Genetic encoding of 3‐nitro‐tyrosine reveals the impacts of 14‐3‐3 nitration on client binding and dephosphorylation
14‐3‐3 proteins are central hub regulators of hundreds of phosphorylated “client” proteins. They are subject to over 60 post‐translational modifications (PTMs), yet little is known how these PTMs alter 14‐3‐3 function and its ability to regulate downstream signaling pathways. An often neglected, but...
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| Published in | Protein science Vol. 32; no. 3; pp. e4574 - n/a |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
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Hoboken, USA
John Wiley & Sons, Inc
01.03.2023
Wiley Subscription Services, Inc Wiley Blackwell (John Wiley & Sons) |
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| Abstract | 14‐3‐3 proteins are central hub regulators of hundreds of phosphorylated “client” proteins. They are subject to over 60 post‐translational modifications (PTMs), yet little is known how these PTMs alter 14‐3‐3 function and its ability to regulate downstream signaling pathways. An often neglected, but well‐documented 14‐3‐3 PTM found under physiological and immune‐stimulatory conditions is the conversion of tyrosine to 3‐nitro‐tyrosine at several Tyr sites, two of which are located at sites considered important for 14‐3‐3 function: Y130 (β‐isoform numbering) is located in the primary phospho‐client peptide‐binding groove, while Y213 is found on a secondary binding site that engages with clients for full 14‐3‐3/client complex formation and client regulation. By genetically encoding 3‐nitro‐tyrosine, we sought to understand if nitration at Y130 and Y213 effectively modulated 14‐3‐3 structure, function, and client complexation. The 1.5 Å resolution crystal structure of 14‐3‐3 nitrated at Y130 showed the nitro group altered the conformation of key residues in the primary binding site, while functional studies confirmed client proteins failed to bind this variant of 14‐3‐3. But, in contrast to other client‐binding deficient variants, it did not localize to the nucleus. The 1.9 Å resolution structure of 14‐3‐3 nitrated at Y213 revealed unusual flexibility of its C‐terminal α‐helix resulting in domain swapping, suggesting additional structural plasticity though its relevance is not clear as this nitrated form retained its ability to bind clients. Collectively, our data suggest that nitration of 14‐3‐3 will alter downstream signaling systems, and if uncontrolled could result in global dysregulation of the 14‐3‐3 interactome.
PDB Code(s): 8EQ8 and 8EQH; |
|---|---|
| AbstractList | 14-3-3 proteins are central hub regulators of hundreds of phosphorylated "client" proteins. They are subject to over 60 post-translational modifications (PTMs), yet little is known how these PTMs alter 14-3-3 function and its ability to regulate downstream signaling pathways. An often neglected, but well-documented 14-3-3 PTM found under physiological and immune-stimulatory conditions is the conversion of tyrosine to 3-nitro-tyrosine at several Tyr sites, two of which are located at sites considered important for 14-3-3 function: Y130 (β-isoform numbering) is located in the primary phospho-client peptide-binding groove, while Y213 is found on a secondary binding site that engages with clients for full 14-3-3/client complex formation and client regulation. By genetically encoding 3-nitro-tyrosine, we sought to understand if nitration at Y130 and Y213 effectively modulated 14-3-3 structure, function, and client complexation. The 1.5 Å resolution crystal structure of 14-3-3 nitrated at Y130 showed the nitro group altered the conformation of key residues in the primary binding site, while functional studies confirmed client proteins failed to bind this variant of 14-3-3. But, in contrast to other client-binding deficient variants, it did not localize to the nucleus. The 1.9 Å resolution structure of 14-3-3 nitrated at Y213 revealed unusual flexibility of its C-terminal α-helix resulting in domain swapping, suggesting additional structural plasticity though its relevance is not clear as this nitrated form retained its ability to bind clients. Collectively, our data suggest that nitration of 14-3-3 will alter downstream signaling systems, and if uncontrolled could result in global dysregulation of the 14-3-3 interactome.14-3-3 proteins are central hub regulators of hundreds of phosphorylated "client" proteins. They are subject to over 60 post-translational modifications (PTMs), yet little is known how these PTMs alter 14-3-3 function and its ability to regulate downstream signaling pathways. An often neglected, but well-documented 14-3-3 PTM found under physiological and immune-stimulatory conditions is the conversion of tyrosine to 3-nitro-tyrosine at several Tyr sites, two of which are located at sites considered important for 14-3-3 function: Y130 (β-isoform numbering) is located in the primary phospho-client peptide-binding groove, while Y213 is