Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-H/Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating neurons
Mutations in ATCAY that encodes the brain-specific protein BNIP-H (or Caytaxin) lead to Cayman cerebellar ataxia. BNIP-H binds to glutaminase, a neurotransmitter-producing enzyme, and affects its activity and intracellular localization. Here we describe the identification and characterization of the...
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| description | Mutations in ATCAY that encodes the brain-specific protein BNIP-H (or Caytaxin) lead to Cayman cerebellar ataxia. BNIP-H binds to glutaminase, a neurotransmitter-producing enzyme, and affects its activity and intracellular localization. Here we describe the identification and characterization of the binding between BNIP-H and Pin1, a peptidyl-prolyl cis/trans isomerase. BNIP-H interacted with Pin1 after nerve growth factor-stimulation and they co-localized in the neurites and cytosol of differentiating pheochromocytoma PC12 cells and the embryonic carcinoma P19 cells. Deletional mutagenesis revealed two cryptic binding sites within the C-terminus of BNIP-H such that single point mutants affecting the WW domain of Pin1 completely abolished their binding. Although these two sites do not contain any of the canonical Pin1-binding motifs they showed differential binding profiles to Pin1 WW domain mutants S16E, S16A and W34A, and the catalytically inert C113A of its isomerase domain. Furthermore, their direct interaction would occur only upon disrupting the ability of BNIP-H to form an intramolecular interaction by two similar regions. Furthermore, expression of Pin1 disrupted the BNIP-H/glutaminase complex formation in PC12 cells under nerve growth factor-stimulation. These results indicate that nerve growth factor may stimulate the interaction of BNIP-H with Pin1 by releasing its intramolecular inhibition. Such a mechanism could provide a post-translational regulation on the cellular activity of BNIP-H during neuronal differentiation. |
| doi_str_mv | 10.1371/journal.pone.0002686 |
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BNIP-H binds to glutaminase, a neurotransmitter-producing enzyme, and affects its activity and intracellular localization. Here we describe the identification and characterization of the binding between BNIP-H and Pin1, a peptidyl-prolyl cis/trans isomerase. BNIP-H interacted with Pin1 after nerve growth factor-stimulation and they co-localized in the neurites and cytosol of differentiating pheochromocytoma PC12 cells and the embryonic carcinoma P19 cells. Deletional mutagenesis revealed two cryptic binding sites within the C-terminus of BNIP-H such that single point mutants affecting the WW domain of Pin1 completely abolished their binding. Although these two sites do not contain any of the canonical Pin1-binding motifs they showed differential binding profiles to Pin1 WW domain mutants S16E, S16A and W34A, and the catalytically inert C113A of its isomerase domain. Furthermore, their direct interaction would occur only upon disrupting the ability of BNIP-H to form an intramolecular interaction by two similar regions. Furthermore, expression of Pin1 disrupted the BNIP-H/glutaminase complex formation in PC12 cells under nerve growth factor-stimulation. These results indicate that nerve growth factor may stimulate the interaction of BNIP-H with Pin1 by releasing its intramolecular inhibition. Such a mechanism could provide a post-translational regulation on the cellular activity of BNIP-H during neuronal differentiation.