scholarly journals Serine–Arginine Protein Kinase SRPK2 Modulates the Assembly of the Active Zone Scaffolding Protein CAST1/ERC2

Cells ◽  
2019 ◽  
Vol 8 (11) ◽  
pp. 1333 ◽  
Author(s):  
Duxan Arancibia ◽  
Matias Lira ◽  
Yocelin Cruz ◽  
Daniela P. Barrera ◽  
Carolina Montenegro-Venegas ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Self Assembly ◽  
Active Zone ◽  
Coiled Coil ◽  
The Self ◽  
Scaffolding Protein ◽  
Drosophila Protein ◽  
Specialized Region ◽  
Presynaptic Assembly ◽  
Self Aggregation

Neurons release neurotransmitters at a specialized region of the presynaptic membrane, the active zone (AZ), where a complex meshwork of proteins organizes the release apparatus. The formation of this proteinaceous cytomatrix at the AZ (CAZ) depends on precise homo- and hetero-oligomerizations of distinct CAZ proteins. The CAZ protein CAST1/ERC2 contains four coiled-coil (CC) domains that interact with other CAZ proteins, but also promote self-assembly, which is an essential step for its integration during AZ formation. The self-assembly and synaptic recruitment of the Drosophila protein Bruchpilot (BRP), a partial homolog of CAST1/ERC2, is modulated by the serine-arginine protein kinase (SRPK79D). Here, we demonstrate that overexpression of the vertebrate SRPK2 regulates the self-assembly of CAST1/ERC2 in HEK293T, SH-SY5Y and HT-22 cells and the CC1 and CC4 domains are involved in this process. Moreover, the isoform SRPK2 forms a complex with CAST1/ERC2 when co-expressed in HEK293T and SH-SY5Y cells. More importantly, SRPK2 is present in brain synaptic fractions and synapses, suggesting that this protein kinase might control the level of self-aggregation of CAST1/ERC2 in synapses, and thereby modulate presynaptic assembly.

scholarly journals Influence of the cis/trans configuration on the supramolecular aggregation of aryltriazoles

2019 ◽  
Vol 15 ◽  
pp. 2881-2888
Author(s):  
Sara Tejera ◽  
Giada Caniglia ◽  
Rosa L Dorta ◽  
Andrea Favero ◽  
Javier González-Platas ◽  
...  
Keyword(s):  
Self Assembly ◽  
Bromine Atom ◽  
The Self ◽  
Stacking Interactions ◽  
Aromatic Rings ◽  
X Ray ◽  
High Degree ◽  
Crystal Packings ◽  
Supramolecular Aggregation ◽  
Self Aggregation

The ability of trans- and cis-1,2-glucopyranosyl and cyclohexyl ditriazoles, synthesized by CuAAC "click" chemistry, to form gels was studied, their physical properties determined, and the self-aggregation behavior investigated by SEM, X-ray, and EDC studies. The results revealed that self-assembly was driven mainly by π–π stacking interactions, in addition to hydrogen bonding, with the aromatic rings adopting a high degree of parallelism, as seen in crystal packings and ECD data. Furthermore, π–bromine interactions between the bromine atom of the aryl substituents and the triazole units might also contribute to an overall stabilization of the supramolecular aggregation of bis(4-bromophenyl)triazoles. The trans or cis spatial disposition of the triazole rings is highly important for gelation, with the cis configuration having higher propensity.

Centrosomal Anchoring of the Protein Kinase CK1δ Mediated by Attachment to the Large, Coiled-coil Scaffolding Protein CG-NAP/AKAP450

2002 ◽  
Vol 322 (4) ◽  
pp. 785-797 ◽  
Author(s):  
James E Sillibourne ◽  
Diane M Milne ◽  
Mikiko Takahashi ◽  
Yoshitaka Ono ◽  
David W Meek
Keyword(s):  
Protein Kinase ◽  
Coiled Coil ◽  
Scaffolding Protein

scholarly journals Biophysical and biochemical properties of Deup1 self-assemblies: a potential driver for deuterosome formation during multiciliogenesis

Biology Open ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. bio056432 ◽  
Author(s):  
Shohei Yamamoto ◽  
Ryoichi Yabuki ◽  
Daiju Kitagawa
Keyword(s):  
Self Assembly ◽  
Large Scale ◽  
Molecular Mechanisms ◽  
Coiled Coil ◽  
Biochemical Properties ◽  
The Self ◽  
Centrosomal Protein ◽  
Biochemical Analyses ◽  
Stable Structures

