scholarly journals A sub-nanometre view of how membrane curvature and composition modulate lipid packing and protein recruitment

2014 ◽  
Vol 5 (1) ◽  
Author(s):  
Stefano Vanni ◽  
Hisaaki Hirose ◽  
Hélène Barelli ◽  
Bruno Antonny ◽  
Romain Gautier
Keyword(s):  
Membrane Curvature ◽  
Lipid Packing ◽  
Protein Recruitment

scholarly journals ArfGAP1 responds to membrane curvature through the folding of a lipid packing sensor motif

2005 ◽  
Vol 24 (13) ◽  
pp. 2244-2253 ◽  
Author(s):  
Joëlle Bigay ◽  
Jean-François Casella ◽  
Guillaume Drin ◽  
Bruno Mesmin ◽  
Bruno Antonny
Keyword(s):  
Membrane Curvature ◽  
Lipid Packing

scholarly journals Synapsin I Senses Membrane Curvature by an Amphipathic Lipid Packing Sensor Motif

2011 ◽  
Vol 31 (49) ◽  
pp. 18149-18154 ◽  
Author(s):  
L. Krabben ◽  
A. Fassio ◽  
V. K. Bhatia ◽  
A. Pechstein ◽  
F. Onofri ◽  
...  
Keyword(s):  
Membrane Curvature ◽  
Synapsin I ◽  
Lipid Packing

scholarly journals Timing of ESCRT-III protein recruitment and membrane scission during HIV-1 assembly

2018 ◽  
Author(s):  
Daniel S. Johnson ◽  
Marina Bleck ◽  
Sanford M. Simon
Keyword(s):  
Multivesicular Body ◽  
Cellular Membrane ◽  
Membrane Curvature ◽  
Gag Protein ◽  
Endosomal Sorting ◽  
Membrane Scission ◽  
Nuclear Envelope Formation ◽  
Protein Recruitment ◽  
Late Domains ◽  
Hiv 1

The Endosomal Sorting Complexes Required for Transport III (ESCRT-III) proteins are critical for cellular membrane scission processes with topologies inverted relative to clathrin-mediated endocytosis. Some viruses appropriate ESCRT-IIIs for their release. By imaging single assembling viral-like particles of HIV-1, we observed that ESCRT-IIIs and the ATPase VPS4 arrive after most of the virion membrane is bent, linger for tens of seconds, and depart ∼20 seconds before scission. These observations suggest ESCRT-IIIs are recruited by a combination of membrane curvature and the late domains of the HIV-1 Gag protein. ESCRT-IIIs may pull the neck into a narrower form but must leave to allow scission. If scission does not occur within minutes of ESCRT departure, ESCRT-III and VPS4 are recruited again. This mechanistic insight is likely relevant for other ESCRT dependent scission processes including cell division, endosome tubulation, multivesicular body and nuclear envelope formation, and secretion of exosomes and ectosomes.

scholarly journals Dynamic recruitment of the curvature-sensitive protein ArhGAP44 to nanoscale membrane deformations limits exploratory filopodia initiation in neurons

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Milos Galic ◽  
Feng-Chiao Tsai ◽  
Sean R Collins ◽  
Maja Matis ◽  
Samuel Bandara ◽  
...  
Keyword(s):  
Actin Polymerization ◽  
Neuronal Development ◽  
Membrane Curvature ◽  
Gtp Hydrolysis ◽  
Bar Domain ◽  
Curvature Sensing ◽  
Contractile Forces ◽  
Dendritic Branches ◽  
Membrane Deformations ◽  
Protein Recruitment

In the vertebrate central nervous system, exploratory filopodia transiently form on dendritic branches to sample the neuronal environment and initiate new trans-neuronal contacts. While much is known about the molecules that control filopodia extension and subsequent maturation into functional synapses, the mechanisms that regulate initiation of these dynamic, actin-rich structures have remained elusive. Here, we find that filopodia initiation is suppressed by recruitment of ArhGAP44 to actin-patches that seed filopodia. Recruitment is mediated by binding of a membrane curvature-sensing ArhGAP44 N-BAR domain to plasma membrane sections that were deformed inward by acto-myosin mediated contractile forces. A GAP domain in ArhGAP44 triggers local Rac-GTP hydrolysis, thus reducing actin polymerization required for filopodia formation. Additionally, ArhGAP44 expression increases during neuronal development, concurrent with a decrease in the rate of filopodia formation. Together, our data reveals a local auto-regulatory mechanism that limits initiation of filopodia via protein recruitment to nanoscale membrane deformations.

Two Lipid-Packing Sensor Motifs Contribute to the Sensitivity of ArfGAP1 to Membrane Curvature†

Biochemistry ◽  
2007 ◽  
Vol 46 (7) ◽  
pp. 1779-1790 ◽  
Author(s):  
Bruno Mesmin ◽  
Guillaume Drin ◽  
Sharon Levi ◽  
Moran Rawet ◽  
Dan Cassel ◽  
...  
Keyword(s):  
Membrane Curvature ◽  
Lipid Packing

scholarly journals Timing of ESCRT-III protein recruitment and membrane scission during HIV-1 assembly

eLife ◽  
2018 ◽  
Vol 7 ◽  
Author(s):  
Daniel S Johnson ◽  
Marina Bleck ◽  
Sanford M Simon
Keyword(s):  
Multivesicular Body ◽  
Cellular Membrane ◽  
Membrane Curvature ◽  
Gag Protein ◽  
Endosomal Sorting ◽  
Membrane Scission ◽  
Nuclear Envelope Formation ◽  
Protein Recruitment ◽  
Late Domains ◽  
Hiv 1

The Endosomal Sorting Complexes Required for Transport III (ESCRT-III) proteins are critical for cellular membrane scission processes with topologies inverted relative to clathrin-mediated endocytosis. Some viruses appropriate ESCRT-IIIs for their release. By imaging single assembling viral-like particles of HIV-1, we observed that ESCRT-IIIs and the ATPase VPS4 arrive after most of the virion membrane is bent, linger for tens of seconds, and depart ~20 s before scission. These observations suggest that ESCRT-IIIs are recruited by a combination of membrane curvature and the late domains of the HIV-1 Gag protein. ESCRT-IIIs may pull the neck into a narrower form but must leave to allow scission. If scission does not occur within minutes of ESCRT departure, ESCRT-IIIs and VPS4 are recruited again. This mechanistic insight is likely relevant for other ESCRT-dependent scission processes including cell division, endosome tubulation, multivesicular body and nuclear envelope formation, and secretion of exosomes and ectosomes.

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