found on a secondary binding site that engages with clients for full 14-3-3/client complex formation and client regulation. By genetically encoding 3-nitro-tyrosine, we sought to understand if nitration at Y130 and Y213 effectively modulated 14-3-3 structure, function, and client complexation. The 1.5 Å resolution crystal structure of 14-3-3 nitrated at Y130 showed the nitro group altered the conformation of key residues in the primary binding site, while functional studies confirmed client proteins failed to bind this variant of 14-3-3. But, in contrast to other client-binding deficient variants, it did not localize to the nucleus. The 1.9 Å resolution structure of 14-3-3 nitrated at Y213 revealed unusual flexibility of its C-terminal α-helix resulting in domain swapping, suggesting additional structural plasticity though its relevance is not clear as this nitrated form retained its ability to bind clients. Collectively, our data suggest that nitration of 14-3-3 will alter downstream signaling systems, and if uncontrolled could result in global dysregulation of the 14-3-3 interactome. 14‐3‐3 proteins are central hub regulators of hundreds of phosphorylated “client” proteins. They are subject to over 60 post‐translational modifications (PTMs), yet little is known how these PTMs alter 14‐3‐3 function and its ability to regulate downstream signaling pathways. An often neglected, but well‐documented 14‐3‐3 PTM found under physiological and immune‐stimulatory conditions is the conversion of tyrosine to 3‐nitro‐tyrosine at several Tyr sites, two of which are located at sites considered important for 14‐3‐3 function: Y130 (β‐isoform numbering) is located in the primary phospho‐client peptide‐binding groove, while Y213 is found on a secondary binding site that engages with clients for full 14‐3‐3/client complex formation and client regulation. By genetically encoding 3‐nitro‐tyrosine, we sought to understand if nitration at Y130 and Y213 effectively modulated 14‐3‐3 structure, function, and client complexation. The 1.5 Å resolution crystal structure of 14‐3‐3 nitrated at Y130 showed the nitro group altered the conformation of key residues in the primary binding site, while functional studies confirmed client proteins failed to bind this variant of 14‐3‐3. But, in contrast to other client‐binding deficient variants, it did not localize to the nucleus. The 1.9 Å resolution structure of 14‐3‐3 nitrated at Y213 revealed unusual flexibility of its C‐terminal α‐helix resulting in domain swapping, suggesting additional structural plasticity though its relevance is not clear as this nitrated form retained its ability to bind clients. Collectively, our data suggest that nitration of 14‐3‐3 will alter downstream signaling systems, and if uncontrolled could result in global dysregulation of the 14‐3‐3 interactome. PDB Code(s): 8EQ8 and 8EQH; 14‐3‐3 proteins are central hub regulators of hundreds of phosphorylated “client” proteins. They are subject to over 60 post‐translational modifications (PTMs), yet little is known how these PTMs alter 14‐3‐3 function and its ability to regulate downstream signaling pathways. An often neglected, but well‐documented 14‐3‐3 PTM found under physiological and immune‐stimulatory conditions is the conversion of tyrosine to 3‐nitro‐tyrosine at several Tyr sites, two of which are located at sites considered important for 14‐3‐3 function: Y130 (β‐isoform numbering) is located in the primary phospho‐client peptide‐binding groove, while Y213 is found on a secondary binding site that engages with clients for full 14‐3‐3/client complex formation and client regulation. By genetically encoding 3‐nitro‐tyrosine, we sought to understand if nitration at Y130 and Y213 effectively modulated 14‐3‐3 structure, function, and client complexation. The 1.5 Å resolution crystal structure of 14‐3‐3 nitrated at Y130 showed the nitro group altered the conformation of key residues in the primary binding site, while functional studies confirmed client proteins failed to bind this variant of 14‐3‐3. But, in contrast to other client‐binding deficient variants, it did not localize to the nucleus. The 1.9 Å resolution structure of 14‐3‐3 nitrated at Y213 revealed unusual flexibility of its C‐terminal α‐helix resulting in domain swapping, suggesting additional structural plasticity though its relevance is not clear as this nitrated form retained its ability to bind clients. Collectively, our data suggest that nitration of 14‐3‐3 will alter downstream signaling systems, and if uncontrolled could result in global dysregulation of the 14‐3‐3 interactome. PDB Code(s): 8EQ8 and 8EQH ; 14-3-3 proteins are central hub regulators of hundreds of phosphorylated "client" proteins. They are subject to over 60 post-translational modifications (PTMs), yet little is known how these PTMs alter 14-3-3 function and its ability to regulate downstream signaling pathways. An often neglected, but well-documented 14-3-3 PTM found under physiological and immune-stimulatory