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| http://dx.doi.org/10.1016/j.isci.2020.101042 | DOI Listing |
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Novel lipid-interaction motifs within the C-terminal domain of Septin10 from Schistosoma mansoni.
Biochim Biophys Acta Biomembr
October 2024
São Carlos Institute of Physics, University of São Paulo, São Carlos, SP 13560-970, Brazil. Electronic address:
Septins are cytoskeletal proteins and their interaction with membranes is crucial for their role in various cellular processes. Septins have polybasic regions (PB1 and PB2) which are important for lipid interaction. Earlier, we and others have highlighted the role of the septin C-terminal domain (CTD) to membrane interaction.
View Article and Find Full Text PDFSeptin 9 Orients the Apico-Basal Polarity Axis and Controls Plasticity Signals.
Cells
July 2023
Unité 1193 INSERM, F-94800 Villejuif, France.
The cytoskeleton is a master organizer of the cellular cortex and membrane trafficking and therefore plays a crucial role in apico-basal polarity. Septins form a family of GTPases that assemble into non-polar filaments, which bind to membranes and recruit cytoskeletal elements such as microtubules and actin using their polybasic (PB) domains, to perform their broad biological functions. Nevertheless, the role of septins and the significance of their membrane-binding ability in apico-basal polarity remains under-investigated.
View Article and Find Full Text PDFAn atomic model for the human septin hexamer by cryo-EM.
J Mol Biol
July 2021
São Carlos Institute of Physics, USP, São Carlos, SP, Brazil. Electronic address:
In order to form functional filaments, human septins must assemble into hetero-oligomeric rod-like particles which polymerize end-to-end. The rules governing the assembly of these particles and the subsequent filaments are incompletely understood. Although crystallographic approaches have been successful in studying the separate components of the system, there has been difficulty in obtaining high resolution structures of the full particle.
View Article and Find Full Text PDFSEPT7 regulates Ca entry through Orai channels in human neural progenitor cells and neurons.
Cell Calcium
September 2020
National Centre for Biological Sciences (NCBS), Tata Institute of Fundamental Research, Bangalore, India. Electronic address:
Article Synopsis
- Human neural progenitor cells (hNPCs) can differentiate into various neuron types, and SEPT7 is crucial for managing calcium levels in these cells by preventing excessive calcium entry through the Orai channel.
- Research indicates that a specific region of SEPT7 interacts with cell membrane lipids to regulate calcium flow, while its GTPase domain is not necessary for this function.
- The study highlights how reduced SEPT7 levels alter the organization of calcium-sensing proteins and could lead to mechanisms that open calcium channels without depleting calcium stores.
A complete compendium of crystal structures for the human SEPT3 subgroup reveals functional plasticity at a specific septin interface.
IUCrJ
May 2020
Instituto de Física de São Carlos, Universidade de São Paulo, Avenida Joao Dagnone 1100, São Carlos-SP 13563-723, Brazil.
Article Synopsis
- Human septins 3, 9, and 12, part of the SEPT3 subgroup, are unique due to their lack of a C-terminal coiled coil and formation of octameric protofilaments, unlike other hexameric septins.
- These septins can self-assemble into mixed filaments and form higher-order complexes with membranes, potentially influencing various cellular processes.
- The study presents detailed crystal structures of the GTP-binding domains of SEPT3 members, revealing a mechanism for membrane interaction linked to GTP binding and hydrolysis, underscoring the special role of this subgroup in cellular functions.
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