Noncanonical Sequences Involving NHERF1 Interaction with NPT2A Govern Hormone-Regulated Phosphate Transport: Binding Outside the Box
Na+/H+ exchange factor-1 (NHERF1), a multidomain PDZ scaffolding phosphoprotein, is required for the type II sodium-dependent phosphate cotransporter (NPT2A)-mediated renal phosphate absorption. Both PDZ1 and PDZ2 domains are involved in NPT2A-dependent phosphate uptake. Though harboring identical c...
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| description | Na+/H+ exchange factor-1 (NHERF1), a multidomain PDZ scaffolding phosphoprotein, is required for the type II sodium-dependent phosphate cotransporter (NPT2A)-mediated renal phosphate absorption. Both PDZ1 and PDZ2 domains are involved in NPT2A-dependent phosphate uptake. Though harboring identical core-binding motifs, PDZ1 and PDZ2 play entirely different roles in hormone-regulated phosphate transport. PDZ1 is required for the interaction with the C-terminal PDZ-binding sequence of NPT2A (-TRL). Remarkably, phosphocycling at Ser(290) distant from PDZ1, the penultimate step for both parathyroid hormone (PTH) and fibroblast growth factor-23 (FGF23) regulation, controls the association between NHERF1 and NPT2A. PDZ2 interacts with the C-terminal PDZ-recognition motif (-TRL) of G Protein-coupled Receptor Kinase 6A (GRK6A), and that promotes phosphorylation of Ser(290). The compelling biological puzzle is how PDZ1 and PDZ2 with identical GYGF core-binding motifs specifically recognize distinct binding partners. Binding determinants distinct from the canonical PDZ-ligand interactions and located "outside the box" explain PDZ domain specificity. Phosphorylation of NHERF1 by diverse kinases and associated conformational changes in NHERF1 add more complexity to PDZ-binding diversity. |
| doi_str_mv | 10.3390/ijms22031087 |
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Both PDZ1 and PDZ2 domains are involved in NPT2A-dependent phosphate uptake. Though harboring identical core-binding motifs, PDZ1 and PDZ2 play entirely different roles in hormone-regulated phosphate transport. PDZ1 is required for the interaction with the C-terminal PDZ-binding sequence of NPT2A (-TRL). Remarkably, phosphocycling at Ser(290) distant from PDZ1, the penultimate step for both parathyroid hormone (PTH) and fibroblast growth factor-23 (FGF23) regulation, controls the association between NHERF1 and NPT2A. PDZ2 interacts with the C-terminal PDZ-recognition motif (-TRL) of G Protein-coupled Receptor Kinase 6A (GRK6A), and that promotes phosphorylation of Ser(290). The compelling biological puzzle is how PDZ1 and PDZ2 with identical GYGF core-binding motifs specifically recognize distinct binding partners. Binding determinants distinct from the canonical PDZ-ligand interactions and located "outside the box" explain PDZ domain specificity. Phosphorylation of NHERF1 by diverse kinases and associated conformational changes in NHERF1 add more complexity to PDZ-binding diversity.</description><identifier>ISSN: 1422-0067</identifier><identifier>ISSN: 1661-6596</identifier><identifier>EISSN: 1422-0067</identifier><identifier>DOI: 10.3390/ijms22031087</identifier><identifier>PMID: 33499384</identifier><language>eng</language><publisher>BASEL: Mdpi</publisher><subject>Amino Acid Motifs ; Binding ; binding affinity ; Binding sites ; Biochemistry & Molecular Biology ; Chemistry ; Chemistry, Multidisciplinary ; Domains ; Fibroblast Growth Factor-23 ; Fibroblasts ; G protein-coupled receptor kinase ; G-Protein-Coupled Receptor Kinases - chemistry ; Growth factors ; Hormones - chemistry ; Humans ; Ion Transport ; Kinases ; Life Sciences & Biomedicine ; Ligands ; Mutation ; Na+/H+-exchanging ATPase ; Parathyroid ; Parathyroid hormone ; parathyroid hormone (PTH) ; Parathyroid Hormone - chemistry ; PDZ domain ; PDZ-ligand interaction ; Peptides ; Phosphate ; phosphate transport ; Phosphates - chemistry ; Phosphoproteins - chemistry ; Phosphorylation ; Physical Sciences ; Protein Binding ; Protein Conformation ; Protein Domains ; Proteins ; Review ; Scaffolding ; Science & Technology ; Serine - chemistry ; Sodium ; Sodium-Hydrogen Exchangers - chemistry ; Sodium-Phosphate Cotransporter Proteins, Type IIa - chemistry ; type II sodium-dependent phosphate cotransporter (NPT2A)</subject><ispartof>International journal of molecular sciences, 2021-01, Vol.22 (3), p.1087, Article 1087</ispartof><rights>2021. This work is licensed under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2021 by the authors. 