scholarly journals The influence of membrane bound proteins on phase separation and coarsening in cell membranes

2012 ◽  
Vol 14 (42) ◽  
pp. 14509 ◽  
Author(s):  
Thomas Witkowski ◽  
Rainer Backofen ◽  
Axel Voigt
1995 ◽  
Vol 268 (2) ◽  
pp. C308-C316 ◽  
Author(s):  
A. K. Rajasekaran ◽  
S. A. Langhans-Rajasekaran ◽  
R. M. Gould ◽  
E. Rodriguez-Boulan ◽  
T. Morimoto

In this report we demonstrate that the changes in size of the rough endoplasmic reticulum (RER) can be determined by quantifying the membrane-bound ribosomal population separated by cell fractionation and sucrose density gradient analysis. Total cell membranes, rather than microsomes, were used as the source of membrane-bound ribosomes to eliminate potential losses during the preparation of microsomes. Bound ribosomes were assayed after quantitative release and recovery from total cell membranes using puromycin in the presence of high-salt buffer. Using this analysis, we demonstrate a 4.2-fold increase in RER in estrogen-treated male Xenopus laevis liver. Furthermore, we show that the ratio of the distribution of free to membrane-bound ribosomes in a nonsecretory cell line (HeLa) was 3.3, while this ratio in a secretory cell line (AR42J) was 1.2, indicating that cells active in secretion contain more RER. We suggest that this biochemical technique provides a simpler assay to detect changes in the size of the RER.


Physiology ◽  
1988 ◽  
Vol 3 (4) ◽  
pp. 154-157
Author(s):  
SA Kempson

The characteristics of phosphate transport across epithelial cell membranes and the influence of hormones and other factors have been studied in detail. Almost no information has emerged about the identity, structure, and biogenesis of the membrane-bound phosphate transporting proteins or how their transport function is regulated by intracellular events. One major difficulty has been the unavailability of a highly specific label for the phosphate transporter.


2014 ◽  
Vol 206 (5) ◽  
pp. 579-588 ◽  
Author(s):  
Jeffrey A. Toretsky ◽  
Peter E. Wright

The partitioning of intracellular space beyond membrane-bound organelles can be achieved with collections of proteins that are multivalent or contain low-complexity, intrinsically disordered regions. These proteins can undergo a physical phase change to form functional granules or other entities within the cytoplasm or nucleoplasm that collectively we term “assemblage.” Intrinsically disordered proteins (IDPs) play an important role in forming a subset of cellular assemblages by promoting phase separation. Recent work points to an involvement of assemblages in disease states, indicating that intrinsic disorder and phase transitions should be considered in the development of therapeutics.


2021 ◽  
Author(s):  
Junyi Song ◽  
Liu Chuanyang ◽  
Baoshan Li ◽  
Liangcheng Liu ◽  
LIng Zeng ◽  
...  

Reflectins are membrane-bound proteins located in cephalopods iridocytes, with repeated canonical domains interspersed with cationic linkers. Scientists keep curious about their evolutionary processes, biochemical properties and intracellular functions. Here, by introducing reflectin A1, A2, B1 and C into HEK-293T cells, these proteins were found to phase out from the crowded intracellular milieu, with distinguished localization preferences. Inspired by their programmable block sequences, several truncated reflectin A1 (RfA1) peptides based on repetition of reflectin motifs were designed and transfected into cells. An obvious cyto-/nucleo-plasmic localization preference was once again observed. The dynamic performance of RfA1 derivatives and their analogic behavior between different reflectins suggest a conceivable evolutionary relationship among reflectin proteins. Additionally, a proteomic survey identified biochemical partners which contribute to the phase separation and intracellular localization of RfA1 and its truncations, as well as the close collaboration between RfA1 and the cytoskeleton systems. These findings indicate that liquid-liquid phase separation could be the fundamental mode for reflectins to achieve spatial organization, to cooperate with cytoskeleton during the regulation of reflective coloration. On the other hand, the dynamic behaviors of RfA1 derivatives strongly recommended themselves as programmable molecular tools.