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0002686</identifier><identifier>PMID: 18628984</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Adaptor Proteins, Signal Transducing - metabolism ; Alzheimer's disease ; Amino acids ; Animals ; Apoptosis ; Ataxia ; Axons ; Binding Sites ; Biochemistry ; Biochemistry/Protein Chemistry ; Brain ; C-Terminus ; Cell Biology/Cell Signaling ; Cell Biology/Neuronal Signaling Mechanisms ; Cell cycle ; Cell Differentiation ; Cell growth ; Cerebellar ataxia ; Cerebellum ; Complex formation ; Cytosol ; Enzymes ; Fibroblasts ; Gene expression ; Gene Expression Regulation, Enzymologic ; Genetic aspects ; Glutaminase ; Glutathione Transferase - metabolism ; Growth factors ; Homeostasis ; Humans ; Kinases ; Localization ; Models, Biological ; Mutagenesis ; Mutants ; Mutation ; Nerve growth factor ; Nerve Growth Factor - metabolism ; Nerve Tissue Proteins - metabolism ; Neurons ; Neurons - enzymology ; Neurons - metabolism ; PC12 Cells ; Peptidylprolyl isomerase ; Pheochromocytoma cells ; Phosphatase ; Phosphorylation ; Pin1 protein ; Post-translation ; Protein Structure, Tertiary ; Proteins ; Rats ; Rodents ; Science ; Stimulation ; Trends</subject><ispartof>PloS one, 2008-07, Vol.3 (7), p.e2686-e2686</ispartof><rights>COPYRIGHT 2008 Public Library of Science</rights><rights>2008 Buschdorf et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Buschdorf et al. 2008</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c693t-e5d863c30ca73aea7bdbf15a765e6e0f8f9de4d208c419b9d7a6b8519398ec673</citedby><cites>FETCH-LOGICAL-c693t-e5d863c30ca73aea7bdbf15a765e6e0f8f9de4d208c419b9d7a6b8519398ec673</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2442193/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2442193/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,2096,2915,23845,27901,27902,53766,53768,79569,79570</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18628984$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Buschdorf, Jan Paul</creatorcontrib><creatorcontrib>Chew, Li Li</creatorcontrib><creatorcontrib>Soh, Unice Jim Kim</creatorcontrib><creatorcontrib>Liou, Yih-Cherng</creatorcontrib><creatorcontrib>Low, Boon Chuan</creatorcontrib><title>Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-H/Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating neurons</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>Mutations in ATCAY that encodes the brain-specific protein BNIP-H (or Caytaxin) lead to Cayman cerebellar ataxia. BNIP-H binds to glutaminase, a neurotransmitter-producing enzyme, and affects its activity and intracellular localization. Here we describe the identification and characterization of the binding between BNIP-H and Pin1, a peptidyl-prolyl cis/trans isomerase. BNIP-H interacted with Pin1 after nerve growth factor-stimulation and they co-localized in the neurites and cytosol of differentiating pheochromocytoma PC12 cells and the embryonic carcinoma P19 cells. Deletional mutagenesis revealed two cryptic binding sites within the C-terminus of BNIP-H such that single point mutants affecting the WW domain of Pin1 completely abolished their binding. Although these two sites do not contain any of the canonical Pin1-binding motifs they showed differential binding profiles to Pin1 WW domain mutants S16E, S16A and W34A, and the catalytically inert C113A of its isomerase domain. Furthermore, their direct interaction would occur only upon disrupting the ability of BNIP-H to form an intramolecular interaction by two similar regions. Furthermore, expression of Pin1 disrupted the BNIP-H/glutaminase complex formation in PC12 cells under nerve growth factor-stimulation. These results indicate that nerve growth factor may stimulate the interaction of BNIP-H with Pin1 by releasing its intramolecular inhibition. Such a mechanism could provide a post-translational regulation on the cellular activity of BNIP-H during neuronal differentiation.</description><subject>Adaptor Proteins, Signal Transducing - metabolism</subject><subject>Alzheimer's disease</subject><subject>Amino acids</subject><subject>Animals</subject><subject>Apoptosis</subject><subject>Ataxia</subject><subject>Axons</subject><subject>Binding Sites</subject><subject>Biochemistry</subject><subject>Biochemistry/Protein Chemistry</subject><subject>Brain</subject><subject>C-Terminus</subject><subject>Cell Biology/Cell Signaling</subject><subject>Cell Biology/Neuronal Signaling Mechanisms</subject><subject>Cell cycle</subject><subject>Cell Differentiation</subject><subject>Cell growth</subject><subject>Cerebellar ataxia</subject><subject>Cerebellum</subject><subject>Complex formation</subject><subject>Cytosol</subject><subject>Enzymes</subject><subject>Fibroblasts</subject><subject>Gene