Stefan Diez Group – RTG 3120 Biomolecular Condensates https://dresdencondensates.org From Physics to Biological Functions Mon, 15 Aug 2022 07:51:53 +0000 en-US hourly 1 https://wordpress.org/?v=6.9.4 https://dresdencondensates.org/wp-content/uploads/2022/01/cropped-Icon-32x32.jpg Stefan Diez Group – RTG 3120 Biomolecular Condensates https://dresdencondensates.org 32 32 The ALS-Associated FUS (P525L) Variant Does Not Directly Interfere with Microtubule-Dependent Kinesin-1 Motility https://dresdencondensates.org/the-als-associated-fus-p525l-variant-does-not-directly-interfere-with-microtubule-dependent-kinesin-1-motility/ https://dresdencondensates.org/the-als-associated-fus-p525l-variant-does-not-directly-interfere-with-microtubule-dependent-kinesin-1-motility/#respond Sun, 28 Feb 2021 13:00:44 +0000 https://dresdencondensates.org/?p=951 The Diez lab, in collaboration with the Hermann lab in Rostock, Germany, have utilised an in vitro microtubule gliding motility assay to study deficient intracellular transport in motor neurons. The findings  exclude a role of mutations in the phase-separating FUS protein, known to be mutated in neurodegenerative diseases like amyotrophic lateral sclerosis (ALS). in The study was published in the International Journal of Molecular Sciences as part of the Special Issue Molecular Mechanisms of Aging-Related Neurodegenerative Diseases.

Reconstituting axonal transport in vitro
]]> https://dresdencondensates.org/the-als-associated-fus-p525l-variant-does-not-directly-interfere-with-microtubule-dependent-kinesin-1-motility/feed/ 0 Cytoskeletal organization through multivalent interactions https://dresdencondensates.org/cytoskeletal-organization-through-multivalent-interactions/ https://dresdencondensates.org/cytoskeletal-organization-through-multivalent-interactions/#respond Mon, 15 Jun 2020 12:46:53 +0000 https://dresdencondensates.org/?p=958 Stefan Diez and collaborators Zdenek Lansky and Marcus Braun from the Institute of Biotechnology of the Czech Academy of Sciences, Czech Republic, published an Opinion article emphasizing the role of multivalent interactions cytoskeletal phenomena including (1) the generation of entropic forces by filament crosslinkers, (2) processivity of molecular motors, (3) spatial sorting of proteins, and (4) concentration-dependent unbinding of filament-associated proteins. The article was published in the Journal of Cell Science.

Consequences of multivalent interactions on ligand–receptor interaction kinetics

]]> https://dresdencondensates.org/cytoskeletal-organization-through-multivalent-interactions/feed/ 0 Kinetically distinct phases of tau on microtubules regulate kinesin motors and severing enzymes https://dresdencondensates.org/kinetically-distinct-phases-of-tau-on-microtubules-regulate-kinesin-motors-and-severing-enzymes/ https://dresdencondensates.org/kinetically-distinct-phases-of-tau-on-microtubules-regulate-kinesin-motors-and-severing-enzymes/#respond Tue, 02 Jul 2019 12:59:13 +0000 https://dresdencondensates.org/?p=969 The Diez and Hyman labs, in collaboration with the Lansky and Braun lab at the Institute of Biotechnology of the Czech Academy of Sciences, Czech Republic, published a study on the role of phase separation of the intrinsically disordered Tau protein  in regulating the activity of motor proteins and severing enzymes on microtubules. The study, published in Nature Cell Biology demonstrated using in vitro protein reconstitution that Tau protects microtubules from degradation by forming reversible cohesive islands.

Tau islands constitute a protective layer around microtubules
]]> https://dresdencondensates.org/kinetically-distinct-phases-of-tau-on-microtubules-regulate-kinesin-motors-and-severing-enzymes/feed/ 0 Local nucleation of microtubule bundles through tubulin concentration into a condensed tau phase https://dresdencondensates.org/local-nucleation-of-microtubule-bundles-through-tubulin-concentration-into-a-condensed-tau-phase/ https://dresdencondensates.org/local-nucleation-of-microtubule-bundles-through-tubulin-concentration-into-a-condensed-tau-phase/#respond Tue, 05 Sep 2017 07:51:22 +0000 https://dresdencondensates.org/?p=974 Theskeleton that supports the structure of our cells, termed cytoskeleton is formed of several kinds of polymers including actin and microtubules. How the single units on the polymers (monomers and dimers) are concentrated to gether to synthesize the polymer is the subject of this study by the labs of Diez, Hyman, and Alberti. The authors identified a protein associated to the cytoskeleton, named Tau, that is able to phase-separate from the cytosol. Tau concentrates the tubulin dimers, which in turn polymerize to make microtubules inside the tau droplet. As opposed to this physiological phenomenon, pathological aggregation of mutated tau is a hallmark of neurodegenerative disorders, including Alzheimer’s disease.

Read more: https://doi.org/10.1016/j.celrep.2017.08.042

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