Involvement of a Mitochondrial Phosphatase in the Regulation of ATP Production and Insulin Secretion in Pancreatic β Cells
Reversible phosphorylation is the cell’s most prevalent form of posttranslational modification, yet its role in the regulation of mitochondrial functions is poorly understood. We have discovered that a member of the dual-specific protein tyrosine phosphatase (DS-PTP) family, PTPMT1 ( PTP localized t...
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| Veröffentlicht in: | Molecular cell 2005-07, Vol.19 (2), p.197-207 |
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| creator | Pagliarini, David J. Wiley, Sandra E. Kimple, Michelle E. Dixon, Jesse R. Kelly, Patrick Worby, Carolyn A. Casey, Patrick J. Dixon, Jack E. |
| description | Reversible phosphorylation is the cell’s most prevalent form of posttranslational modification, yet its role in the regulation of mitochondrial functions is poorly understood. We have discovered that a member of the dual-specific protein tyrosine phosphatase (DS-PTP) family, PTPMT1 (
PTP localized to the
Mi
tochondrion
1) resides nearly exclusively in mitochondria. PTPMT1 is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. Knockdown of PTPMT1 expression in the pancreatic insulinoma cell line INS-1 832/13 alters the mitochondrial phosphoprotein profile and markedly enhances both ATP production and insulin secretion. These data define PTPMT1 as a potential drug target for the treatment of type II diabetes and strengthen the notion that mitochondria are an underappreciated site of signaling by reversible phosphorylation. |
| doi_str_mv | 10.1016/j.molcel.2005.06.008 |
| format | Article |
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PTP localized to the
Mi
tochondrion
1) resides nearly exclusively in mitochondria. PTPMT1 is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. Knockdown of PTPMT1 expression in the pancreatic insulinoma cell line INS-1 832/13 alters the mitochondrial phosphoprotein profile and markedly enhances both ATP production and insulin secretion. These data define PTPMT1 as a potential drug target for the treatment of type II diabetes and strengthen the notion that mitochondria are an underappreciated site of signaling by reversible phosphorylation.</description><identifier>ISSN: 1097-2765</identifier><identifier>EISSN: 1097-4164</identifier><identifier>DOI: 10.1016/j.molcel.2005.06.008</identifier><identifier>PMID: 16039589</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Triphosphate - biosynthesis ; Adenosine Triphosphate - metabolism ; Amino Acid Sequence ; Animals ; Cercopithecus aethiops ; Cloning, Molecular ; COS Cells ; Insulin - metabolism ; Insulin Secretion ; Islets of Langerhans - cytology ; Islets of Langerhans - enzymology ; Islets of Langerhans - metabolism ; Mice ; Mitochondria - enzymology ; Mitochondria - metabolism ; Molecular Sequence Data ; Protein Tyrosine Phosphatases - metabolism ; Time Factors</subject><ispartof>Molecular cell, 2005-07, Vol.19 (2), p.197-207</ispartof><rights>2005 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c406t-c91f085ce32c9b4c13196f62e20aaddc9b63fb249e1e7854f017aa7be98e51f43</citedby><cites>FETCH-LOGICAL-c406t-c91f085ce32c9b4c13196f62e20aaddc9b63fb249e1e7854f017aa7be98e51f43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S1097276505013869$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16039589$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pagliarini, David J.</creatorcontrib><creatorcontrib>Wiley, Sandra E.</creatorcontrib><creatorcontrib>Kimple, Michelle E.</creatorcontrib><creatorcontrib>Dixon, Jesse R.</creatorcontrib><creatorcontrib>Kelly, Patrick</creatorcontrib><creatorcontrib>Worby, Carolyn A.</creatorcontrib><creatorcontrib>Casey, Patrick J.</creatorcontrib><creatorcontrib>Dixon, Jack E.</creatorcontrib><title>Involvement of a Mitochondrial Phosphatase in the Regulation of ATP Production and Insulin Secretion in Pancreatic β Cells</title><title>Molecular cell</title><addtitle>Mol Cell</addtitle><description>Reversible phosphorylation is the cell’s most prevalent form of posttranslational modification, yet its role in the regulation of mitochondrial functions is poorly understood. We have discovered that a member of the dual-specific protein tyrosine phosphatase (DS-PTP) family, PTPMT1 (
PTP localized to the
Mi
tochondrion
1) resides nearly exclusively in mitochondria. PTPMT1 is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. Knockdown of PTPMT1 expression in the pancreatic insulinoma cell line INS-1 832/13 alters the mitochondrial phosphoprotein profile and markedly enhances both ATP production and insulin secretion. These data define PTPMT1 as a potential drug target for the treatment of type II diabetes and strengthen the notion that mitochondria are an underappreciated site of signaling by reversible phosphorylation.