conditions is the conversion of tyrosine to 3-nitro-tyrosine at several Tyr sites, two of which are located at sites considered important for 14-3-3 function: Y130 (β-isoform numbering) is located in the primary phospho-client peptide-binding groove, while Y213 is found on a secondary binding site that engages with clients for full 14-3-3/client complex formation and client regulation. By genetically encoding 3-nitro-tyrosine, we sought to understand if nitration at Y130 and Y213 effectively modulated 14-3-3 structure, function, and client complexation. The 1.5 Å resolution crystal structure of 14-3-3 nitrated at Y130 showed the nitro group altered the conformation of key residues in the primary binding site, while functional studies confirmed client proteins failed to bind this variant of 14-3-3. But, in contrast to other client-binding deficient variants, it did not localize to the nucleus. The 1.9 Å resolution structure of 14-3-3 nitrated at Y213 revealed unusual flexibility of its C-terminal α-helix resulting in domain swapping, suggesting additional structural plasticity though its relevance is not clear as this nitrated form retained its ability to bind clients. Collectively, our data suggest that nitration of 14-3-3 will alter downstream signaling systems, and if uncontrolled could result in global dysregulation of the 14-3-3 interactome. 14‐3‐3 proteins are central hub regulators of hundreds of phosphorylated “client” proteins. They are subject to over 60 post‐translational modifications (PTMs), yet little is known how these PTMs alter 14‐3‐3 function and its ability to regulate downstream signaling pathways. An often neglected, but well‐documented 14‐3‐3 PTM found under physiological and immune‐stimulatory conditions is the conversion of tyrosine to 3‐nitro‐tyrosine at several Tyr sites, two of which are located at sites considered important for 14‐3‐3 function: Y130 (β‐isoform numbering) is located in the primary phospho‐client peptide‐binding groove, while Y213 is found on a secondary binding site that engages with clients for full 14‐3‐3/client complex formation and client regulation. By genetically encoding 3‐nitro‐tyrosine, we sought to understand if nitration at Y130 and Y213 effectively modulated 14‐3‐3 structure, function, and client complexation. The 1.5 Å resolution crystal structure of 14‐3‐3 nitrated at Y130 showed the nitro group altered the conformation of key residues in the primary binding site, while functional studies confirmed client proteins failed to bind this variant of 14‐3‐3. But, in contrast to other client‐binding deficient variants, it did not localize to the nucleus. The 1.9 Å resolution structure of 14‐3‐3 nitrated at Y213 revealed unusual flexibility of its C‐terminal α‐helix resulting in domain swapping, suggesting additional structural plasticity though its relevance is not clear as this nitrated form retained its ability to bind clients. Collectively, our data suggest that nitration of 14‐3‐3 will alter downstream signaling systems, and if uncontrolled could result in global dysregulation of the 14‐3‐3 interactome. Abstract 14‐3‐3 proteins are central hub regulators of hundreds of phosphorylated “client” proteins. They are subject to over 60 post‐translational modifications (PTMs), yet little is known how these PTMs alter 14‐3‐3 function and its ability to regulate downstream signaling pathways. An often neglected, but well‐documented 14‐3‐3 PTM found under physiological and immune‐stimulatory conditions is the conversion of tyrosine to 3‐nitro‐tyrosine at several Tyr sites, two of which are located at sites considered important for 14‐3‐3 function: Y130 (β‐isoform numbering) is located in the primary phospho‐client peptide‐binding groove, while Y213 is found on a secondary binding site that engages with clients for full 14‐3‐3/client complex formation and client regulation. By genetically encoding 3‐nitro‐tyrosine, we sought to understand if nitration at Y130 and Y213 effectively modulated 14‐3‐3 structure, function, and client complexation. The 1.5 Å resolution crystal structure of 14‐3‐3 nitrated at Y130 showed the nitro group altered the conformation of key residues in the primary binding site, while functional studies confirmed client proteins failed to bind this variant of 14‐3‐3. But, in contrast to other client‐binding deficient variants, it did not localize to the nucleus. The 1.9 Å resolution structure of 14‐3‐3 nitrated at Y213 revealed unusual flexibility of its C‐terminal α‐helix resulting in domain swapping, suggesting additional structural plasticity though its relevance is not clear as this nitrated form retained its ability to bind clients. Collectively, our data suggest that nitration of 14‐3‐3 will alter downstream signaling systems, and if uncontrolled could result in global dysregulation of the 14‐3‐3 interactome. Abstract 14‐3‐3 proteins are central hub regulators of hundreds of phosphorylated “client” proteins. They are subject to over 60 post‐translational