Eukaryotic Cytoskeleton In Cell Division

Cell division is a highly regulated process requiring the interplay of physical and chemical cues. The cytoskeleton is a central player, serving as energy source for dramatic movements requiring complex mechano-chemistry, as well as acting as a scaffold that facilitates molecular encounters at the right time and place within the cell. We study two cytoskeletal systems, microtubules (MTs) and septin filaments, that play critical roles in mitosis and cytokinesis, respectively. Importantly, their self-assembly and interactions can serve both as input or readout in checkpoint processes that regulate critical and often irreversible steps in cell division progression.

Structural Basis of Microtubule Dynamic Instability

In our microtubule cytoskeleton studies we are interested in defining the conformational landscape of tubulin as defined by its nucleotide and assembly states, in order to obtain detail mechanistic understanding of the process of microtubule dynamic instability ... read more


Microtubule-Kinetochore Interface

In the cell the dynamics of microtubules are regulated and made use of by their interaction with different factors. Of special interest is the coupling of microtubules to the kinetochore, a process where microtubule dynamics reaches its "climax". We pursue a mechanistic understanding of the molecular interactions governing the regulated, dynamic attachment of kinetochores to microtubules that underlies the accurate segregation of chromosomes during mitosis ... read more


Septins Structure And Assembly

Septins are conserved GTases defining a new type of cytoskeletal filaments essential in cytokinesis and other membrane-remodeling processes. We are studying the yeast septins to define the organization of different septin assembly units, their polymerization and their regulation ... read more



Recent publications

Liu JJ et al. <a href=https://www.nature.com/articles/s41586-019-0908-x> CasX enzymes comprise a distinct family of RNA-guided genome editors </a> Nature 2019 Feb 04 Patel et al. <a href=http://science.sciencemag.org/content/early/2018/11/14/science.aau8872> Structure of human TFIID and mechanism of TBP loading onto promoter DNA </a> Science 2018 Nov 15 Kellogg et al. <a href=http://science.sciencemag.org/content/early/2018/05/09/science.aat1780?rss=1> Near-atomic model of microtubule-tau interactions </a> Science 2018 May 10 Nguyen et al. <a href= https://www.nature.com/articles/s41586-018-0062-x>  Cryo-EM structure of substrate-bound human telomerase holoenzyme.
</a> Nature 2018 Apr 25 Poepsel et al. <a href=https://www.nature.com/articles/s41594-018-0023-y > Cryo-EM structures of PRC2 simultaneously engaged with two functionally distinct nucleosomes. </a> Nature Structural and Molecular Biology 2018 Jan 29 Kasinath et al. <a href=http://science.sciencemag.org/content/early/2018/01/17/science.aar5700 > Structures of human PRC2 with its cofactors AEBP2 and JARID2. </a> Science 2018 Jan 18 Haloupek et al. <a href=http://science.sciencemag.org/content/358/6365/888 > The structural basis of flagellin detection by NAIP5: a strategy to limit pathogen immune evasion. </a> Science 2017 Nov 17 Zhang et al. <a href=https://elifesciences.org/articles/30959 > Structural Insight into TPX2-Stimulated Microtubule Assembly.</a> Elife 2017 Nov 9 Greber et al.  <a href=https://www.ncbi.nlm.nih.gov/pubmed/28902838\ > The cryo-electron microscopy structure of human transcription factor IIH. </a><i> Nature </i>, 2017 Sep 21;549(7672):414-417 Wright AV, Liu JJ et al. <a  href=https://www.ncbi.nlm.nih.gov/pubmed/28729350\ > Structures of the CRISPR genome integration complex. </a>
Science 2017 Sep 15 Kellogg et al. <a href=http://www.sciencedirect.com/science/article/pii/S0022283617300153\> Insights into the Distinct Mechanisms of Action of Taxane and Non-Taxane Microtubule Stabilizers from Cryo-EM Structures</a><i> Journal of Molecular Biology</i>, 2017 Mar 10 He et al. <a href=https://www.ncbi.nlm.nih.gov/pubmed/27193682\> Near-atomic resolution visualization of human transcription promoter opening</a><i> Nature</i>, 2016 May 11 Louder et al. <a href=http://www.ncbi.nlm.nih.gov/pubmed/27007846> Structure of promoter-bound TFIID and model of human pre-initiation complex assembly</a><i> Nature</i>, 2016 Mar 23;531(7596):604-9 Jiang and Taylor et al. <a href=http://www.ncbi.nlm.nih.gov/pubmed/26841432> Structures of a CRISPR-Cas9 R-loop complex primed for DNA cleavage.</a> <i>Science</i>, Jan 2016 Nogales and Zhang<a href=http://www.sciencedirect.com/science/article/pii/S0959440X16000038> Visualizing microtubule structural transitions and interactions with associated proteins</a> <i>COSB</i>, April 2016; <b>37</b>, 90-96 Zhang et al. <a href=http://www.sciencedirect.com/science/article/pii/S0092867415008491> Mechanistic origin of microtubule dynamic instability and its modulation by EB proteins</a><i> Cell 2015 Aug 13;162(4):849-59

Eva Nogales Named a 2020 Biophysical Society Fellow EMBO

Lab Member, Vignesh Kasinath has been awarded the the NIH Pathway to Independence (K99) award

Lab Member, Kelly Nguyen , will be starting as a Group Leader at the MRC-Laboratory of Molecular Biology in Cambridge, UK in August 2019

Lab member, Simon Poepsel, has started an Independent Research Group at the Center for Molecular Medicine at the University of Cologne, Germany in June 2019

Eva Nogales is the 2019 recipient of the Grimwade Medal

Eva Nogales talks about CryoEM in Molecules in Motion podcast