scholarly journals When the strategies for cellular selectivity fail. Challenges and surprises in the design and application of fluorescent benzothiadiazole derivatives for mitochondrial staining

2019 ◽  
Vol 6 (14) ◽  
pp. 2371-2384 ◽  
Author(s):  
Pedro H. P. R. Carvalho ◽  
Jose R. Correa ◽  
Karen L. R. Paiva ◽  
Michele Baril ◽  
Daniel F. S. Machado ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Molecular Architecture ◽  
Design Synthesis ◽  
Membrane Staining ◽  
Mitochondrial Staining ◽  
Design And Application ◽  
Unexpected Behavior

Design, synthesis, molecular architecture and the unexpected behavior of fluorescent benzothiadiazole for selective mitochondrial and plasma membrane staining are investigated.

scholarly journals Molecular architecture of the endocytic TPLATE complex

2021 ◽  
Vol 7 (9) ◽  
pp. eabe7999
Author(s):  
Klaas Yperman ◽  
Jie Wang ◽  
Dominique Eeckhout ◽  
Joanna Winkler ◽  
Lam Dai Vu ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Structural Approach ◽  
Eukaryotic Cells ◽  
Molecular Architecture ◽  
Membrane Proteome ◽  
Complex Assembly ◽  
Membrane Interaction ◽  
Structural Insight ◽  
Fresh Insight ◽  
Insight Into

Eukaryotic cells rely on endocytosis to regulate their plasma membrane proteome and lipidome. Most eukaryotic groups, except fungi and animals, have retained the evolutionary ancient TSET complex as an endocytic regulator. Unlike other coatomer complexes, structural insight into TSET is lacking. Here, we reveal the molecular architecture of plant TSET [TPLATE complex (TPC)] using an integrative structural approach. We identify crucial roles for specific TSET subunits in complex assembly and membrane interaction. Our data therefore generate fresh insight into the differences between the hexameric TSET in Dictyostelium and the octameric TPC in plants. Structural elucidation of this ancient adaptor complex represents the missing piece in the coatomer puzzle and vastly advances our functional as well as evolutionary insight into the process of endocytosis.

Four-Color Single-Molecule Imaging with Engineered Tags Resolves the Molecular Architecture of Signaling Complexes in the Plasma Membrane

2021 ◽  
Author(s):  
Junel Sotolongo Bellón ◽  
Oliver Birkholz ◽  
Christian Paolo Richter ◽  
Florian Eull ◽  
Hella Kenneweg ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Single Molecule ◽  
Single Molecule Imaging ◽  
Molecular Architecture

scholarly journals Neuronal junctophilins recruit specific CaV and RyR isoforms to ER-PM junctions and functionally alter CaV2.1 and CaV2.2

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Stefano Perni ◽  
Kurt Beam
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Calcium Channels ◽  
High Voltage ◽  
Low Voltage ◽  
Cytoplasmic Domain ◽  
Inactivation Rate ◽  
Molecular Architecture ◽  
Brain Areas ◽  
Junctional Proteins

Junctions between the endoplasmic reticulum and plasma membrane that are induced by the neuronal junctophilins are of demonstrated importance, but their molecular architecture is still poorly understood and challenging to address in neurons. This is due to the small size of the junctions and the multiple isoforms of candidate junctional proteins in different brain areas. Using colocalization of tagged proteins expressed in tsA201 cells, and electrophysiology, we compared the interactions of JPH3 and JPH4 with different calcium channels. We found that JPH3 and JPH4 caused junctional accumulation of all the tested high-voltage-activated CaV isoforms, but not a low-voltage-activated CaV. Also, JPH3 and JPH4 noticeably modify CaV2.1 and CaV2.2 inactivation rate. RyR3 moderately colocalized at junctions with JPH4, whereas RyR1 and RyR2 did not. By contrast, RyR1 and RyR3 strongly colocalized with JPH3, and RyR2 moderately. Likely contributing to this difference, JPH3 binds to cytoplasmic domain constructs of RyR1 and RyR3, but not of RyR2.