2021 ◽  
Vol 220 (10) ◽  
Author(s):  
Halim Kusumaatmaja ◽  
Alexander I. May ◽  
Roland L. Knorr

Protein-rich droplets, such as stress granules, P-bodies, and the nucleolus, perform diverse and specialized cellular functions. Recent evidence has shown the droplets, which are also known as biomolecular condensates or membrane-less compartments, form by phase separation. Many droplets also contact membrane-bound organelles, thereby functioning in development, intracellular degradation, and organization. These underappreciated interactions have major implications for our fundamental understanding of cells. Starting with a brief introduction to wetting phenomena, we summarize recent progress in the emerging field of droplet–membrane contact. We describe the physical mechanism of droplet–membrane interactions, discuss how these interactions remodel droplets and membranes, and introduce "membrane scaffolding" by liquids as a novel reshaping mechanism, thereby demonstrating that droplet–membrane interactions are elastic wetting phenomena. “Membrane-less” and “membrane-bound” condensates likely represent distinct wetting states that together link phase separation with mechanosensitivity and explain key structures observed during embryogenesis, during autophagy, and at synapses. We therefore contend that droplet wetting on membranes provides a robust and intricate means of intracellular organization.


2021 ◽  
Vol 118 (25) ◽  
pp. e2100099118
Author(s):  
Dan Deviri ◽  
Samuel A. Safran

Maintaining homeostasis is a fundamental characteristic of living systems. In cells, this is contributed to by the assembly of biochemically distinct organelles, many of which are not membrane bound but form by the physical process of liquid–liquid phase separation (LLPS). By analogy with LLPS in binary solutions, cellular LLPS was hypothesized to contribute to homeostasis by facilitating “concentration buffering,” which renders the local protein concentration within the organelle robust to global variations in the average cellular concentration (e.g., due to expression noise). Interestingly, concentration buffering was experimentally measured in vivo in a simple organelle with a single solute, while it was observed not to be obeyed in one with several solutes. Here, we formulate theoretically and solve analytically a physical model of LLPS in a ternary solution of two solutes (ϕ and ψ) that interact both homotypically (ϕ–ϕ attractions) and heterotypically (ϕ–ψ attractions). Our physical theory predicts how the coexisting concentrations in LLPS are related to expression noise and thus, generalizes the concept of concentration buffering to multicomponent systems. This allows us to reconcile the seemingly contradictory experimental observations. Furthermore, we predict that incremental changes of the homotypic and heterotypic interactions among the molecules that undergo LLPS, such as those that are caused by mutations in the genes encoding the proteins, may increase the efficiency of concentration buffering of a given system. Thus, we hypothesize that evolution may optimize concentration buffering as an efficient mechanism to maintain LLPS homeostasis and suggest experimental approaches to test this in different systems.


1981 ◽  
Vol 78 (5) ◽  
pp. 547-568 ◽  
Author(s):  
R W Mercer ◽  
P B Dunham

ATP stimulates Na transport into inside-out vesicles (IOVs) made from human red cell membranes; strophanthidin inhibits the ATP-stimulated transport. The substrates for glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoglycerate kinase (PGK) (glycolytic enzymes bound to the cytoplasmic surface of the red cell membrane) also stimulate Na transport into IOVs without added ATP. The elution of GAPDH from the membranes prevents the stimulation by the substrates, but not by exogenous ATP. Hexokinase plus glucose (agents that promote breakdown of ATP) prevent stimulation of Na transport by exogenous ATP but not by the substrates for GAPDH and PGK. [32P]orthophosphate is incorporated into a membrane-bound organic phosphate compound shown chromatographically to be ATP. The level of membrane-bound ATP is decreased when Na is added, and this decrease is inhibited by strophanthidin. When further synthesis of [32P]ATP is blocked by the addition of unlabeled orthophosphate, all of the membrane-bound [32P]ATP is dissipated by the addition of Na. From these observations it was concluded that membrane-bound glycolytic enzymes synthesize ATP and deposit it in a membrane-associated compartment from which it is used by the Na/K pump.


1987 ◽  
Vol 78 (2-3) ◽  
pp. 105-108 ◽  
Author(s):  
Catherine Rice-Evans ◽  
Erol Baysal

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