[PDF][PDF] Viral infection controlled by a calcium-dependent lipid-binding module in ALIX
ALIX plays a role in nucleocapsid release during viral infection, as does lysobisphosphatidic
acid (LBPA). However, the mechanism remains unclear. Here we report that LBPA is …
acid (LBPA). However, the mechanism remains unclear. Here we report that LBPA is …
In vitro budding of intralumenal vesicles into late endosomes is regulated by Alix and Tsg101
…, PP Luyet, C Bissig, CC Scott, MC Velluz… - Molecular biology of …, 2008 - Am Soc Cell Biol
Endosomes along the degradation pathway leading to lysosomes accumulate membranes
in their lumen and thus exhibit a characteristic multivesicular appearance. These lumenal …
in their lumen and thus exhibit a characteristic multivesicular appearance. These lumenal …
[PDF][PDF] Motor usage imprints microtubule stability along the shaft
M Andreu-Carbó, S Fernandes, MC Velluz, K Kruse… - Developmental cell, 2022 - cell.com
Tubulin dimers assemble into dynamic microtubules, which are used by molecular motors as
tracks for intracellular transport. Organization and dynamics of the microtubule network are …
tracks for intracellular transport. Organization and dynamics of the microtubule network are …
Tubulin engineering by semi-synthesis reveals that polyglutamylation directs detyrosination
…, N Guidotti, TM Reichart, L Reymond, MC Velluz… - Nature Chemistry, 2023 - nature.com
Microtubules, a critical component of the cytoskeleton, carry post-translational modifications
(PTMs) that are important for the regulation of key cellular processes. Long-lived …
(PTMs) that are important for the regulation of key cellular processes. Long-lived …
Phase separation of+ TIP networks regulates microtubule dynamics
J Miesch, RT Wimbish, MC Velluz… - Proceedings of the …, 2023 - National Acad Sciences
Regulation of microtubule dynamics is essential for diverse cellular functions, and proteins
that bind to dynamic microtubule ends can regulate network dynamics. Here, we show that …
that bind to dynamic microtubule ends can regulate network dynamics. Here, we show that …
Conversion of a transmembrane to a water-soluble protein complex by a single point mutation
…, CJ Morton, C El Bez, P Paumard, MC Velluz… - nature structural …, 2002 - nature.com
Proteins exist in one of two generally incompatible states: either membrane associated or
soluble. Pore-forming proteins are exceptional because they are synthesized as a water-…
soluble. Pore-forming proteins are exceptional because they are synthesized as a water-…
[HTML][HTML] The glycan core of GPI-anchored proteins modulates aerolysin binding but is not sufficient: the polypeptide moiety is required for the toxin–receptor interaction
L Abrami, MC Velluz, Y Hong, K Ohishi, A Mehlert… - FEBS letters, 2002 - Elsevier
Sensitivity of mammalian cells to the bacterial toxin aerolysin is due to the presence at their
surface of glycosylphosphatidyl inositol (GPI)-anchored proteins which act as receptors. …
surface of glycosylphosphatidyl inositol (GPI)-anchored proteins which act as receptors. …
[HTML][HTML] Microtubule damage shapes the acetylation gradient
M Andreu-Carbó, C Egoldt, MC Velluz… - Nature …, 2024 - nature.com
The properties of single microtubules within the microtubule network can be modulated
through post-translational modifications (PTMs), including acetylation within the lumen of …
through post-translational modifications (PTMs), including acetylation within the lumen of …
[HTML][HTML] Dimer dissociation of the pore-forming toxin aerolysin precedes receptor binding
M Fivaz, MC Velluz, FG van der Goot - Journal of Biological Chemistry, 1999 - ASBMB
The pore-forming toxin aerolysin is secreted byAeromonas hydrophila as an inactive precursor.
Based on chemical cross-linking and gel filtration, we show here that proaerolysin exists …
Based on chemical cross-linking and gel filtration, we show here that proaerolysin exists …
N-Glycans mutations rule oligomeric assembly and functional expression of P2X3 receptor for extracellular ATP
…, ML Cucchiaroni, A Tozzi, MC Velluz… - …, 2011 - academic.oup.com
N-Glycosylation affects the function of ion channels at the level of multisubunit assembly,
protein trafficking, ligand binding and channel opening. Like the majority of membrane proteins, …
protein trafficking, ligand binding and channel opening. Like the majority of membrane proteins, …