Plasma membrane staining with fluorescent hybrid benzothiadiazole and coumarin derivatives: Tuning the cellular selection by molecular design

2021 ◽  
Vol 186 ◽  
pp. 109005
Author(s):  
Saulo T.A. Passos ◽  
Gisele C. Souza ◽  
Douglas C. Brandão ◽  
Daniel F.S. Machado ◽  
Cesar K. Grisolia ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Molecular Design ◽  
Coumarin Derivatives ◽  
Membrane Staining

scholarly journals Molecular Design of Amphiphilic Plasma Membrane-Targeted Azobenzenes for Nongenetic Optical Stimulation

2021 ◽  
Vol 7 ◽  
Author(s):  
Vito Vurro ◽  
Gaia Bondelli ◽  
Valentina Sesti ◽  
Francesco Lodola ◽  
Giuseppe Maria Paternò ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Chemical Engineering ◽  
Molecular Design ◽  
Biological Properties ◽  
Molecular Architecture ◽  
Structure Property ◽  
Switching Unit ◽  
Key Factor ◽  
New Generation ◽  
End Group

We present a series of cationic membrane-targeted azobenzene molecules, with the aim to understand how variations in molecular architecture influence the relative optical and biological properties. 1,4-Amino-substituted azobenzene was chosen as the switching unit while the number of linked alkyl chains and their cationic end-group were systematically varied. Their photophysics, membrane partitioning, and electrophysiological efficacy were studied. We found that the polar end group is a key-factor determining the interaction with the phospholipid heads in the plasma membrane bilayer and consequently the ability to dimerize. The monosubstituted photoswitch with a pyridinium-terminated alkyl chain was found to be the best candidate for photostimulation. This study provides a structure-property investigation that can guide the chemical engineering of a new generation of molecular photo-actuators.

Regulation by Gibberellins of the Orientation of Cortical Microtubules in Plant Cells

1993 ◽  
Vol 20 (5) ◽  
pp. 461 ◽  
Author(s):  
H Shibaoka
Keyword(s):  
Plasma Membrane ◽  
Cell Expansion ◽  
Plant Cells ◽  
Cellulose Microfibrils ◽  
Molecular Architecture ◽  
Cortical Microtubules ◽  
Microtubule Stability ◽  
The Stability ◽  
The Way

Gibberellins control the direction of expansion of plant cells. They change the orientation of cellulose microfibrils by changing the orientation of cortical microtubules and, hence, the direction of cell expansion. When gibberellins change the orientation of cortical microtubules, they also change their stability. If the way in which gibberellins change the orientation of microtubules is identical to the way in which they change microtubule stability, then studies on the mechanism that regulates this stability should give us some clues to the mechanism that regulates the orientation of microtubules. With this possibility in mind, we undertook a series of studies on the stability of cortical microtubules. These revealed that the association of cortical microtubules with the plasma membrane is an important part of the mechanism for their stabilisation. Gibberellins seem to change the stability of microtubules by affecting their association with the plasma membrane. To study the way in which the gibberellins affect this association, it is necessary to clarify the molecular architecture of the structure that links cortical microtubules with the plasma membrane.

Retromer and sorting nexins in endosomal sorting

2015 ◽  
Vol 43 (1) ◽  
pp. 33-47 ◽  
Author(s):  
Matthew Gallon ◽  
Peter J. Cullen
Keyword(s):  
Plasma Membrane ◽  
Present Article ◽  
Transmembrane Proteins ◽  
Molecular Architecture ◽  
Sorting Nexins ◽  
Endosomal Sorting ◽  
Sorting Nexin ◽  
Cargo Proteins ◽  
Associated Proteins ◽  
Lysosome Related Organelles

The evolutionarily conserved endosomal retromer complex rescues transmembrane proteins from the lysosomal degradative pathway and facilitates their recycling to other cellular compartments. Retromer functions in conjunction with numerous associated proteins, including select members of the sorting nexin (SNX) family. In the present article, we review the molecular architecture and cellular roles of retromer and its various functional partners. The endosomal network is a crucial hub in the trafficking of proteins through the cellular endomembrane system. Transmembrane proteins, here termed cargos, enter endosomes by endocytosis from the plasma membrane or by trafficking from the trans-Golgi network (TGN). Endosomal cargo proteins face one of the two fates: retention in the endosome, leading ultimately to lysosomal degradation or export from the endosome for reuse (‘recycling’). The balance of protein degradation and recycling is crucial to cellular homoeostasis; inappropriate sorting of proteins to either fate leads to cellular dysfunction. Retromer is an endosome-membrane-associated protein complex central to the recycling of many cargo proteins from endosomes, both to the TGN and the plasma membrane (and other specialized compartments, e.g. lysosome-related organelles). Retromer function is reliant on a number of proteins from the SNX family. In the present article, we discuss this inter-relationship and how defects in retromer function are increasingly being linked with human disease.

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