modifications (PTMs), yet little is known how these PTMs alter 14‐3‐3 function and its ability to regulate downstream signaling pathways. An often neglected, but well‐documented 14‐3‐3 PTM found under physiological and immune‐stimulatory conditions is the conversion of tyrosine to 3‐nitro‐tyrosine at several Tyr sites, two of which are located at sites considered important for 14‐3‐3 function: Y130 (β‐isoform numbering) is located in the primary phospho‐client peptide‐binding groove, while Y213 is found on a secondary binding site that engages with clients for full 14‐3‐3/client complex formation and client regulation. By genetically encoding 3‐nitro‐tyrosine, we sought to understand if nitration at Y130 and Y213 effectively modulated 14‐3‐3 structure, function, and client complexation. The 1.5 Å resolution crystal structure of 14‐3‐3 nitrated at Y130 showed the nitro group altered the conformation of key residues in the primary binding site, while functional studies confirmed client proteins failed to bind this variant of 14‐3‐3. But, in contrast to other client‐binding deficient variants, it did not localize to the nucleus. The 1.9 Å resolution structure of 14‐3‐3 nitrated at Y213 revealed unusual flexibility of its C‐terminal α‐helix resulting in domain swapping, suggesting additional structural plasticity though its relevance is not clear as this nitrated form retained its ability to bind clients. Collectively, our data suggest that nitration of 14‐3‐3 will alter downstream signaling systems, and if uncontrolled could result in global dysregulation of the 14‐3‐3 interactome. PDB Code(s): 8EQ8 and 8EQH ; |
| Author | Estelle, Aidan B. Sluchanko, Nikolai N. Zhu, Phillip Nguyen, Kyle T. Mehl, Ryan A. Cooley, Richard B. |
| AuthorAffiliation | 1 Department of Biochemistry and Biophysics, 2011 Agricultural and Life Sciences Oregon State University Corvallis Oregon USA 2 Federal Research Center of Biotechnology of the Russian Academy of Sciences A.N. Bach Institute of Biochemistry Moscow Russia |
| AuthorAffiliation_xml | – name: 2 Federal Research Center of Biotechnology of the Russian Academy of Sciences A.N. Bach Institute of Biochemistry Moscow Russia – name: 1 Department of Biochemistry and Biophysics, 2011 Agricultural and Life Sciences Oregon State University Corvallis Oregon USA |
| Author_xml | – sequence: 1 givenname: Phillip orcidid: 0000-0002-9756-2637 surname: Zhu fullname: Zhu, Phillip organization: Oregon State University – sequence: 2 givenname: Kyle T. surname: Nguyen fullname: Nguyen, Kyle T. organization: Oregon State University – sequence: 3 givenname: Aidan B. surname: Estelle fullname: Estelle, Aidan B. organization: Oregon State University – sequence: 4 givenname: Nikolai N. orcidid: 0000-0002-8608-1416 surname: Sluchanko fullname: Sluchanko, Nikolai N. organization: A.N. Bach Institute of Biochemistry – sequence: 5 givenname: Ryan A. surname: Mehl fullname: Mehl, Ryan A. email: ryan.mehl@oregonstate.edu organization: Oregon State University – sequence: 6 givenname: Richard B. surname: Cooley fullname: Cooley, Richard B. email: rick.cooley@oregonstate.edu organization: Oregon State University |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/36691781$$D View this record in MEDLINE/PubMed https://www.osti.gov/biblio/1924571$$D View this record in Osti.gov |
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| Keywords | 14-3-3 nitration 3-nitrotyrosine genetic code expansion phosphorylation oxidative stress protein-protein interactions |
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| Snippet | 14‐3‐3 proteins are central hub regulators of hundreds of phosphorylated “client” proteins. They are subject to over 60 post‐translational modifications... 14-3-3 proteins are central hub regulators of hundreds of phosphorylated "client" proteins. They are subject to over 60 post-translational modifications... Abstract 14‐3‐3 proteins are central hub regulators of hundreds of phosphorylated “client” proteins. They are subject to over 60 post‐translational... |
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| SubjectTerms | 14‐3‐3 3‐nitrotyrosine Binding sites Clients Complex formation Conformation Crystal structure Dephosphorylation Full‐length Paper Full‐length Papers genetic code expansion Grooves Humans Nitrates - chemistry Nitrates - metabolism Nitration Oxidative stress phosphorylation Proteins Proteins - chemistry protein–protein interactions Signalling systems Structure-function relationships Tyrosine Tyrosine - chemistry |
| Title | Genetic encoding of 3‐nitro‐tyrosine reveals the impacts of 14‐3‐3 nitration on client binding and dephosphorylation |
| URI | https://onlinelibrary.wiley.com/doi/abs/10.1002%2Fpro.4574 https://www.ncbi.nlm.nih.gov/pubmed/36691781 https://www.proquest.com/docview/2780014641 https://www.proquest.com/docview/2769375858/abstract/ https://www.osti.gov/biblio/1924571 https://pubmed.ncbi.nlm.nih.gov/PMC9926477 |
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