein kinase FA) were identified to exist in brain synaptosome. The inactive protein phosphatase was found to exist in the synaptosomal cytosol whereas its activating factor (protein kinase FA) was present in the synaptosom...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1992-01, Vol.182 (1), p.129-136 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Yang, Shiaw-Der Yu, Jau-Song Fong, Yiu-Lian Liu, Jen-Sing |
| description | The ATP.Mg-dependent type-1 protein phosphatase and its activating factor (protein kinase FA) were identified to exist in brain synaptosome. The inactive protein phosphatase was found to exist in the synaptosomal cytosol whereas its activating factor (protein kinase FA) was present in the synaptosomal membrane, indicating that the inactive protein phosphatase and its activating factor FA are localized in two separate subcellular compartments. The membrane-bound FA was found to exist in two forms; approximately 75% of FA is inactive and trypsin-resistant, whereas 25% of FA is active and trypsin-labile. When membranes were incubated with exogenous phospholipase C, the inactive/trypsin-resistant FA could be activated and sequestered to become the active/trypsin-labile FA in a time-and dose-dependent manner. Taken together, the results provide initial evidence that the activation-sequestration of membrane-bound protein kinase FA may represent one mode of control modulating the activity of protein kinase FA and thereby to activate protein phosphatase in brain synaptosome, representing an efficient regulatory mechanism for regulating neurotransmission in the central nervous system. |
| doi_str_mv | 10.1016/S0006-291X(05)80121-4 |
| format | Article |
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The inactive protein phosphatase was found to exist in the synaptosomal cytosol whereas its activating factor (protein kinase FA) was present in the synaptosomal membrane, indicating that the inactive protein phosphatase and its activating factor FA are localized in two separate subcellular compartments. The membrane-bound FA was found to exist in two forms; approximately 75% of FA is inactive and trypsin-resistant, whereas 25% of FA is active and trypsin-labile. When membranes were incubated with exogenous phospholipase C, the inactive/trypsin-resistant FA could be activated and sequestered to become the active/trypsin-labile FA in a time-and dose-dependent manner. Taken together, the results provide initial evidence that the activation-sequestration of membrane-bound protein kinase FA may represent one mode of control modulating the activity of protein kinase FA and thereby to activate protein phosphatase in brain synaptosome, representing an efficient regulatory mechanism for regulating neurotransmission in the central nervous system.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(05)80121-4</identifier><identifier>PMID: 1310012</identifier><identifier>CODEN: BBRCA9</identifier><language>eng</language><publisher>San Diego, CA: Elsevier Inc</publisher><subject>Adenosine Triphosphate - metabolism ; Animals ; Biological and medical sciences ; Calcium-Calmodulin-Dependent Protein Kinases ; Cell physiology ; Cerebral Cortex - enzymology ; Enzyme Activation ; Fundamental and applied biological sciences. Psychology ; Intracellular Membranes - enzymology ; Kinetics ; Molecular and cellular biology ; Neurotransmission ; Phosphoprotein Phosphatases - metabolism ; Phosphorylase b - metabolism ; Phosphorylase Kinase - metabolism ; Protein Kinases - metabolism ; Rabbits ; Swine ; Synaptosomes - enzymology ; Type C Phospholipases - metabolism</subject><ispartof>Biochemical and biophysical research communications, 1992-01, Vol.182 (1), p.129-136</ispartof><rights>1992 Academic Press, Inc.</rights><rights>1992 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c335t-65db026fedbfce5d4f55f458f6a70fd59be238ca27501dd0d5e91dce7c6dc4f43</citedby><cites>FETCH-LOGICAL-c335t-65db026fedbfce5d4f55f458f6a70fd59be238ca27501dd0d5e91dce7c6dc4f43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X05801214$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=5077901$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1310012$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yang, Shiaw-Der</creatorcontrib><creatorcontrib>Yu, Jau-Song</creatorcontrib><creatorcontrib>Fong, Yiu-Lian</creatorcontrib><creatorcontrib>Liu, Jen-Sing</creatorcontrib><title>The mechanism of activation of protein kinase FA (the activator of type-1 protein phosphatase) in brain synaptosomes</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The ATP.Mg-dependent type-1 protein phosphatase and its activating factor (protein kinase FA) were identified to exist in brain synaptosome. The inactive protein phosphatase was found to exist in the synaptosomal cytosol whereas its activating factor (protein kinase FA) was present in the synaptosomal membrane, indicating that the inactive protein phosphatase and its activating factor FA are localized in two separate subcellular compartments. The membrane-bound FA was found to exist in two forms; approximately 75% of FA is inactive and trypsin-resistant, whereas 25% of FA is active and trypsin-labile. When membranes were incubated with exogenous phospholipase C, the inactive/trypsin-resistant FA could be activated and sequestered to become the active/trypsin-labile FA in a time-and dose-dependent manner. Taken together, the results provide initial evidence that the activation-sequestration of membrane-bound protein kinase FA may represent one mode of control modulating the activity of protein kinase FA and thereby to activate protein phosphatase in brain synaptosome, representing an efficient regulatory mechanism for regulating neurotransmission in the central nervous system.