scholarly journals Membrane Thinning Induces Sorting of Lipids and the Amphipathic Lipid Packing Sensor (ALPS) Protein Motif

2020 ◽  
Vol 11 ◽  
Author(s):  
Niek van Hilten ◽  
Kai Steffen Stroh ◽  
Herre Jelger Risselada
Keyword(s):  
Protein Motif ◽  
Lipid Packing ◽  
Membrane Thinning

TBC proteins: GAPs for mammalian small GTPase Rab?

2011 ◽  
Vol 31 (3) ◽  
pp. 159-168 ◽  
Author(s):  
Mitsunori Fukuda
Keyword(s):  
Insulin Resistance ◽  
Small Gtpases ◽  
Structure And Function ◽  
Small Gtpase ◽  
Cell Cycle Regulators ◽  
Gtpase Activating Protein ◽  
Domain Family ◽  
Protein Motif ◽  
Conserved Domain ◽  
And Function

The TBC (Tre-2/Bub2/Cdc16) domain was originally identified as a conserved domain among the tre-2 oncogene product and the yeast cell cycle regulators Bub2 and Cdc16, and it is now widely recognized as a conserved protein motif that consists of approx. 200 amino acids in all eukaryotes. Since the TBC domain of yeast Gyps [GAP (GTPase-activating protein) for Ypt proteins] has been shown to function as a GAP domain for small GTPase Ypt/Rab, TBC domain-containing proteins (TBC proteins) in other species are also expected to function as a certain Rab-GAP. More than 40 different TBC proteins are present in humans and mice, and recent accumulating evidence has indicated that certain mammalian TBC proteins actually function as a specific Rab-GAP. Some mammalian TBC proteins {e.g. TBC1D1 [TBC (Tre-2/Bub2/Cdc16) domain family, member 1] and TBC1D4/AS160 (Akt substrate of 160 kDa)} play an important role in homoeostasis in mammals, and defects in them are directly associated with mouse and human diseases (e.g. leanness in mice and insulin resistance in humans). The present study reviews the structure and function of mammalian TBC proteins, especially in relation to Rab small GTPases.

Penetration and preferential binding of charged nanoparticles to mixed lipid monolayers: interplay of lipid packing and charge density

Soft Matter ◽  
2020 ◽  
Author(s):  
Anurag Chaudhury ◽  
Koushik Debnath ◽  
Wei Bu ◽  
Nikhil R. Jana ◽  
Jaydeep Kumar Basu
Keyword(s):  
Charge Density ◽  
Biomedical Applications ◽  
Cell Membranes ◽  
Lipid Monolayers ◽  
Cytotoxic Effects ◽  
Lipid Packing ◽  
Preferential Binding ◽  
Charged Nanoparticles

Designing of nanoparticles (NPs) for biomedical applications or mitigating their cytotoxic effects require microscopic understanding of their interactions with cell membranes. Such insight is best obtained by studying model biomembranes...

Specificity and promiscuity in membrane helix interactions

1994 ◽  
Vol 27 (2) ◽  
pp. 157-218 ◽  
Author(s):  
Mark A. Lemmon ◽  
Donald M. Engelman
Keyword(s):  
Membrane Proteins ◽  
Transmembrane Helix ◽  
Integral Membrane Proteins ◽  
Lipid Packing ◽  
Membrane Protein Folding ◽  
Membrane Spanning ◽  
Α Helix ◽  
Prosthetic Groups ◽  
Packing Effects ◽  
Helix Interactions

The membrane-spanning portions of many integral membrane proteins consist of one or a number of transmembrane α-helices, which are expected to be independently stable on thermodynamic grounds. Side-by-side interactions between these transmembrane α-helices are important in the folding and assembly of such integral membrane proteins and their complexes. In considering the contribution of these helix–helix interactions to membrane protein folding and oligomerization, a distinction between the energetics and specificity should be recognized. A number of contributions to the energetics of transmembrane helix association within the lipid bilayer will be relatively non-specific, including those resulting from charge–charge interactions and lipid–packing effects. Specificity (and part of the energy) in transmembrane α-helix association, however, appears to rely mainly upon a detailed stereochemical fit between sets of dynamically accessible states of particular helices. In some cases, these interactions are mediated in part by prosthetic groups.

scholarly journals Entropic Forces, Zippering Pressure and Membrane Thinning Drive Snare-Mediated Membrane Fusion

2021 ◽  
Vol 120 (3) ◽  
pp. 51a
Author(s):  
Jin Zeng ◽  
Zachary A. McDargh ◽  
Ben O’Shaughnessy
Keyword(s):  
Membrane Fusion ◽  
Membrane Thinning

scholarly journals Super-Resolving Membrane Geometry and Lipid Packing in Living Cells

2021 ◽  
Vol 120 (3) ◽  
pp. 40a
Author(s):  
Gabriele Kockelkoren ◽  
Line Lauritsen ◽  
Dimitrios Stamou
Keyword(s):  
Living Cells ◽  
Lipid Packing ◽  
Membrane Geometry

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
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