The Role of Drebrin-Binding Stable Actin Filaments in Dendritic Spine Morphogenesis

AbstractDendritic spines, small protrusions of the dendrites, enlarge upon LTP induction, linking morphological and functional properties. Although the role of actin in spine enlargement has been well studied, little is known about its relationship with mechanical membrane properties, such as membrane tension, which is involved in many cell processes, like exocytosis. Here, we use a 3D model of the dendritic spine to investigate how polymerization of actin filaments can effectively elevate the membrane tension to trigger exocytosis in a domain close to the tip of the spine. Moreover, we show that the same pool of actin promotes full membrane fusion after exocytosis and spine stabilization.

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Exploring new roles for actin upon LTP induction in dendritic spines

10.1101/2020.11.14.382663 ◽

2020 ◽

Author(s):

Mayte Bonilla-Quintana ◽

Florentin Wörgötter

Keyword(s):

Membrane Fusion ◽

Dendritic Spines ◽

Dendritic Spine ◽

Actin Filaments ◽

3D Model ◽

Membrane Properties ◽

Membrane Tension ◽

Spine Stabilization ◽

Cell Processes

AbstractDendritic spines, small protrusions of the dendrites, enlarge upon LTP induction, linking morphological and functional properties. Although the role of actin in spine enlargement has been well studied, little is known about its relationship with mechanical membrane properties, such as membrane tension, which is involved in many cell processes, like exocytosis. Here, we use a 3D model of the dendritic spine to investigate how polymerization of actin filaments can effectively elevate the membrane tension to trigger exocytosis in a domain close to the tip of the spine. Moreover, we show that the same pool of actin promotes full membrane fusion after exocytosis and spine stabilization.

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The Role of Rac GTPase in Dendritic Spine Morphogenesis and Memory

Frontiers in Synaptic Neuroscience ◽

10.3389/fnsyn.2020.00012 ◽

2020 ◽

Vol 12 ◽

Cited By ~ 3

Author(s):

Joana Freitas Costa ◽

Monica Dines ◽

Raphael Lamprecht

Keyword(s):

Dendritic Spine ◽

Rac Gtpase ◽

Spine Morphogenesis

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Faculty Opinions recommendation of Rapid induction of dendritic spine morphogenesis by trans-synaptic ephrinB-EphB receptor activation of the Rho-GEF kalirin.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.1011905.183726 ◽

2003 ◽

Author(s):

Angus Nairn

Keyword(s):

Dendritic Spine ◽

Receptor Activation ◽

Rapid Induction ◽

Ephb Receptor ◽

Rho Gef ◽

Spine Morphogenesis

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Faculty Opinions recommendation of The role of synaptopodin in membrane protein diffusion in the dendritic spine neck.

Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature ◽

10.3410/f.726116756.793519383 ◽

2016 ◽

Author(s):

Donna Webb

Keyword(s):

Membrane Protein ◽

Dendritic Spine ◽

Protein Diffusion

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Platelet Shape Changes during Thrombus Formation: Role of Actin-Based Protrusions

Hämostaseologie ◽

10.1055/a-1325-0993 ◽

2021 ◽

Vol 41 (01) ◽

pp. 014-021

Author(s):

Markus Bender ◽

Raghavendra Palankar

Keyword(s):

Blood Loss ◽

Actin Filaments ◽

Thrombus Formation ◽

Short Review ◽

Critical Component ◽

Clot Retraction ◽

Shape Changes ◽

Platelet Shape

AbstractPlatelet activation and aggregation are essential to limit blood loss at sites of vascular injury but may also lead to occlusion of diseased vessels. The platelet cytoskeleton is a critical component for proper hemostatic function. Platelets change their shape after activation and their contractile machinery mediates thrombus stabilization and clot retraction. In vitro studies have shown that platelets, which come into contact with proteins such as fibrinogen, spread and first form filopodia and then lamellipodia, the latter being plate-like protrusions with branched actin filaments. However, the role of platelet lamellipodia in hemostasis and thrombus formation has been unclear until recently. This short review will briefly summarize the recent findings on the contribution of the actin cytoskeleton and lamellipodial structures to platelet function.

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