2n1o › Citations

Structural Analysis of the Pin1-CPEB1 interaction and its potential role in CPEB1 degradation.

<div class='caption-title'>Phosphorylation independent interaction of CPEB1 and Pin1 WW.</div>
<div class='caption-title'>CPEB1 pS210 and pS184 are the preferred Pin1 binding sites.</div>
<div class='caption-title'>Characterization of the phosphorylation dependent CPEB1-Pin1 interaction by NMR.</div>
Schelhorn C, Martín-Malpartida P, Suñol D, Macias MJ
OpenAccess logo Sci Rep 5 14990 (2015)
Cited: 11 times
EuropePMC logo PMID: 26456073

Abstract

The Cytoplasmic Polyadenylation Element Binding proteins are RNA binding proteins involved in the translational regulation of mRNA. During cell cycle progression, CPEB1 is labeled for degradation by phosphorylation-dependent ubiquitination by the SCF(β-TrCP) ligase. The peptidyl-prolyl isomerase Pin1 plays a key role in CPEB1 degradation. Conditioned by the cell cycle stage, CPEB1 and Pin1 interactions occur in a phosphorylation-independent or -dependent manner. CPEB1 contains six potential phosphorylatable Pin1 binding sites. Using a set of biophysical techniques, we discovered that the pS210 site is unique, since it displays binding activity not only to the WW domain but also to the prolyl-isomerase domain of Pin1. The NMR structure of the Pin1 WW-CPEB1 pS210 (PDB ID: 2n1o) reveals that the pSerPro motif is bound in trans configuration through contacts with amino acids located in the first turn of the WW domain and the conserved tryptophan in the β3-strand. NMR relaxation analyses of Pin1 suggest that inter-domain flexibility is conferred by the modulation of the interaction with peptides containing the pS210 site, which is essential for degradation.

Articles - 2n1o mentioned but not cited (3)

  1. Coordination of the Copper Centers in Particulate Methane Monooxygenase: Comparison between Methanotrophs and Characterization of the CuC Site by EPR and ENDOR Spectroscopies. Jodts RJ, Ross MO, Koo CW, Doan PE, Rosenzweig AC, Hoffman BM. J Am Chem Soc 143 15358-15368 (2021)
  2. Systematic domain-based aggregation of protein structures highlights DNA-, RNA- and other ligand-binding positions. Kobren SN, Singh M. Nucleic Acids Res 47 582-593 (2019)
  3. Structural Analysis of the Pin1-CPEB1 interaction and its potential role in CPEB1 degradation. Schelhorn C, Martín-Malpartida P, Suñol D, Macias MJ. Sci Rep 5 14990 (2015)


Reviews citing this publication (2)

  1. Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs. Kliche J, Ivarsson Y. Biochem J 479 1-22 (2022)
  2. Molecular Mechanisms of Parathyroid Disorders in Chronic Kidney Disease. Hassan A, Khalaily N, Kilav-Levin R, Nechama M, Volovelsky O, Silver J, Naveh-Many T. Metabolites 12 111 (2022)

Articles citing this publication (6)

  1. Activity-dependent isomerization of Kv4.2 by Pin1 regulates cognitive flexibility. Hu JH, Malloy C, Tabor GT, Gutzmann JJ, Liu Y, Abebe D, Karlsson RM, Durell S, Cameron HA, Hoffman DA. Nat Commun 11 1567 (2020)
  2. Phosphorylation Dynamics Dominate the Regulated Proteome during Early Xenopus Development. Peuchen EH, Cox OF, Sun L, Hebert AS, Coon JJ, Champion MM, Dovichi NJ, Huber PW. Sci Rep 7 15647 (2017)
  3. Structural and cellular mechanisms of peptidyl-prolyl isomerase Pin1-mediated enhancement of Tissue Factor gene expression, protein half-life, and pro-coagulant activity. Kurakula K, Koenis DS, Herzik MA, Liu Y, Craft JW, van Loenen PB, Vos M, Tran MK, Versteeg HH, Goumans MTH, Ruf W, de Vries CJM, Şen M. Haematologica 103 1073-1082 (2018)
  4. Changes in the folding landscape of the WW domain provide a molecular mechanism for an inherited genetic syndrome. Pucheta-Martinez E, D'Amelio N, Lelli M, Martinez-Torrecuadrada JL, Sudol M, Saladino G, Gervasio FL. Sci Rep 6 30293 (2016)
  5. Molecular Mechanism of the Pin1-Histone H1 Interaction. Jinasena D, Simmons R, Gyamfi H, Fitzkee NC. Biochemistry 58 788-798 (2019)
  6. Identification of novel functional mini-receptors by combinatorial screening of split-WW domains. Neitz H, Paul NB, Häge FR, Lindner C, Graebner R, Kovermann M, Thomas F. Chem Sci 13 9079-9090 (2022)


Quick links