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The conserved ubiquitin-like protein Hub1 plays a critical role in splicing in human cells

Journal of Molecular Cell Biology 2014年第4期8卷 312-323页

作者： Tim Ammon Shravan Kumar Mishra Kaja Kowalska Grzegorz M. Popowicz Tad A. Holak Stefan Jentsch Department of Molecular Cell Biology Max Planck Institute of Biochemistry Am Klopferspitz 18 82152 Martinsried Germany NMR Spectroscopy Max Planck Institute of Biochemistry Am Klopferspitz 18 82152 Martinsried Germany Department of Biological Sciences Indian Institute of Science Education and Research (IISER) Mohali Knowledge City Sector 81 SAS Nagar 140306 Punjab India Institute of Structural Biology Helmholtz Zentrum MLinchen Ingolst~idter Landstrasse 1 85764 Neuherberg Germany Faculty of Chemistry Jagiellonian University Ingardena 3 30-060 Cracow Poland

Different from canonical ubiquitin-like proteins, Hub1 does not form covalent conjugates with substrates but binds proteins noncovalently. In Socchoromyces cerevisioe, Hub1 associates with spUceosomes and mediates alternative splicing of SRCI, without affecting pre-mRNA splicing generaity. Human Hub1 is highty similar to its yeast homotog, but its cellular function remains largely unexplored. Here, we show that human Hub1 binds to the spliceosomal protein Snu66 as in yeast; however, unlike its 5. cerevisioe homolos, human Hub1 is essential for viability. Prolonged in vivo depletion of human Hub1 leads to various cellular defects, including splicing speckle abnormalities, partial nuclear retention of mRNAs, mitotic catastrophe, and consequently cell death by apoptosis. Early consequences of Hub1 depletion are severe splicing defects, however, only for specific splice sites leading to exon skipping and intron retention. Thus, the ubiquitin-iike protein Hub1 is not a canonlcal spliceosomal factor needed generally for splicing, but rather a modulator of spliceosome performance and facilitator of alternative splicing.

关键词： apoptosis hubl splicing spliceosome ubiquitin-like proteins

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