ribosome assembly; nuclear import; nuclear transport; RanGTP, Crm1, Slx9
Olombrada Miriam, Peña Cohue, Rodríguez-Galán Olga, Klingauf-Nerurkar Purnima, Portugal-Calisto Daniela, Oborská-Oplová Michaela, Altvater Martin, Gavilanes José G, Martínez-del-Pozo Álvaro, de la Cruz Jesús, García-Ortega Lucía, Panse Vikram Govind (2020), The ribotoxin α-sarcin can cleave the sarcin/ricin loop on late 60S pre-ribosomes, in Nucleic Acids Research
, 48(11), 6210-6222.
Swart A. Leoni, Steiner Bernhard, Gomez-Valero Laura, Schütz Sabina, Hannemann Mandy, Janning Petra, Irminger Michael, Rothmeier Eva, Buchrieser Carmen, Itzen Aymelt, Panse Vikram Govind, Hilbi Hubert (2020), Divergent Evolution of Legionella RCC1 Repeat Effectors Defines the Range of Ran GTPase Cycle Targets, in mBio
, 11(2), 1-14.
Klingauf-Nerurkar Purnima, Gillet Ludovic C, Portugal-Calisto Daniela, Oborská-Oplová Michaela, Jäger Martin, Schubert Olga T, Pisano Agnese, Peña Cohue, Rao Sanjana, Altvater Martin, Chang Yiming, Aebersold Ruedi, Panse Vikram G (2020), The GTPase Nog1 co-ordinates the assembly, maturation and quality control of distant ribosomal functional centers, in eLife
, 9, 1-25.
Strumillo Marta J., Oplová Michaela, Viéitez Cristina, Ochoa David, Shahraz Mohammed, Busby Bede P., Sopko Richelle, Studer Romain A., Perrimon Norbert, Panse Vikram G., Beltrao Pedro (2019), Conserved phosphorylation hotspots in eukaryotic protein domain families, in Nature Communications
, 10(1), 1977-1977.
Panasenko Olesya O., Somasekharan Syam Prakash, Villanyi Zoltan, Zagatti Marina, Bezrukov Fedor, Rashpa Ravish, Cornut Julien, Iqbal Jawad, Longis Marion, Carl Sarah H., Peña Cohue, Panse Vikram G., Collart Martine A. (2019), Co-translational assembly of proteasome subunits in NOT1-containing assemblysomes, in Nature Structural & Molecular Biology
, 26(2), 110-120.
Schütz Sabina, Michel Erich, Damberger Fred F., Oplová Michaela, Peña Cohue, Leitner Alexander, Aebersold Ruedi, Allain Frederic H.-T., Panse Vikram Govind (2018), Molecular basis for disassembly of an importin:ribosomal protein complex by the escortin Tsr2, in Nature Communications
, 9(1), 3669-3669.
Khajuria Rajiv K., Munschauer Mathias, Ulirsch Jacob C., Fiorini Claudia, Ludwig Leif S., McFarland Sean K., Abdulhay Nour J., Specht Harrison, Keshishian Hasmik, Mani D.R., Jovanovic Marko, Ellis Steven R., Fulco Charles P., Engreitz Jesse M., Schütz Sabina, Lian John, Gripp Karen W., Weinberg Olga K., Pinkus Geraldine S., Gehrke Lee, Regev Aviv, Lander Eric S., Gazda Hanna T., Lee Winston Y., et al. (2018), Ribosome Levels Selectively Regulate Translation and Lineage Commitment in Human Hematopoiesis, in Cell
, 173(1), 90-103.e19.
Scaiola Alain, Peña Cohue, Weisser Melanie, Böhringer Daniel, Leibundgut Marc, Klingauf‐Nerurkar Purnima, Gerhardy Stefan, Panse Vikram Govind, Ban Nenad (2018), Structure of a eukaryotic cytoplasmic pre‐40S ribosomal subunit, in The EMBO Journal
, 37(7), 1-10.
Peña Cohue, Hurt Ed, Panse Vikram Govind (2017), Eukaryotic ribosome assembly, transport and quality control, in Nature Structural & Molecular Biology
, 24(9), 689-699.
Peña Cohue, Schütz Sabina, Fischer Ute, Chang Yiming, Panse Vikram G (2016), Prefabrication of a ribosomal protein subcomplex essential for eukaryotic ribosome formation, in eLife
, 5, 1-24.
Error-free translation of the genetic code to proteins is key to cellular growth and proliferation. This essential task is carried out by the ribosome. While the structure of the mature ribosome is giving insights into the mechanics of translation, our knowledge regarding the assembly, quality control and cellular targeting of this universal machine is emerging. Eukaryotic ribosome assembly is a spectacular example of a highly dynamic and regulated process that stretches across different cellular territories: the nucleolus, nucleoplasm and the cytoplasm. This poorly understood process, which begins in the nucleolus, requires >300 conserved transiently associating assembly factors, whose site(s) of action and function(s) on maturing pre-ribosomal particles are beginning to be elucidated. Eukaryotic ribosome assembly also relies on efficient nucleocytoplasmic transport. In the model organism budding yeast, the import machinery delivers ~140,000 ribosomal proteins every minute to the nucleus for ribosome assembly. Within the same time, the export machinery facilitates translocation of ~2000 pre-ribosomal particles every minute through ~200 nuclear pore complexes into the cytoplasm. By exploiting the genetically tractable organism budding yeast, in combination with biochemical and structural biology approaches, we will uncover:(1) Mechanisms by which ribosomal proteins are precisely targeted to their rRNA binding site on assembling pre-ribosomal particles in the nucleolus. (2) Mechanisms by which pre-ribosomal particles are prepared for transport through nuclear pore complexes. Our analyses will shed light on how the nucleocytoplasmic transport machinery, the ribosome assembly pathway and the quality control machinery co-ordinate their activities to commit functional ribosomes for translation.