The nuclear basket proteins Mlp1p and Mlp2p are part of a dynamic interactome including Esc1p and the proteasome
Molloy, Kelly R.
Farr, Julia C.
Meinema, Anne C.
Cristea, Ileana M.
Chait, Brian T.
Rout, Michael P.
UMass Chan AffiliationsProgram in Molecular Medicine
Keywordsnuclear pore complex
Amino Acids, Peptides, and Proteins
Biochemistry, Biophysics, and Structural Biology
Enzymes and Coenzymes
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AbstractThe basket of the nuclear pore complex (NPC) is generally depicted as a discrete structure of eight protein filaments that protrude into the nucleoplasm and converge in a ring distal to the NPC. We show that the yeast proteins Mlp1p and Mlp2p are necessary components of the nuclear basket and that they also embed the NPC within a dynamic protein network, whose extended interactome includes the spindle organizer, silencing factors, the proteasome, and key components of messenger ribonucleoproteins (mRNPs). Ultrastructural observations indicate that the basket reduces chromatin crowding around the central transporter of the NPC and might function as a docking site for mRNP during nuclear export. In addition, we show that the Mlps contribute to NPC positioning, nuclear stability, and nuclear envelope morphology. Our results suggest that the Mlps are multifunctional proteins linking the nuclear transport channel to multiple macromolecular complexes involved in the regulation of gene expression and chromatin maintenance.
Niepel M, Molloy KR, Williams R, Farr JC, Meinema AC, Vecchietti N, Cristea IM, Chait BT, Rout MP, Strambio-De-Castillia C. The nuclear basket proteins Mlp1p and Mlp2p are part of a dynamic interactome including Esc1p and the proteasome. Mol Biol Cell. 2013 Dec;24(24):3920-38. doi: 10.1091/mbc.E13-07-0412. Epub 2013 Oct 23. PMID: 24152732; PMCID: PMC3861087. Link to article on publisher's site