expression</subject><subject>Gene Expression Regulation, Enzymologic</subject><subject>Genetic aspects</subject><subject>Glutaminase</subject><subject>Glutathione Transferase - metabolism</subject><subject>Growth factors</subject><subject>Homeostasis</subject><subject>Humans</subject><subject>Kinases</subject><subject>Localization</subject><subject>Models, Biological</subject><subject>Mutagenesis</subject><subject>Mutants</subject><subject>Mutation</subject><subject>Nerve growth factor</subject><subject>Nerve Growth Factor - metabolism</subject><subject>Nerve Tissue Proteins - metabolism</subject><subject>Neurons</subject><subject>Neurons - enzymology</subject><subject>Neurons - metabolism</subject><subject>PC12 Cells</subject><subject>Peptidylprolyl isomerase</subject><subject>Pheochromocytoma cells</subject><subject>Phosphatase</subject><subject>Phosphorylation</subject><subject>Pin1 protein</subject><subject>Post-translation</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Rats</subject><subject>Rodents</subject><subject>Science</subject><subject>Stimulation</subject><subject>Trends</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><sourceid>DOA</sourceid><recordid>eNqNk19v0zAQwCMEYmPwDRBYQprEQzvbSRznBWlUwCpN28S_V-vqXFpXiV1sZ1u_Bp8YlxZoEQ88JTr_7ue7ky_LnjM6ZnnFzpZu8Ba68cpZHFNKuZDiQXbM6pyPBKf5w73_o-xJCEtKy1wK8Tg7YlJwWcviOPt-hf4Wydy7u7ggLejoPAnR9EMHEQMxNqJPUeMscS2ZwLoHSyDCvQGy8i6iseTt1fRmdHGWDjdxS-5Mcq1wFU2z7kaJ6tYdMcH1SRWQ3BjLkpg0pm3Ro40GorFzYnHwzoan2aMWuoDPdt-T7Mv7d58nF6PL6w_TyfnlSIs6jyMsGylynVMNVQ4I1ayZtayESpQokLayrRssGk6lLlg9q5sKxEyWaSa1RC2q_CR7ufWuOhfUbpxBsZxxXleMb4jplmgcLNXKmx78Wjkw6mfA-bkCH43uULGC6VnLoWpEWVSpJs1liRXTNa00tJhcb3a3DbMeG53a9tAdSA9PrFmoubtVvCh4KjoJTncC774NGKLqTdDYdWDRDUFxRouK8zKBr_4C_93beEvNIZVvbOvSralsaLA3Or2p1qT4eVKKghZSpoTXBwmJiXgf5zCEoKafPv4_e_31kD3dYxcIXVwE1w2bJxcOwWILau9C8Nj-Hh6jarMSv_pUm5VQu5VIaS_2B_8nabcD-Q9sLQta</recordid><startdate>20080716</startdate><enddate>20080716</enddate><creator>Buschdorf, Jan Paul</creator><creator>Chew, Li Li</creator><creator>Soh, Unice Jim Kim</creator><creator>Liou, Yih-Cherng</creator><creator>Low, Boon Chuan</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>IOV</scope><scope>ISR</scope><scope>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>7TK</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20080716</creationdate><title>Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-H/Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating neurons</title><author>Buschdorf, Jan Paul ; Chew, Li Li ; Soh, Unice Jim Kim ; Liou, Yih-Cherng ; Low, Boon Chuan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c693t-e5d863c30ca73aea7bdbf15a765e6e0f8f9de4d208c419b9d7a6b8519398ec673</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Adaptor Proteins, Signal Transducing - metabolism</topic><topic>Alzheimer's disease</topic><topic>Amino acids</topic><topic>Animals</topic><topic>Apoptosis</topic><topic>Ataxia</topic><topic>Axons</topic><topic>Binding Sites</topic><topic>Biochemistry</topic><topic>Biochemistry/Protein Chemistry</topic><topic>Brain</topic><topic>C-Terminus</topic><topic>Cell Biology/Cell Signaling</topic><topic>Cell Biology/Neuronal Signaling Mechanisms</topic><topic>Cell cycle</topic><topic>Cell Differentiation</topic><topic>Cell growth</topic><topic>Cerebellar ataxia</topic><topic>Cerebellum</topic><topic>Complex formation</topic><topic>Cytosol</topic><topic>Enzymes</topic><topic>Fibroblasts</topic><topic>Gene expression</topic><topic>Gene Expression Regulation, Enzymologic</topic><topic>Genetic aspects</topic><topic>Glutaminase</topic><topic>Glutathione Transferase - metabolism</topic><topic>Growth factors</topic><topic>Homeostasis</topic><topic>Humans</topic><topic>Kinases</topic><topic>Localization</topic><topic>Models, Biological</topic><topic>Mutagenesis</topic><topic>Mutants</topic><topic>Mutation</topic><topic>Nerve growth factor</topic><topic>Nerve Growth Factor - metabolism</topic><topic>Nerve Tissue Proteins - metabolism</topic><topic>Neurons</topic><topic>Neurons - enzymology</topic><topic>Neurons - metabolism</topic><topic>PC12 Cells</topic><topic>Peptidylprolyl isomerase</topic><topic>Pheochromocytoma