2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>true</woscitedreferencessubscribed><woscitedreferencescount>8</woscitedreferencescount><woscitedreferencesoriginalsourcerecordid>wos000615306200001</woscitedreferencesoriginalsourcerecordid><citedby>FETCH-LOGICAL-c478t-efd8e6e712fd044e6303f634f2037c90348b1d0be90e5d5e8c2c4efe3cf6dc1b3</citedby><cites>FETCH-LOGICAL-c478t-efd8e6e712fd044e6303f634f2037c90348b1d0be90e5d5e8c2c4efe3cf6dc1b3</cites><orcidid>0000-0003-1905-1468 ; 0000-0002-6324-0330</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7866199/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC7866199/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,886,27929,27930,39263,53796,53798</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/33499384$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mamonova, Tatyana</creatorcontrib><creatorcontrib>Friedman, Peter A.</creatorcontrib><title>Noncanonical Sequences Involving NHERF1 Interaction with NPT2A Govern Hormone-Regulated Phosphate Transport: Binding Outside the Box</title><title>International journal of molecular sciences</title><addtitle>INT J MOL SCI</addtitle><addtitle>Int J Mol Sci</addtitle><description>Na+/H+ exchange factor-1 (NHERF1), a multidomain PDZ scaffolding phosphoprotein, is required for the type II sodium-dependent phosphate cotransporter (NPT2A)-mediated renal phosphate absorption. Both PDZ1 and PDZ2 domains are involved in NPT2A-dependent phosphate uptake. Though harboring identical core-binding motifs, PDZ1 and PDZ2 play entirely different roles in hormone-regulated phosphate transport. PDZ1 is required for the interaction with the C-terminal PDZ-binding sequence of NPT2A (-TRL). Remarkably, phosphocycling at Ser(290) distant from PDZ1, the penultimate step for both parathyroid hormone (PTH) and fibroblast growth factor-23 (FGF23) regulation, controls the association between NHERF1 and NPT2A. PDZ2 interacts with the C-terminal PDZ-recognition motif (-TRL) of G Protein-coupled Receptor Kinase 6A (GRK6A), and that promotes phosphorylation of Ser(290). The compelling biological puzzle is how PDZ1 and PDZ2 with identical GYGF core-binding motifs specifically recognize distinct binding partners. Binding determinants distinct from the canonical PDZ-ligand interactions and located "outside the box" explain PDZ domain specificity. Phosphorylation of NHERF1 by diverse kinases and associated conformational changes in NHERF1 add more complexity to PDZ-binding diversity.</description><subject>Amino Acid Motifs</subject><subject>Binding</subject><subject>binding affinity</subject><subject>Binding sites</subject><subject>Biochemistry & Molecular Biology</subject><subject>Chemistry</subject><subject>Chemistry, Multidisciplinary</subject><subject>Domains</subject><subject>Fibroblast Growth Factor-23</subject><subject>Fibroblasts</subject><subject>G protein-coupled receptor kinase</subject><subject>G-Protein-Coupled Receptor Kinases - chemistry</subject><subject>Growth factors</subject><subject>Hormones - chemistry</subject><subject>Humans</subject><subject>Ion Transport</subject><subject>Kinases</subject><subject>Life Sciences & Biomedicine</subject><subject>Ligands</subject><subject>Mutation</subject><subject>Na+/H+-exchanging ATPase</subject><subject>Parathyroid</subject><subject>Parathyroid hormone</subject><subject>parathyroid hormone (PTH)</subject><subject>Parathyroid Hormone - 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chemistry</topic><topic>Growth factors</topic><topic>Hormones - chemistry</topic><topic>Humans</topic><topic>Ion Transport</topic><topic>Kinases</topic><topic>Life Sciences & Biomedicine</topic><topic>Ligands</topic><topic>Mutation</topic><topic>Na+/H+-exchanging ATPase</topic><topic>Parathyroid</topic><topic>Parathyroid hormone</topic><topic>parathyroid hormone (PTH)</topic><topic>Parathyroid Hormone - chemistry</topic><topic>PDZ domain</topic><topic>PDZ-ligand interaction</topic><topic>Peptides</topic><topic>Phosphate</topic><topic>phosphate transport</topic><topic>Phosphates - chemistry</topic><topic>Phosphoproteins - chemistry</topic><topic>Phosphorylation</topic><topic>Physical Sciences</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Protein Domains</topic><topic>Proteins</topic><topic>Review</topic><topic>Scaffolding</topic><topic>Science & Technology</topic><topic>Serine - chemistry</topic><topic>Sodium</topic><topic>Sodium-Hydrogen Exchangers - chemistry</topic><topic>Sodium-Phosphate Cotransporter Proteins, Type IIa - chemistry</topic><topic>type II sodium-dependent phosphate cotransporter (NPT2A)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mamonova, Tatyana</creatorcontrib><creatorcontrib>Friedman, Peter A.