ABSTRACTThe deuterosome is a non-membranous organelle involved in large-scale centriole amplification during multiciliogenesis. Deuterosomes are specifically assembled during the process of multiciliogenesis. However, the molecular mechanisms underlying deuterosome formation are poorly understood. In this study, we investigated the molecular properties of deuterosome protein 1 (Deup1), an essential protein involved in deuterosome assembly. We found that Deup1 has the ability to self-assemble into macromolecular condensates both in vitro and in cells. The Deup1-containing structures formed in multiciliogenesis and the Deup1 condensates self-assembled in vitro showed low turnover of Deup1, suggesting that Deup1 forms highly stable structures. Our biochemical analyses revealed that an increase of the concentration of Deup1 and a crowded molecular environment both facilitate Deup1 self-assembly. The self-assembly of Deup1 relies on its N-terminal region, which contains multiple coiled coil domains. Using an optogenetic approach, we demonstrated that self-assembly and the C-terminal half of Deup1 were sufficient to spatially compartmentalize centrosomal protein 152 (Cep152) and polo like kinase 4 (Plk4), master components for centriole biogenesis, in the cytoplasm. Collectively, the present data suggest that Deup1 forms the structural core of the deuterosome through self-assembly into stable macromolecular condensates.This article has an associated First Person interview with the first author of the paper.

Polypeptide-engineered physical hydrogels designed from the coiled-coil region of cartilage oligomeric matrix protein for three-dimensional cell culture

2014 ◽  
Vol 2 (20) ◽  
pp. 3123-3132 ◽  
Author(s):  
Ming-Hao Yao ◽  
Jie Yang ◽  
Ming-Shuo Du ◽  
Ji-Tao Song ◽  
Yong Yu ◽  
...  
Keyword(s):  
Cell Culture ◽  
Self Assembly ◽  
Cartilage Oligomeric Matrix Protein ◽  
Matrix Protein ◽  
Three Dimensional ◽  
Coiled Coil ◽  
The Self ◽  
Coiled Coil Region ◽  
Dimensional Cell

A class of physical hydrogels photo-cross-linked from multi-branched photopolymeriized monomers based on the self-assembly of coiled-coil polypeptide P is developed.

scholarly journals Principles Governing the Self-Assembly of Coiled-Coil Protein Nanoparticles

2016 ◽  
Vol 110 (3) ◽  
pp. 646-660 ◽  
Author(s):  
Giuliana Indelicato ◽  
Newton Wahome ◽  
Philippe Ringler ◽  
Shirley A. Müller ◽  
Mu-Ping Nieh ◽  
...  
Keyword(s):  
Self Assembly ◽  
Coiled Coil ◽  
The Self ◽  
Protein Nanoparticles

Metal Ion Assisted Folding and Supramolecular Organization of a De Novo Designed Metalloprotein

2004 ◽  
Vol 57 (1) ◽  
pp. 33 ◽  
Author(s):  
Guido W. M. Vandermeulen ◽  
Christos Tziatzios ◽  
Dieter Schubert ◽  
Philip R. Andres ◽  
Alexander Alexeev ◽  
...  
Keyword(s):  
Protein Folding ◽  
Self Assembly ◽  
Metal Ion ◽  
De Novo ◽  
Coiled Coil ◽  
Coiled Coils ◽  
The Self ◽  
Supramolecular Organization ◽  
Low Concentrations ◽  
The Moment

This paper describes the supramolecular organization of a novel de novo designed metalloprotein, which consists of two N-terminal terpyridine modified coiled-coil protein folding motif sequences held together by an iron(II) ion. The self-assembly of the metalloprotein is the result of the interplay of metal ion complexation and protein folding, and can be manipulated by changes in concentration, temperature, and solvent. At low concentrations, folding and organization of the metalloprotein resembles that of the native coiled-coil peptide. Besides unimeric species, also dimeric and tetrameric metalloprotein assemblies were found. Several indications suggest that at least part of these unimeric species may exist as intramolecularly folded coiled-coils, however, unambiguous proof is lacking at the moment. At higher concentrations, folding and organization is dominated by the large octahedral [FeII(terpy)2] complexes (terpy = 2,2′:6′,2″-terpyridine) and considerable amounts of large, ill-defined aggregates are formed.

