scholarly journals Organization of the axon initial segment: Actin like a fence

2016 ◽  
Vol 215 (1) ◽  
pp. 9-11 ◽  
Author(s):  
Yu-Mei Huang ◽  
Matthew N. Rasband
Keyword(s):  
Particle Tracking ◽  
Single Particle ◽  
High Speed ◽  
Initial Segment ◽  
Single Particle Tracking ◽  
Axon Initial Segment ◽  
Membrane Domains ◽  
Superresolution Microscopy ◽  
Cell Biol ◽  
Actin Rings

What prevents the movement of membrane molecules between axonal and somatodendritic domains is unclear. In this issue, Albrecht et. al. (2016. J. Cell Biol. http://dx.doi.org/10.1083/jcb.201603108) demonstrate via high-speed single-particle tracking and superresolution microscopy that lipid-anchored molecules in the axon initial segment are confined to membrane domains separated by periodically spaced actin rings.

scholarly journals Nanoscopic compartmentalization of membrane protein motion at the axon initial segment

2016 ◽  
Author(s):  
David Albrecht ◽  
Christian M. Winterflood ◽  
Thomas Tschager ◽  
Helge Ewers
Keyword(s):  
Membrane Protein ◽  
Particle Tracking ◽  
Single Particle ◽  
Diffusion Barrier ◽  
High Speed ◽  
Initial Segment ◽  
Single Particle Tracking ◽  
Axon Initial Segment ◽  
Periodic Pattern ◽  
Protein Motion

AbstractThe axon initial segment (AIS) is enriched in specific adaptor, cytoskeletal and transmembrane molecules. During AIS establishment, a membrane diffusion barrier is formed between the axon and the somatodendritic domain. Recently, an axonal periodic pattern of actin, spectrin and ankyrin forming 190 nm distanced, ring-like structures has been discovered. However, whether this structure is related to the diffusion barrier function is unclear.Here, we performed single particle tracking timecourse experiments on hippocampal neurons during AIS development. We analyzed the mobility of lipid-anchored molecules by high-speed single particle tracking and correlated positions of membrane molecules with the nanoscopic organization of the AIS cytoskeleton.We observe a strong reduction in mobility early in AIS development. Membrane protein motion in the AIS plasma membrane is confined to a repetitive pattern of ~190 nm spaced segments along the AIS axis as early as DIV4 and this pattern alternates with actin rings. Our data provide a new model for the mechanism of the AIS diffusion barrier.

scholarly journals Nanoscopic compartmentalization of membrane protein motion at the axon initial segment

2016 ◽  
Vol 215 (1) ◽  
pp. 37-46 ◽  
Author(s):  
David Albrecht ◽  
Christian M. Winterflood ◽  
Mohsen Sadeghi ◽  
Thomas Tschager ◽  
Frank Noé ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Particle Tracking ◽  
Single Particle ◽  
Diffusion Barrier ◽  
Initial Segment ◽  
Time Course ◽  
Single Particle Tracking ◽  
Axon Initial Segment ◽  
Periodic Pattern ◽  
Protein Motion

The axon initial segment (AIS) is enriched in specific adaptor, cytoskeletal, and transmembrane molecules. During AIS establishment, a membrane diffusion barrier is formed between the axonal and somatodendritic domains. Recently, an axonal periodic pattern of actin, spectrin, and ankyrin forming 190-nm-spaced, ring-like structures has been discovered. However, whether this structure is related to the diffusion barrier function is unclear. Here, we performed single-particle tracking time-course experiments on hippocampal neurons during AIS development. We analyzed the mobility of lipid-anchored molecules by high-speed single-particle tracking and correlated positions of membrane molecules with the nanoscopic organization of the AIS cytoskeleton. We observe a strong reduction in mobility early in AIS development. Membrane protein motion in the AIS plasma membrane is confined to a repetitive pattern of ∼190-nm-spaced segments along the AIS axis as early as day in vitro 4, and this pattern alternates with actin rings. Mathematical modeling shows that diffusion barriers between the segments significantly reduce lateral diffusion along the axon.

scholarly journals High-Density Single Particle Tracking on the Plasma Membrane using High-Speed Hyperspectral Imaging

2012 ◽  
Vol 102 (3) ◽  
pp. 581a
Author(s):  
Patrick J. Cutler ◽  
Michael D. Malik ◽  
Sheng Liu ◽  
Jason M. Byars ◽  
Diane S. Lidke ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Hyperspectral Imaging ◽  
Particle Tracking ◽  
Single Particle ◽  
High Speed ◽  
Single Particle Tracking ◽  
High Density

scholarly journals Small stepping motion of processive dynein revealed by load-free high-speed single-particle tracking

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Jun Ando ◽  
Tomohiro Shima ◽  
Riko Kanazawa ◽  
Rieko Shimo-Kon ◽  
Akihiko Nakamura ◽  
...  
Keyword(s):  
Particle Tracking ◽  
Single Particle ◽  
High Speed ◽  
Single Particle Tracking

scholarly journals High-Speed Single-Particle Tracking of GM1 in Model Membranes Reveals Anomalous Diffusion due to Interleaflet Coupling and Molecular Pinning

Nano Letters ◽  
2014 ◽  
Vol 14 (9) ◽  
pp. 5390-5397 ◽  
Author(s):  
Katelyn M. Spillane ◽  
Jaime Ortega-Arroyo ◽  
Gabrielle de Wit ◽  
Christian Eggeling ◽  
Helge Ewers ◽  
...  
Keyword(s):  
Particle Tracking ◽  
Anomalous Diffusion ◽  
Single Particle ◽  
High Speed ◽  
Single Particle Tracking ◽  
Model Membranes

scholarly journals High-throughput single-particle tracking reveals nested membrane nanodomain organization that dictates Ras diffusion and trafficking

2019 ◽  
Author(s):  
Yerim Lee ◽  
Carey Phelps ◽  
Tao Huang ◽  
Barmak Mostofian ◽  
Lei Wu ◽  
...  
Keyword(s):  
High Throughput ◽  
Particle Tracking ◽  
Single Particle ◽  
Single Particle Tracking ◽  
Ras Signaling ◽  
Fast Diffusion ◽  
Membrane Domains ◽  
Spatial Mechanisms ◽  
Insight Into ◽  
Distinct Membrane

AbstractMembrane nanodomains have been implicated in Ras signaling, but what these domains are and how they interact with Ras remain obscure. Using high throughput single particle tracking with photoactivated localization microscopy and detailed trajectory analysis, here we show that distinct membrane domains dictate KRas diffusion and trafficking in U2OS cells. KRas exhibits an immobile state in domains ∼70 nm in size, each embedded in a larger domain (∼200 nm) that confers intermediate mobility, while the rest of the membrane supports fast diffusion. Moreover, KRas is continuously removed from the membrane via the immobile state and replenished to the fast state, likely coupled to internalization and recycling. Importantly, both the diffusion and trafficking properties of KRas remain invariant over a broad range of protein expression levels. Our results reveal how membrane organization dictates KRas diffusion and trafficking and offer insight into how Ras signaling may be regulated through spatial mechanisms.

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