New publication from our lab! Can semiflexible polymers (lamin fibers, dsDNA, actin, etc) alter the shape of elastic shells or lipid vesicles? Indeed, the nematic/random ordering of these polymers on the surface could tune their shapes.
Read more on: pubs.rsc.org/en/content/a...

paper with @erbash.bsky.social now published in @narjournal.bsky.social
academic.oup.com/nar/article/...

Changes to the 2026 and 2027 Work Programmes With the launch of the competitions for grants under ERC Work Programme 2026 in July of this year, several changes to the submission of applications and the evaluation of proposals will apply. The mai...

Planning to apply for #research #funding from the ERC?

From the next application rounds, expect changes to the:

• proposal structure
• evaluation process
• extra funding you can request
• eligibility for Starting & Consolidator #Grants (from 2027)

More 👇 europa.eu/!RPHWvv

Phase behavior and dissociation kinetics of lamins in a polymer model of progeria One of the key structural proteins in the eukaryotic cell nucleus is lamin. Lamins can assemble into a two-dimensional protein meshwork at the nuclear periphery

Read more 👉 pubs.aip.org/aip/jcp/arti...
#CellBiology #Laminopathies #HGPS #NuclearMechanics #Research #Biophysics

Phase behavior and dissociation kinetics of lamins in a polymer model of progeria One of the key structural proteins in the eukaryotic cell nucleus is lamin. Lamins can assemble into a two-dimensional protein meshwork at the nuclear periphery

we uncover how changes in lamin-lamin and lamin-INM interaction could drive the emergence of abnormal lamin phases that can appear in laminopathies. These findings hint at how competition between various physical interactions can affect lamina and maybe drive disease progression.

Phase behavior and dissociation kinetics of lamins in a polymer model of progeria One of the key structural proteins in the eukaryotic cell nucleus is lamin. Lamins can assemble into a two-dimensional protein meshwork at the nuclear periphery

Our recent study (using a minimal molecular dynamics model) investigates how lamin concentration and affinity interactions dictate the formation of these dense nematic domains, affecting dissociation dynamics. By modeling lamin fibers as rod-like polymer chains,

Phase behavior and dissociation kinetics of lamins in a polymer model of progeria One of the key structural proteins in the eukaryotic cell nucleus is lamin. Lamins can assemble into a two-dimensional protein meshwork at the nuclear periphery

How Can Mesoscale Phases of Lamin Fibrous Structure Form on the Nuclear Surface? 🔍🧬
Lamina is a protective meshwork at the nuclear periphery, but in diseases like HGPS, its structure becomes disrupted and becomes thicker with the traces of nematically ordered lamin fibers.

Peripheral heterochromatin tethering is required for chromatin-based nuclear mechanical response The cell nucleus is a mechanically responsive structure that governs how external forces affect chromosomes. Chromatin, particularly transcriptionally inactive heterochromatin, resists nuclear deformations through its mechanical response. However, chromatin also exhibits liquid-like properties, casting ambiguity on the physical mechanisms of chromatin-based nuclear elasticity. To determine how heterochromatin strengthens nuclear mechanical response, we performed polymer physics simulations of a nucleus model validated by micromechanical measurements and chromosome conformation capture data. The attachment of peripheral heterochromatin to the lamina is required to transmit forces directly to the chromatin and elicit its elastic response. Thus, increases in heterochromatin levels increase nuclear rigidity by increasing the linkages between chromatin and the lamina. Crosslinks within heterochromatin, such as HP1α proteins, can also stiffen nuclei, but only if chromatin is peripherally tethered. In contrast, heterochromatin affinity interactions that may drive liquid-liquid phase separation do not contribute to nuclear rigidity. When the nucleus is stretched, gel-like peripheral heterochromatin can bear stresses and deform, while the more fluid-like interior euchromatin is less perturbed. Thus, heterochromatin's internal structure and stiffness may regulate nuclear mechanics via peripheral attachment to the lamina, while also enabling nuclear mechanosensing of external forces and external measurement of the nucleus' internal architecture. ### Competing Interest Statement The authors have declared no competing interest.

A bright spot in the midst of this ongoing disaster: new work in collab w/ Aykut Erbas + his former student Goktug Attar

Heterochromatin stiffens cell nuclei, but how? What is the physical mechanism of chromatin-based force response? We use polymer sims...
www.biorxiv.org/content/10.1...