Heterogeneity in the Binding of Lipid Molecules to the Surface of a Membrane Protein:  Hot Spots for Anionic Lipids on the Mechanosensitive Channel of Large Conductance MscL and Effects on Conformation†

Biochemistry ◽  
2005 ◽  
Vol 44 (15) ◽  
pp. 5873-5883 ◽  
Author(s):  
Andrew M. Powl ◽  
J. Malcolm East ◽  
Anthony G. Lee
Keyword(s):  
Membrane Protein ◽  
Hot Spots ◽  
Mechanosensitive Channel ◽  
Protein Hot Spots ◽  
Anionic Lipids

scholarly journals PDZD8 mediates a Rab7-dependent interaction of the ER with late endosomes and lysosomes

2019 ◽  
Vol 116 (45) ◽  
pp. 22619-22623 ◽  
Author(s):  
Andrés Guillén-Samander ◽  
Xin Bian ◽  
Pietro De Camilli
Keyword(s):  
Endoplasmic Reticulum ◽  
Membrane Protein ◽  
Hot Spots ◽  
Transport Proteins ◽  
Lipid Transport ◽  
Domain Family ◽  
Late Endosomes ◽  
Dependent Interaction

Contacts between the endoplasmic reticulum (ER) and other membranes are hot spots for protein-mediated lipid transport between the 2 adjacent bilayers. Compiling a molecular inventory of lipid transport proteins present at these sites is a premise to the elucidation of their function. Here we show that PDZD8, an intrinsic membrane protein of the ER with a lipid transport module of the SMP domain family, concentrates at contacts between the ER and late endosomes/lysosomes, where it interacts with GTP-Rab7. These findings suggest that PDZD8 may cooperate with other proteins that function at the ER–endo/lysosome interface in coordinating endocytic flow with lipid transport between endocytic membranes and the ER.

scholarly journals Anionic lipids stimulate Sec‐independent insertion of a membrane protein lacking charged amino acid side chains

EMBO Reports ◽  
2001 ◽  
Vol 2 (5) ◽  
pp. 403-408 ◽  
Author(s):  
Anja N J A Ridder ◽  
Andreas Kuhn ◽  
J Antoinette Killian ◽  
Ben de Kruijff
Keyword(s):  
Amino Acid ◽  
Membrane Protein ◽  
Side Chains ◽  
Amino Acid Side Chains ◽  
Anionic Lipids

scholarly journals Diblock copolymers enhance folding of a mechanosensitive membrane protein during cell-free expression

2019 ◽  
Vol 116 (10) ◽  
pp. 4031-4036 ◽  
Author(s):  
Miranda L. Jacobs ◽  
Margrethe A. Boyd ◽  
Neha P. Kamat
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Physical Properties ◽  
Diblock Copolymers ◽  
Biological Membrane ◽  
Membrane Surface ◽  
Lipid Vesicles ◽  
Mechanosensitive Channel ◽  
Membrane Area ◽  
Vesicle Membranes

The expression and integration of membrane proteins into vesicle membranes is a critical step in the design of cell-mimetic biosensors, bioreactors, and artificial cells. While membrane proteins have been integrated into a variety of nonnatural membranes, the effects of the chemical and physical properties of these vesicle membranes on protein behavior remain largely unknown. Nonnatural amphiphiles, such as diblock copolymers, provide an interface that can be synthetically controlled to better investigate this relationship. Here, we focus on the initial step in a membrane protein’s life cycle: expression and folding. We observe improvements in both the folding and overall production of a model mechanosensitive channel protein, the mechanosensitive channel of large conductance, during cell-free reactions when vesicles containing diblock copolymers are present. By systematically tuning the membrane composition of vesicles through incorporation of a poly(ethylene oxide)-b-poly(butadiene) diblock copolymer, we show that membrane protein folding and production can be improved over that observed in traditional lipid vesicles. We then reproduce this effect with an alternate membrane-elasticizing molecule, C12E8. Our results suggest that global membrane physical properties, specifically available membrane surface area and the membrane area expansion modulus, significantly influence the folding and yield of a membrane protein. Furthermore, our results set the stage for explorations into how nonnatural membrane amphiphiles can be used to both study and enhance the production of biological membrane proteins.

Diverse Fragment Clustering and Water Exclusion Identify Protein Hot Spots

2011 ◽  
Vol 133 (28) ◽  
pp. 10740-10743 ◽  
Author(s):  
John L. Kulp ◽  
John L. Kulp ◽  
David L. Pompliano ◽  
Frank Guarnieri
Keyword(s):  
Hot Spots ◽  
Protein Hot Spots

scholarly journals Protein hot spots at bio-nano interfaces

2011 ◽  
Vol 14 (7-8) ◽  
pp. 360-365 ◽  
Author(s):  
Gerald F. Audette ◽  
Stephanie Lombardo ◽  
Jonathan Dudzik ◽  
Thomas M. Arruda ◽  
Michal Kolinski ◽  
...  
Keyword(s):  
Hot Spots ◽  
Protein Hot Spots

scholarly journals TMEM120A is a coenzyme A-binding membrane protein with structural similarities to ELOVL fatty acid elongase

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Jing Xue ◽  
Yan Han ◽  
Hamid Baniasadi ◽  
Weizhong Zeng ◽  
Jimin Pei ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Membrane Protein ◽  
Coenzyme A ◽  
Transmembrane Domain ◽  
Coiled Coil ◽  
Structural Features ◽  
Mechanosensitive Channel ◽  
Transmembrane Helices ◽  
Long Chain Fatty Acid ◽  
Fatty Acid Elongase

TMEM120A, also named as TACAN, is a novel membrane protein highly conserved in vertebrates and was recently proposed to be a mechanosensitive channel involved in sensing mechanical pain. Here we present the single particle cryo-EM structure of human TMEM120A which forms a tightly packed dimer with extensive interactions mediate by the N-terminal coiled coil domain (CCD), the C-terminal transmembrane domain (TMD), and the re-entrant loop between the two domains. The TMD of each TMEM120A subunit contains six transmembrane helices (TMs) and has no clear structural feature of a channel protein. Instead, the six TMs form an α-barrel with a deep pocket where a coenzyme A (CoA) molecule is bound. Intriguingly, some structural features of TMEM120A resemble those of elongase for very long-chain fatty acid (ELOVL) despite low sequence homology between them, pointing to the possibility that TMEM120A may function as an enzyme for fatty acid metabolism, rather than a mechanosensitive channel.

Protein Hot Spots: The Islands of Stability

2012 ◽  
Vol 415 (2) ◽  
pp. 419-428 ◽  
Author(s):  
Yosef Y. Kuttner ◽  
Stanislav Engel
Keyword(s):  
Hot Spots ◽  
Protein Hot Spots
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