scholarly journals Developmental formation of a diffusion barrier in the axonal initial segment membrane of the neuron ; a single molecule approach.

2001 ◽  
Vol 41 (supplement) ◽  
pp. S121
Author(s):  
C. Nakada ◽  
Kenneth Ritchie ◽  
T. Fujiwara ◽  
Y. Hotta ◽  
R. Iino ◽  
...  
Keyword(s):  
Single Molecule ◽  
Diffusion Barrier ◽  
Initial Segment ◽  
Axonal Initial Segment

scholarly journals Developmental formation of a diffusion barrier in the plasma membrane of the axonal initial segment : single lipid molecule approach

2000 ◽  
Vol 40 (supplement) ◽  
pp. S212
Author(s):  
C. Nakada ◽  
M. Nozaki ◽  
H. Yamashita ◽  
K. Yamaguchi ◽  
Ken Ritchie ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Diffusion Barrier ◽  
Initial Segment ◽  
Lipid Molecule ◽  
Axonal Initial Segment

scholarly journals Formation mechanism of a diffusion barrier in the initial segment membrane of the neuron as studied by single molecule techniques

2001 ◽  
Vol 41 (supplement) ◽  
pp. S28
Author(s):  
C. Nakada ◽  
Kenneth Ritchie ◽  
T. Fujiwara ◽  
Y. Hotta ◽  
R. Iino ◽  
...  
Keyword(s):  
Formation Mechanism ◽  
Single Molecule ◽  
Diffusion Barrier ◽  
Initial Segment

scholarly journals Axonal spectrins: All-purpose fences

2013 ◽  
Vol 203 (3) ◽  
pp. 381-383 ◽  
Author(s):  
Yael Eshed-Eisenbach ◽  
Elior Peles
Keyword(s):  
Adhesion Molecules ◽  
Diffusion Barrier ◽  
Initial Segment ◽  
Nodes Of Ranvier ◽  
Myelinated Axons ◽  
Membrane Cytoskeleton ◽  
Cell Biol ◽  
Axonal Initial Segment ◽  
Membrane Barrier

A membrane barrier important for assembly of the nodes of Ranvier is found at the paranodal junction. This junction is comprised of axonal and glial adhesion molecules linked to the axonal actin–spectrin membrane cytoskeleton through specific adaptors. In this issue, Zhang et al. (2013. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201308116) show that axonal βII spectrin maintains the diffusion barrier at the paranodal junction. Thus, βII spectrin serves to compartmentalize the membrane of myelinated axons at specific locations that are determined either intrinsically (i.e., at the axonal initial segment), or by axoglial contacts (i.e., at the paranodal junction).

scholarly journals Ankyrin G restricts ion channel diffusion at the axonal initial segment before the establishment of the diffusion barrier

2010 ◽  
Vol 191 (2) ◽  
pp. 383-395 ◽  
Author(s):  
Anna Brachet ◽  
Christophe Leterrier ◽  
Marie Irondelle ◽  
Marie-Pierre Fache ◽  
Victor Racine ◽  
...  
Keyword(s):  
Ion Channels ◽  
Ion Channel ◽  
Diffusion Barrier ◽  
Hippocampal Neurons ◽  
Initial Segment ◽  
Specific Binding ◽  
Single Particle Tracking ◽  
Binding Motif ◽  
Ankyrin G ◽  
Axonal Initial Segment

In mammalian neurons, the precise accumulation of sodium channels at the axonal initial segment (AIS) ensures action potential initiation. This accumulation precedes the immobilization of membrane proteins and lipids by a diffusion barrier at the AIS. Using single-particle tracking, we measured the mobility of a chimeric ion channel bearing the ankyrin-binding motif of the Nav1.2 sodium channel. We found that ankyrin G (ankG) limits membrane diffusion of ion channels when coexpressed in neuroblastoma cells. Site-directed mutants with decreased affinity for ankG exhibit increased diffusion speeds. In immature hippocampal neurons, we demonstrated that ion channel immobilization by ankG is regulated by protein kinase CK2 and occurs as soon as ankG accumulates at the AIS of elongating axons. Once the diffusion barrier is formed, ankG is still required to stabilize ion channels. In conclusion, our findings indicate that specific binding to ankG constitutes the initial step for Nav channel immobilization at the AIS membrane and precedes the establishment of the diffusion barrier.

scholarly journals Ca2+ entry through NaV channels generates submillisecond axonal Ca2+ signaling

eLife ◽  
2020 ◽  
Vol 9 ◽  
Author(s):  
Naomi AK Hanemaaijer ◽  
Marko A Popovic ◽  
Xante Wilders ◽  
Sara Grasman ◽  
Oriol Pavón Arocas ◽  
...  
Keyword(s):  
Calcium Channels ◽  
High Speed ◽  
Initial Segment ◽  
Hek 293 ◽  
Voltage Gated ◽  
Voltage Gated Calcium Channels ◽  
293 Cells ◽  
Axonal Initial Segment ◽  
Nav Channels ◽  
Activity Dependent