</description><subject>Adenosine Triphosphate - metabolism</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Calcium-Calmodulin-Dependent Protein Kinases</subject><subject>Cell physiology</subject><subject>Cerebral Cortex - enzymology</subject><subject>Enzyme Activation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Intracellular Membranes - enzymology</subject><subject>Kinetics</subject><subject>Molecular and cellular biology</subject><subject>Neurotransmission</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Phosphorylase b - metabolism</subject><subject>Phosphorylase Kinase - metabolism</subject><subject>Protein Kinases - metabolism</subject><subject>Rabbits</subject><subject>Swine</subject><subject>Synaptosomes - enzymology</subject><subject>Type C Phospholipases - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFr3DAQhUVpSbdpf0LAh1KSg9sZ2ZLtUwmhaQKBHppCb0KWRqzateVK2sD--9i7y_aYy4jHfDN6zGPsAuEzAsovPwFAlrzD35cgrlpAjmX9iq0QOig5Qv2arU7IW_YupT8AiLXsztgZVjgLvmL5cU3FQGatR5-GIrhCm-yfdPZhXNQUQyY_Fn_9qBMVt9fFZZ4njlCIC5N3E5V4Qqd1SNNa55m_KmbdRz3XtBv1lEMKA6X37I3Tm0Qfju85-3X77fHmrnz48f3-5vqhNFUlcimF7YFLR7Z3hoStnRCuFq2TugFnRdcTr1qjeSMArQUrqENrqDHSmtrV1Tn7dNg7W_u3pZTV4JOhzUaPFLZJNbxpKy7aF0GUHKXcg-IAmhhSiuTUFP2g404hqCUWtY9FLTdXINQ-FrU4uTh-sO0Hsv-nDjnM_Y_Hvk5Gb1zUo_HphAlomg5wxr4eMJqv9uQpqmQ8jYasj2SyssG_YOQZeYmrOg</recordid><startdate>19920115</startdate><enddate>19920115</enddate><creator>Yang, Shiaw-Der</creator><creator>Yu, Jau-Song</creator><creator>Fong, Yiu-Lian</creator><creator>Liu, Jen-Sing</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</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>7X8</scope></search><sort><creationdate>19920115</creationdate><title>The mechanism of activation of protein kinase FA (the activator of type-1 protein phosphatase) in brain synaptosomes</title><author>Yang, Shiaw-Der ; Yu, Jau-Song ; Fong, Yiu-Lian ; Liu, Jen-Sing</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c335t-65db026fedbfce5d4f55f458f6a70fd59be238ca27501dd0d5e91dce7c6dc4f43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Adenosine Triphosphate - metabolism</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Calcium-Calmodulin-Dependent Protein Kinases</topic><topic>Cell physiology</topic><topic>Cerebral Cortex - enzymology</topic><topic>Enzyme Activation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Intracellular Membranes - enzymology</topic><topic>Kinetics</topic><topic>Molecular and cellular biology</topic><topic>Neurotransmission</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Phosphorylase b - metabolism</topic><topic>Phosphorylase Kinase - metabolism</topic><topic>Protein Kinases - metabolism</topic><topic>Rabbits</topic><topic>Swine</topic><topic>Synaptosomes - enzymology</topic><topic>Type C Phospholipases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yang, Shiaw-Der</creatorcontrib><creatorcontrib>Yu, Jau-Song</creatorcontrib><creatorcontrib>Fong, Yiu-Lian</creatorcontrib><creatorcontrib>Liu, Jen-Sing</creatorcontrib><collection>Pascal-Francis</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>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yang, Shiaw-Der</au><au>Yu, Jau-Song</au><au>Fong, Yiu-Lian</au><au>Liu, Jen-Sing</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The mechanism of activation of protein kinase FA (the activator of type-1 protein phosphatase) in brain synaptosomes</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1992-01-15</date><risdate>1992</risdate><volume>182</volume><issue>1</issue><spage>129</spage><epage>136</epage><pages>129-136</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>The ATP.Mg-dependent type-1 protein phosphatase and its activating factor (protein kinase FA) were identified to exist in brain synaptosome. The inactive protein phosphatase was found to exist in the synaptosomal cytosol whereas its activating factor (protein kinase FA) was present in the synaptosomal membrane, indicating that the inactive protein phosphatase and its activating factor FA are localized in two separate subcellular compartments. The membrane-bound FA was found to exist in two forms; approximately 75% of FA is inactive and trypsin-resistant, whereas 25% of FA is active and trypsin-labile. When membranes were incubated with exogenous phospholipase C, the inactive/trypsin-resistant FA could be activated and sequestered to become the active/trypsin-labile FA in a time-and dose-dependent manner. Taken together, the results provide initial evidence that the activation-sequestration of membrane-bound protein kinase FA may represent one mode of control modulating the activity of protein kinase FA and thereby to activate protein phosphatase in brain synaptosome, representing an efficient regulatory mechanism for regulating neurotransmission in the central nervous system.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>1310012</pmid><doi>10.1016/S0006-291X(05)80121-4</doi><tpages>8</tpages></addata></record> |
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| subjects | Adenosine Triphosphate - metabolism Animals Biological and medical sciences Calcium-Calmodulin-Dependent Protein Kinases Cell physiology Cerebral Cortex - enzymology Enzyme Activation Fundamental and applied biological sciences. Psychology Intracellular Membranes - enzymology Kinetics Molecular and cellular biology Neurotransmission Phosphoprotein Phosphatases - metabolism Phosphorylase b - metabolism Phosphorylase Kinase - metabolism Protein Kinases - metabolism Rabbits Swine Synaptosomes - enzymology Type C Phospholipases - metabolism |
| title | The mechanism of activation of protein kinase FA (the activator of type-1 protein phosphatase) in brain synaptosomes |
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