1rk8
From Proteopedia
Structure of the cytosolic protein PYM bound to the Mago-Y14 core of the exon junction complex
Structural highlights
Function[RBM8A_DROME] Involved in mRNA quality control via the nonsense-mediated mRNA decay (NMD) pathway. Also involved in localization of osk (oskar) mRNA in the posterior pole of oocytes via its interaction with mago.[1] [2] [WIBG_DROME] Regulator of the exon junction complex (EJC), a multiprotein complex that associates immediately upstream of the exon-exon junction on mRNAs and serves as a positional landmarks for the intron exon structure of genes and directs post-transcriptional processes in the cytoplasm such as mRNA export, nonsense-mediated mRNA decay (NMD) or translation. [MGN_DROME] Participates in the bidirectional intercellular signaling between the posterior follicle cells and oocyte to establish spatial coordinates that induces axis formation. Complex with tsu is essential for cytoplasmic localization of oskar in the posterior pole of oocytes. Required for the polarization of the oocyte microtubule cytoskeleton.[3] [4] [5] [6] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe exon junction complex (EJC) is deposited on mRNAs as a consequence of splicing and influences postsplicing mRNA metabolism. The Mago-Y14 heterodimer is a core component of the EJC. Recently, the protein PYM has been identified as an interacting partner of Mago-Y14. Here we show that PYM is a cytoplasmic RNA-binding protein that is excluded from the nucleus by Crm1. PYM interacts directly with Mago-Y14 by means of its N-terminal domain. The crystal structure of the Drosophila ternary complex at 1.9 A resolution reveals that PYM binds Mago and Y14 simultaneously, capping their heterodimerization interface at conserved surface residues. Formation of this ternary complex is also observed with the human proteins. Mago residues involved in the interaction with PYM have been implicated in nonsense-mediated mRNA decay (NMD). Consistently, human PYM is active in NMD tethering assays. Together, these data suggest a role for PYM in NMD. Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex.,Bono F, Ebert J, Unterholzner L, Guttler T, Izaurralde E, Conti E EMBO Rep. 2004 Mar;5(3):304-10. Epub 2004 Feb 13. PMID:14968132[7] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Drome | Large Structures | Bono, F | Conti, E | Ebert, J | Guettler, T | Izaurralde, E | Mrna processing | Nmd | Oskar mrna localization | Rbd | Rrm | Translation