Calcium ions (Ca2+) are essential for many cellular signaling mechanisms and enter the cytosol mostly through voltage-gated calcium channels. Here, using high-speed Ca2+ imaging up to 20 kHz in the rat layer five pyramidal neuron axon we found that activity-dependent intracellular calcium concentration ([Ca2+]i) in the axonal initial segment was only partially dependent on voltage-gated calcium channels. Instead, [Ca2+]i changes were sensitive to the specific voltage-gated sodium (NaV) channel blocker tetrodotoxin. Consistent with the conjecture that Ca2+ enters through the NaV channel pore, the optically resolved ICa in the axon initial segment overlapped with the activation kinetics of NaV channels and heterologous expression of NaV1.2 in HEK-293 cells revealed a tetrodotoxin-sensitive [Ca2+]i rise. Finally, computational simulations predicted that axonal [Ca2+]i transients reflect a 0.4% Ca2+ conductivity of NaV channels. The findings indicate that Ca2+ permeation through NaV channels provides a submillisecond rapid entry route in NaV-enriched domains of mammalian axons.

scholarly journals Altered action potential waveform and shorter axonal initial segment in hiPSC-derived motor neurons with mutations in VRK1

2022 ◽  
pp. 105609
Author(s):  
Rémi Bos ◽  
Khalil Rihan ◽  
Patrice Quintana ◽  
Lara El-Bazzal ◽  
Nathalie Bernard-Marissal ◽  
...  
Keyword(s):  
Action Potential ◽  
Motor Neurons ◽  
Initial Segment ◽  
Axonal Initial Segment ◽  
Action Potential Waveform ◽  
Potential Waveform

scholarly journals LS3A1 Diffusion barrier in the neuronal cell membrane : a single molecule study

2002 ◽  
Vol 42 (supplement2) ◽  
pp. S223
Author(s):  
C. Nakada ◽  
Kenneth Ritchie ◽  
T. Fujiwara ◽  
M. Nakamura ◽  
Y. Oba ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Single Molecule ◽  
Diffusion Barrier ◽  
Neuronal Cell

scholarly journals BBSome trains remove activated GPCRs from cilia by enabling passage through the transition zone

2018 ◽  
Vol 217 (5) ◽  
pp. 1847-1868 ◽  
Author(s):  
Fan Ye ◽  
Andrew R. Nager ◽  
Maxence V. Nachury
Keyword(s):  
Transition Zone ◽  
Single Molecule ◽  
Diffusion Barrier ◽  
Diffusion Barriers ◽  
G Protein Coupled Receptors ◽  
Lateral Transport ◽  
Step Process ◽  
Signaling Receptors ◽  
Guanosine Triphosphatase ◽  
G Protein Coupled

A diffusion barrier at the transition zone enables the compartmentalization of signaling molecules by cilia. The BBSome and the small guanosine triphosphatase Arl6, which triggers BBSome coat polymerization, are required for the exit of activated signaling receptors from cilia, but how diffusion barriers are crossed when membrane proteins exit cilia remains to be determined. In this study, we found that activation of the ciliary G protein–coupled receptors (GPCRs) Smoothened and SSTR3 drove the Arl6-dependent assembly of large, highly processive, and cargo-laden retrograde BBSome trains. Single-molecule imaging revealed that the assembly of BBSome trains enables the lateral transport of ciliary GPCRs across the transition zone. However, the removal of activated GPCRs from cilia was inefficient because a second periciliary diffusion barrier was infrequently crossed. We conclude that exit from cilia is a two-step process in which BBSome/Arl6 trains first move activated GPCRs through the transition zone before a periciliary barrier can be crossed.

scholarly journals BBSome trains remove activated GPCRs from cilia by enabling passage through the transition zone

2017 ◽  
Author(s):  
Fan Ye ◽  
Andrew R. Nager ◽  
Maxence V. Nachury
Keyword(s):  
Transition Zone ◽  
Single Molecule ◽  
Diffusion Barrier ◽  
Small Gtpase ◽  
Single Molecule Imaging ◽  
Lateral Transport ◽  
Step Process ◽  
On Demand ◽  
Gpcr Activation ◽  
Signaling Receptors

AbstractA diffusion barrier at the transition zone enables the compartmentalization of signaling molecules by cilia. The BBSome and the small GTPase Arl6, which triggers BBSome coat polymerization, are required for the exit of activated signaling receptors from cilia, but how diffusion barriers are crossed when membrane proteins exit cilia remains to be determined. Here we found that activation of the ciliary GPCRs Smoothened and SSTR3 drove the Arl6-dependent assembly of large, highly processive and cargo-laden retrograde BBSome trains. Single-molecule imaging revealed that the assembly of BBSome trains enables the lateral transport of ciliary GPCRs across the transition zone. Yet, the removal of activated GPCRs from cilia was inefficient because a second, periciliary diffusion barrier was infrequently crossed. We conclude that exit from cilia is a two-step process in which BBSome/Arl6 trains first moves activated GPCRs through the transition zone before a periciliary barrier can be crossed.SummaryUpon activation, GPCRs must exit cilia for appropriate signal transduction. Using bulk imaging of BBSome and single molecule imaging of GPCRs, Ye et al. demonstrate that retrograde BBSome trains assemble on-demand upon GPCR activation and ferry GPCRs across the transition zone. Yet, ciliary exit often fails because of a second diffusion barrier.

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