</creatorcontrib><collection>Web of Science Core Collection</collection><collection>Science Citation Index Expanded</collection><collection>Web of Science - Science Citation Index Expanded - 2021</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Research Library</collection><collection>Research Library (Corporate)</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><collection>DOAJ Directory of Open Access Journals</collection><jtitle>International journal of molecular sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mamonova, Tatyana</au><au>Friedman, Peter A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Noncanonical Sequences Involving NHERF1 Interaction with NPT2A Govern Hormone-Regulated Phosphate Transport: Binding Outside the Box</atitle><jtitle>International journal of molecular sciences</jtitle><stitle>INT J MOL SCI</stitle><addtitle>Int J Mol Sci</addtitle><date>2021-01-22</date><risdate>2021</risdate><volume>22</volume><issue>3</issue><spage>1087</spage><pages>1087-</pages><artnum>1087</artnum><issn>1422-0067</issn><issn>1661-6596</issn><eissn>1422-0067</eissn><abstract>Na+/H+ exchange factor-1 (NHERF1), a multidomain PDZ scaffolding phosphoprotein, is required for the type II sodium-dependent phosphate cotransporter (NPT2A)-mediated renal phosphate absorption. Both PDZ1 and PDZ2 domains are involved in NPT2A-dependent phosphate uptake. Though harboring identical core-binding motifs, PDZ1 and PDZ2 play entirely different roles in hormone-regulated phosphate transport. PDZ1 is required for the interaction with the C-terminal PDZ-binding sequence of NPT2A (-TRL). Remarkably, phosphocycling at Ser(290) distant from PDZ1, the penultimate step for both parathyroid hormone (PTH) and fibroblast growth factor-23 (FGF23) regulation, controls the association between NHERF1 and NPT2A. PDZ2 interacts with the C-terminal PDZ-recognition motif (-TRL) of G Protein-coupled Receptor Kinase 6A (GRK6A), and that promotes phosphorylation of Ser(290). The compelling biological puzzle is how PDZ1 and PDZ2 with identical GYGF core-binding motifs specifically recognize distinct binding partners. Binding determinants distinct from the canonical PDZ-ligand interactions and located "outside the box" explain PDZ domain specificity. Phosphorylation of NHERF1 by diverse kinases and associated conformational changes in NHERF1 add more complexity to PDZ-binding diversity.</abstract><cop>BASEL</cop><pub>Mdpi</pub><pmid>33499384</pmid><doi>10.3390/ijms22031087</doi><tpages>15</tpages><orcidid>https://orcid.org/0000-0003-1905-1468</orcidid><orcidid>https://orcid.org/0000-0002-6324-0330</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Motifs Binding binding affinity Binding sites Biochemistry & Molecular Biology Chemistry Chemistry, Multidisciplinary Domains Fibroblast Growth Factor-23 Fibroblasts G protein-coupled receptor kinase G-Protein-Coupled Receptor Kinases - chemistry Growth factors Hormones - chemistry Humans Ion Transport Kinases Life Sciences & Biomedicine Ligands Mutation Na+/H+-exchanging ATPase Parathyroid Parathyroid hormone parathyroid hormone (PTH) Parathyroid Hormone - chemistry PDZ domain PDZ-ligand interaction Peptides Phosphate phosphate transport Phosphates - chemistry Phosphoproteins - chemistry Phosphorylation Physical Sciences Protein Binding Protein Conformation Protein Domains Proteins Review Scaffolding Science & Technology Serine - chemistry Sodium Sodium-Hydrogen Exchangers - chemistry Sodium-Phosphate Cotransporter Proteins, Type IIa - chemistry type II sodium-dependent phosphate cotransporter (NPT2A) |
| title | Noncanonical Sequences Involving NHERF1 Interaction with NPT2A Govern Hormone-Regulated Phosphate Transport: Binding Outside the Box |
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