The Nature of Rapidly Extracted Phycocyanin from the Blue-Green Alga Plectonema Boryanum

1971 ◽  
Vol 29 ◽  
pp. 366-367
Author(s):  
M. Kessel ◽  
R. MacColl
Keyword(s):  
Self Assembly ◽  
Analytical Ultracentrifugation ◽  
Uranyl Acetate ◽  
The Self ◽  
Major Protein ◽  
Subunit Structure ◽  
Blue Green Alga ◽  
Thin Sections ◽  
Blue Green Algae ◽  
Cacodylate Buffer

The major protein of the blue-green algae is the biliprotein, C-phycocyanin (Amax = 620 nm), which is presumed to exist in the cell in the form of distinct aggregates called phycobilisomes. The self-assembly of C-phycocyanin from monomer to hexamer has been extensively studied, but the proposed next step in the assembly of a phycobilisome, the formation of 19s subunits, is completely unknown. We have used electron microscopy and analytical ultracentrifugation in combination with a method for rapid and gentle extraction of phycocyanin to study its subunit structure and assembly.To establish the existence of phycobilisomes, cells of P. boryanum in the log phase of growth, growing at a light intensity of 200 foot candles, were fixed in 2% glutaraldehyde in 0.1M cacodylate buffer, pH 7.0, for 3 hours at 4°C. The cells were post-fixed in 1% OsO4 in the same buffer overnight. Material was stained for 1 hour in uranyl acetate (1%), dehydrated and embedded in araldite and examined in thin sections.

Interrelationship of the cellular distribution and secretion of regular structure (RS) protein in Bacillus licheniformis nm 105

1992 ◽  
Vol 50 (1) ◽  
pp. 712-713
Author(s):  
Xiaorong Zhu ◽  
Richard McVeigh ◽  
Bijan K. Ghosh
Keyword(s):  
Alkaline Phosphatase ◽  
Bacillus Licheniformis ◽  
Self Assembly ◽  
Gel Electrophoresis ◽  
Culture Supernatant ◽  
Regular Structure ◽  
The Self ◽  
Cellular Distribution ◽  
Structural Protein ◽  
Laboratory Cultures

A mutant of Bacillus licheniformis 749/C, NM 105 exhibits some notable properties, e.g., arrest of alkaline phosphatase secretion and overexpression and hypersecretion of RS protein. Although RS is known to be widely distributed in many microbes, it is rarely found, with a few exceptions, in laboratory cultures of microorganisms. RS protein is a structural protein and has the unusual properties to form aggregate. This characteristic may have been responsible for the self assembly of RS into regular tetragonal structures. Another uncommon characteristic of RS is that enhanced synthesis and secretion which occurs when the cells cease to grow. Assembled RS protein with a tetragonal structure is not seen inside cells at any stage of cell growth including cells in the stationary phase of growth. Gel electrophoresis of the culture supernatant shows a very large amount of RS protein in the stationary culture of the B. licheniformis. It seems, Therefore, that the RS protein is cotranslationally secreted and self assembled on the envelope surface.

Nanoscale Self-Assembly Using Ion and Electron Beam Techniques: A Rapid Review

MRS Advances ◽  
2020 ◽  
Vol 5 (64) ◽  
pp. 3507-3520
Author(s):  
Chunhui Dai ◽  
Kriti Agarwal ◽  
Jeong-Hyun Cho
Keyword(s):  
Electron Beam ◽  
Self Assembly ◽  
Ion Beam ◽  
Three Dimensional ◽  
The Self ◽  
Stress Generation ◽  
Rapid Review ◽  
High Yield ◽  
3D Nanostructures ◽  
Self Assembled

AbstractNanoscale self-assembly, as a technique to transform two-dimensional (2D) planar patterns into three-dimensional (3D) nanoscale architectures, has achieved tremendous success in the past decade. However, an assembly process at nanoscale is easily affected by small unavoidable variations in sample conditions and reaction environment, resulting in a low yield. Recently, in-situ monitored self-assembly based on ion and electron irradiation has stood out as a promising candidate to overcome this limitation. The usage of ion and electron beam allows stress generation and real-time observation simultaneously, which significantly enhances the controllability of self-assembly. This enables the realization of various complex 3D nanostructures with a high yield. The additional dimension of the self-assembled 3D nanostructures opens the possibility to explore novel properties that cannot be demonstrated in 2D planar patterns. Here, we present a rapid review on the recent achievements and challenges in nanoscale self-assembly using electron and ion beam techniques, followed by a discussion of the novel optical properties achieved in the self-assembled 3D nanostructures.

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