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https://hdl.handle.net/2440/9538
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dc.contributor.author | Woodcock, J. | - |
dc.contributor.author | Murphy, J. | - |
dc.contributor.author | Stomski, F. | - |
dc.contributor.author | Berndt, M. | - |
dc.contributor.author | Lopez, A. | - |
dc.date.issued | 2003 | - |
dc.identifier.citation | Journal of Biological Chemistry, 2003; 278(38):36323-36327 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.issn | 1083-351X | - |
dc.identifier.uri | http://hdl.handle.net/2440/9538 | - |
dc.description.abstract | The 14-3-3 proteins play a central role in the regulation of cell growth, cycling, and apoptosis by modulating the functional activities of key signaling proteins. Through binding to a phosphoserine motif, 14-3-3 alters target proteins activities by sequestering them, relocalizing them, conformationally altering their functional activity, or by promoting interaction with other proteins. These functions of 14-3-3 are facilitated by, if not dependent on, its dimeric structure. We now show that the dimeric status of 14-3-3 is regulated by site-specific serine phosphorylation. We found that a sphingosine-dependent kinase phosphorylates 14-3-3 in vitro and in vivo on a serine residue (Ser58) located within the dimer interface. Furthermore, by developing an antibody that specifically recognizes 14-3-3zeta phosphorylated on Ser58 and employing native-PAGE and cross-linking techniques, we found that 14-3-3 phosphorylated on Ser58 is monomeric both in vitro and in vivo. Phosphorylated 14-3-3 was detected solely as a monomer, indicating that phosphorylation of a single monomer within a dimer is sufficient to disrupt the dimeric structure. Significantly, phosphorylation-induced monomerization did not prevent 14-3-3 binding to a phosphopeptide target. We propose that this regulated monomerization of 14-3-3 controls its ability to modulate the activity of target proteins and thus may have significant implications for 14-3-3 function and the regulation of many cellular processes. | - |
dc.description.statementofresponsibility | Joanna M. Woodcock, Jane Murphy, Frank C. Stomski, Michael C. Berndt, and Angel F. Lopez | - |
dc.language.iso | en | - |
dc.publisher | Amer Soc Biochemistry Molecular Biology Inc | - |
dc.source.uri | http://dx.doi.org/10.1074/jbc.m304689200 | - |
dc.subject | NIH 3T3 Cells | - |
dc.subject | Animals | - |
dc.subject | Mice, Inbred BALB C | - |
dc.subject | Rabbits | - |
dc.subject | Mice | - |
dc.subject | Tyrosine 3-Monooxygenase | - |
dc.subject | Serine | - |
dc.subject | 14-3-3 Proteins | - |
dc.subject | Recombinant Proteins | - |
dc.subject | Cross-Linking Reagents | - |
dc.subject | Immunoblotting | - |
dc.subject | Electrophoresis, Polyacrylamide Gel | - |
dc.subject | Signal Transduction | - |
dc.subject | Apoptosis | - |
dc.subject | Amino Acid Motifs | - |
dc.subject | Protein Conformation | - |
dc.subject | Protein Binding | - |
dc.subject | Dimerization | - |
dc.subject | Phosphorylation | - |
dc.title | The dimeric versus monomeric status of 14-3-3z is controlled by phosphorylation of Ser58 at the dimer interface | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1074/jbc.M304689200 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Lopez, A. [0000-0001-7430-0135] | - |
Appears in Collections: | Aurora harvest Medicine publications |
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