cells</topic><topic>Phosphatase</topic><topic>Phosphorylation</topic><topic>Pin1 protein</topic><topic>Post-translation</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Rats</topic><topic>Rodents</topic><topic>Science</topic><topic>Stimulation</topic><topic>Trends</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Buschdorf, Jan Paul</creatorcontrib><creatorcontrib>Chew, Li Li</creatorcontrib><creatorcontrib>Soh, Unice Jim Kim</creatorcontrib><creatorcontrib>Liou, Yih-Cherng</creatorcontrib><creatorcontrib>Low, Boon Chuan</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Gale In Context: Opposing Viewpoints</collection><collection>Gale In Context: Science</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Biotechnology Research Abstracts</collection><collection>Nursing & Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Meteorological & Geoastrophysical Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies & Aerospace Collection</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing & Allied Health Database (Alumni Edition)</collection><collection>Meteorological & Geoastrophysical Abstracts - 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BNIP-H binds to glutaminase, a neurotransmitter-producing enzyme, and affects its activity and intracellular localization. Here we describe the identification and characterization of the binding between BNIP-H and Pin1, a peptidyl-prolyl cis/trans isomerase. BNIP-H interacted with Pin1 after nerve growth factor-stimulation and they co-localized in the neurites and cytosol of differentiating pheochromocytoma PC12 cells and the embryonic carcinoma P19 cells. Deletional mutagenesis revealed two cryptic binding sites within the C-terminus of BNIP-H such that single point mutants affecting the WW domain of Pin1 completely abolished their binding. Although these two sites do not contain any of the canonical Pin1-binding motifs they showed differential binding profiles to Pin1 WW domain mutants S16E, S16A and W34A, and the catalytically inert C113A of its isomerase domain. Furthermore, their direct interaction would occur only upon disrupting the ability of BNIP-H to form an intramolecular interaction by two similar regions. Furthermore, expression of Pin1 disrupted the BNIP-H/glutaminase complex formation in PC12 cells under nerve growth factor-stimulation. These results indicate that nerve growth factor may stimulate the interaction of BNIP-H with Pin1 by releasing its intramolecular inhibition. Such a mechanism could provide a post-translational regulation on the cellular activity of BNIP-H during neuronal differentiation.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>18628984</pmid><doi>10.1371/journal.pone.0002686</doi><tpages>e2686</tpages><oa>free_for_read</oa></addata></record> |
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| source | Public Library of Science (PLoS) Journals Open Access; MEDLINE; DOAJ Directory of Open Access Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Free Full-Text Journals in Chemistry |
| subjects | Adaptor Proteins, Signal Transducing - metabolism Alzheimer's disease Amino acids Animals Apoptosis Ataxia Axons Binding Sites Biochemistry Biochemistry/Protein Chemistry Brain C-Terminus Cell Biology/Cell Signaling Cell Biology/Neuronal Signaling Mechanisms Cell cycle Cell Differentiation Cell growth Cerebellar ataxia Cerebellum Complex formation Cytosol Enzymes Fibroblasts Gene expression Gene Expression Regulation, Enzymologic Genetic aspects Glutaminase Glutathione Transferase - metabolism Growth factors Homeostasis Humans Kinases Localization Models, Biological Mutagenesis Mutants Mutation Nerve growth factor Nerve Growth Factor - metabolism Nerve Tissue Proteins - metabolism Neurons Neurons - enzymology Neurons - metabolism PC12 Cells Peptidylprolyl isomerase Pheochromocytoma cells Phosphatase Phosphorylation Pin1 protein Post-translation Protein Structure, Tertiary Proteins Rats Rodents Science Stimulation Trends |
| title | Nerve growth factor stimulates interaction of Cayman ataxia protein BNIP-H/Caytaxin with peptidyl-prolyl isomerase Pin1 in differentiating neurons |
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