Symposium Review

The14th CRG sympossium took place on the 22nd-23rd of October at the PRBB auditorium CRG. The sympossium featured talks of 19 speakers from some of the most important science centers of the world, and it was distributed in 4 sessions, dedicated to topics related to Cellular Machineries.

Both attendees and speakers expressed the value that had for them to attend the symposium, concluding that it was a great place for networking, meeting with old colleagues or making new acquiantances, and overall be updated on new discoveries and interesting information on their fields.

First day’s session was about Mechanochemistry of Cell Biology, and included talks about reconstruction of mitotic spindle organization by speaker Marileen Dogterom (Delf University of Technology, NL), tweaking cartwheel and centriole symmetry by Michel Steinmetz (Paul Scherrer Institute, CH), ER organization at increased resolution, by Jenniffer Lippincot-Schwartz (Eunice Kennedy Shriver National Institute of Child, US) Induction of cellular invasion from centrosome amplification, by Susana Godinho (Barts Cancer Institute, UK) and short talks by Julia Von Blume, about cargo sorting during protein secretion (CRG Alumni, Max Planck, DE) and Eli Zamir, about building blocks and assembly of cell adhesion machineries (Max Planck, DE)

In the afternoon Session 2 about Morphogensis and cytoskeleton counted with 4 talks, Actin cortex mechanics in animal cell morphogenesis, by Eva Paluch (UCL, UK), radial Cell intercalations in zebrafish gastrulation, by Carl Philipp Heisenberg (Institute of Science and Technology, AT), Control of intracellular forces and cancer cell invasion by the adhesome, by Xavier Trepat (Institute of Bioengineering of Catalonia) and last talk of the day by Anna Akhmanova, on Mycrotubule dynamics (UtrechtUniversity, NL)

By the end of Session 1, it was time for poster session, exposed outside the Auditorium building, that counted with 25 different posters from centers all over the world, on Cellular Machineries.

Day 2′s Session 3, Nuclear Organization, had no less interesting talks, starting with Manuel Mendoza ,CRG researcher and organizer of the symposium, on Modulation of gene repositioning controlling cell cycle entry, and was followed by speakers Camilla Sjögren (Karolinska Institutet, SE) on SMC protein complexes and Ulrike Kutay (ETH Zurich, CH) on Taking apart nuclear envelope during Open Mitosis. Two shorts talks closed the morning session, Gabriel Neurohr (CRG Alumni, MIT, US) about cell size limiting cell proliferation in yeast and Danny Nedialkova (Max Planck, DE) about optimization of codon translation rates maintaining proteome integrity.

Last Session of the Symposium, had 4 researchers speaking about Proteostasis: Protein folding homeostasis in the endoplasmatic reticulum by David Ron (University of Cambridge, UK), Autophagy machinery and role in suppression of diseases, by Tamotsu Yoshimori (Osaka University, JP), Proteasis impairment in protein misfolding and aggregation diseases, by Mark Hipp (Max Planck, DE) and Structure and function of an Escrt-III filament, by Wes Sundquist (University of Utah School of Medicine, US).

The 14th CRG Sympossium finished with the closing remarks of organizer Vivek Malhotra, inviting everybody to come back soon to Barcelona and the CRG, and expressing his admiration for both speakers and current PhD students attending the Sympossium.

You can now review, or watch for the first time, if you were not there, some of the talks in the VIDEOS section of the web, and feel free to let us know your thoughts on this year symposium on social Media. You can find us on FACEBOOK and TWITTER.

Optimization of Codon translation rates via tRNA modifications maintains proteome integrity

Session 3 of the 14^th CRG Sympossium features, among others,  Danny NEDIALKOVA from the Max Planck Institute for Molecular Biomedicine, Max Planck Research Group for RNA Biology, from Münster DE, presenting a short talk about how optimization of codon translation rates via tRNA modifications maintains proteome integrity.  

- Codon translation speed can impact protein folding and tRNA modifications stabilize codon-anticodon pairing

- U34 (wobble modified codon) modifications are required for fitness. They studied how modified U34 enhances codon translation rates in vivo:

• Elevated tRNA levels restores cellular fitness.

• U34 modifications promote efficient decoding in yeast and maintain protein homeostasis, while loss of them triggers proteotoxic stress and elicits proteins aggregation

• Metastable proteins aggregate in cells with unmodified U34 while elevated tRNA levels restore protein homeostasis

• U34 modifications  promote efficient decoding in metazoans while U34 modification loss impairs proteostasis in metazoans, and triggers protein homeostasis failure

Resolving the building blocks and assembly principles of cell adhesion machineries

Short Talk by Eli ZAMIR, from theDepartment of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Dortmund DE, about how  adhesion sites get self-assembled and function.

• Adhesion sites contain hundred different proteins called integrin adhesome. This proteins interact with each other, self-organizing as diverse adhesion sites with distinct properties
• Studies have been carried out about this self assembly, investigating the state of the integrin adhesome network in the cytosol and space and time relations with focal adhesions
• Using FCCS and FRAP measurements, it was found that cytosol complexes correlate with the internal organization: integrin adhesome is extensively pre-assembled in the cytosol, forming multi-protein building blocks for adhesion sites that are combinatorially diversified, and they correlate with the structural and functional organization of proteins across focal adhesions.
• Building blocks enter and exit this focal adhesions without being altered, preserving specifications and assembly logic. They are currently investigating the recruitment of specific multi-protein blocs to focal adhesions and its regulation to decipher this assembly logic.