</description><subject>Adenosine Triphosphate - biosynthesis</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Cercopithecus aethiops</subject><subject>Cloning, Molecular</subject><subject>COS Cells</subject><subject>Insulin - metabolism</subject><subject>Insulin Secretion</subject><subject>Islets of Langerhans - cytology</subject><subject>Islets of Langerhans - enzymology</subject><subject>Islets of Langerhans - metabolism</subject><subject>Mice</subject><subject>Mitochondria - enzymology</subject><subject>Mitochondria - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Protein Tyrosine Phosphatases - metabolism</subject><subject>Time Factors</subject><issn>1097-2765</issn><issn>1097-4164</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFOGzEQhq0KVCjtGyDkE7dsx7te7-4FCUVAIwU1ovRsOd5Z4shrB3s3EuKteJA-Ux0SiRunmfn1_zOaj5BzBhkDJn6us95bjTbLAcoMRAZQfyGnDJpqwpngR4c-r0R5Qr7FuAZgvKybr-SECSia1J6S15nbervFHt1AfUcVvTeD1yvv2mCUpYuVj5uVGlREahwdVkgf8Gm0ajDe7QLXjwu6CL4d9buiXEtnLo42mf-gDviupmGhXJpSTNN_b3SK1sbv5LhTNuKPQz0jf29vHqe_JvPfd7Pp9XyiOYhhohvWQV1qLHLdLLlmBWtEJ3LMQam2TZooumXOG2RY1SXvgFVKVUtsaixZx4szcrnfuwn-ecQ4yN7ERM4qh36MUtRQsZxDMvK9UQcfY8BOboLpVXiRDOQOulzLPXS5gy5ByAQ9xS4O-8dlj-1H6EA5Ga72Bkxfbg0GGbVBp7E1AfUgW28-v_AfZYyXQA</recordid><startdate>20050722</startdate><enddate>20050722</enddate><creator>Pagliarini, David J.</creator><creator>Wiley, Sandra E.</creator><creator>Kimple, Michelle E.</creator><creator>Dixon, Jesse R.</creator><creator>Kelly, Patrick</creator><creator>Worby, Carolyn A.</creator><creator>Casey, Patrick J.</creator><creator>Dixon, Jack E.</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>7X8</scope></search><sort><creationdate>20050722</creationdate><title>Involvement of a Mitochondrial Phosphatase in the Regulation of ATP Production and Insulin Secretion in Pancreatic β Cells</title><author>Pagliarini, David J. ; Wiley, Sandra E. ; Kimple, Michelle E. ; Dixon, Jesse R. ; Kelly, Patrick ; Worby, Carolyn A. ; Casey, Patrick J. ; Dixon, Jack E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c406t-c91f085ce32c9b4c13196f62e20aaddc9b63fb249e1e7854f017aa7be98e51f43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Adenosine Triphosphate - biosynthesis</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Cercopithecus aethiops</topic><topic>Cloning, Molecular</topic><topic>COS Cells</topic><topic>Insulin - metabolism</topic><topic>Insulin Secretion</topic><topic>Islets of Langerhans - cytology</topic><topic>Islets of Langerhans - enzymology</topic><topic>Islets of Langerhans - metabolism</topic><topic>Mice</topic><topic>Mitochondria - enzymology</topic><topic>Mitochondria - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Protein Tyrosine Phosphatases - metabolism</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pagliarini, David J.</creatorcontrib><creatorcontrib>Wiley, Sandra E.</creatorcontrib><creatorcontrib>Kimple, Michelle E.</creatorcontrib><creatorcontrib>Dixon, Jesse R.</creatorcontrib><creatorcontrib>Kelly, Patrick</creatorcontrib><creatorcontrib>Worby, Carolyn A.</creatorcontrib><creatorcontrib>Casey, Patrick J.</creatorcontrib><creatorcontrib>Dixon, Jack E.</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>MEDLINE - Academic</collection><jtitle>Molecular cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pagliarini, David J.</au><au>Wiley, Sandra E.</au><au>Kimple, Michelle E.</au><au>Dixon, Jesse R.</au><au>Kelly, Patrick</au><au>Worby, Carolyn A.</au><au>Casey, Patrick J.</au><au>Dixon, Jack E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Involvement of a Mitochondrial Phosphatase in the Regulation of ATP Production and Insulin Secretion in Pancreatic β Cells</atitle><jtitle>Molecular cell</jtitle><addtitle>Mol Cell</addtitle><date>2005-07-22</date><risdate>2005</risdate><volume>19</volume><issue>2</issue><spage>197</spage><epage>207</epage><pages>197-207</pages><issn>1097-2765</issn><eissn>1097-4164</eissn><abstract>Reversible phosphorylation is the cell’s most prevalent form of posttranslational modification, yet its role in the regulation of mitochondrial functions is poorly understood. We have discovered that a member of the dual-specific protein tyrosine phosphatase (DS-PTP) family, PTPMT1 (
PTP localized to the
Mi
tochondrion
1) resides nearly exclusively in mitochondria. PTPMT1 is targeted to the mitochondrion by an N-terminal signal sequence and is found anchored to the matrix face of the inner membrane. Knockdown of PTPMT1 expression in the pancreatic insulinoma cell line INS-1 832/13 alters the mitochondrial phosphoprotein profile and markedly enhances both ATP production and insulin secretion. These data define PTPMT1 as a potential drug target for the treatment of type II diabetes and strengthen the notion that mitochondria are an underappreciated site of signaling by reversible phosphorylation.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>16039589</pmid><doi>10.1016/j.molcel.2005.06.008</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Free Full-Text Journals in Chemistry |
| subjects | Adenosine Triphosphate - biosynthesis Adenosine Triphosphate - metabolism Amino Acid Sequence Animals Cercopithecus aethiops Cloning, Molecular COS Cells Insulin - metabolism Insulin Secretion Islets of Langerhans - cytology Islets of Langerhans - enzymology Islets of Langerhans - metabolism Mice Mitochondria - enzymology Mitochondria - metabolism Molecular Sequence Data Protein Tyrosine Phosphatases - metabolism Time Factors |
| title | Involvement of a Mitochondrial Phosphatase in the Regulation of ATP Production and Insulin Secretion in Pancreatic β Cells |
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