Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1 Journal Article
| Authors: | Cappadocia, L.; Mascle, X. H.; Bourdeau, V.; Tremblay-Belzile, S.; Chaker-Margot, M.; Lussier-Price, M.; Wada, J.; Sakaguchi, K.; Aubry, M.; Ferbeyre, G.; Omichinski, J. G. |
| Article Title: | Structural and functional characterization of the phosphorylation-dependent interaction between PML and SUMO1 |
| Abstract: | PML and several other proteins localizing in PML-nuclear bodies (PML-NB) contain phosphoSIMs (SUMO-interacting motifs), and phosphorylation of this motif plays a key role in their interaction with SUMO family proteins. We examined the role that phosphorylation plays in the binding of the phosphoSIMs of PML and Daxx to SUMO1 at the atomic level. The crystal structures of SUMO1 bound to unphosphorylated and tetraphosphorylated PML-SIM peptides indicate that three phosphoserines directly contact specific positively charged residues of SUMO1. Surprisingly, the crystal structure of SUMO1 bound to a diphosphorylated Daxx-SIM peptide indicate that the hydrophobic residues of the phosphoSIM bind in a manner similar to that seen with PML, but important differences are observed when comparing the phosphorylated residues. Together, the results provide an atomic level description of how specific acetylation patterns within different SUMO family proteins can work together with phosphorylation of phosphoSIM's regions of target proteins to regulate binding specificity. |
| Keywords: | signal transduction; mitogen activated protein kinase; controlled study; unclassified drug; nonhuman; protein function; mouse; animal tissue; protein depletion; fluorescent dye; animal experiment; animal model; enzyme activation; morphology; regulatory mechanism; nerve fiber; adenosine triphosphate; homeostasis; energy; adaptor protein; nerve fiber degeneration; mitogen activated protein kinase kinase 4; priority journal; article; sarm1 protein; axonal injury |
| Journal Title: | Structure |
| Volume: | 23 |
| Issue: | 1 |
| ISSN: | 0969-2126 |
| Publisher: | Cell Press |
| Date Published: | 2015-01-06 |
| Start Page: | 126 |
| End Page: | 138 |
| Language: | English |
| DOI: | 10.1016/j.str.2014.10.015 |
| PROVIDER: | scopus |
| PUBMED: | 25497731 |
| DOI/URL: | |
| Notes: | Export Date: 2 February 2015 -- Source: Scopus |
