Abstract
Axons of neurons are contractile, i.e., they actively maintain a rest tension. However, the spatial origin of this contractility along the axon and the role of the cytoskeleton in generating tension and sustaining rigidity are unknown. Here, using a microfluidic platform, we exposed a small segment of the axons of embryonic Drosophila motor neurons to specific cytoskeletal disruption drugs. We observed that a local actomyosin disruption led to a total loss in axonal tension, with the stiffness of the axon remaining unchanged. A local disruption of microtubules led to a local reduction in bending stiffness, while tension remained unchanged. These observations demonstrated that contractile forces are generated and transferred along the entire length of the axon in a serial fashion. Thus, a local force disruption results in a collapse of tension of the entire axon. This mechanism potentially provides a pathway for rapid tension regulation to facilitate physiological processes that are influenced by axonal tension.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 3133-3139 |
| Number of pages | 7 |
| Journal | Lab on a chip |
| Volume | 19 |
| Issue number | 18 |
| DOIs | |
| State | Published - Jan 1 2019 |
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ASJC Scopus subject areas
- Bioengineering
- Biochemistry
- Chemistry(all)
- Biomedical Engineering
Cite this
A connected cytoskeleton network generates axonal tension in embryonic : Drosophila. / Fan, Anthony; Joy, Md Saddam Hossain; Saif, Taher.
In: Lab on a chip, Vol. 19, No. 18, 01.01.2019, p. 3133-3139.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - A connected cytoskeleton network generates axonal tension in embryonic
T2 - Drosophila
AU - Fan, Anthony
AU - Joy, Md Saddam Hossain
AU - Saif, Taher
PY - 2019/1/1
Y1 - 2019/1/1
N2 - Axons of neurons are contractile, i.e., they actively maintain a rest tension. However, the spatial origin of this contractility along the axon and the role of the cytoskeleton in generating tension and sustaining rigidity are unknown. Here, using a microfluidic platform, we exposed a small segment of the axons of embryonic Drosophila motor neurons to specific cytoskeletal disruption drugs. We observed that a local actomyosin disruption led to a total loss in axonal tension, with the stiffness of the axon remaining unchanged. A local disruption of microtubules led to a local reduction in bending stiffness, while tension remained unchanged. These observations demonstrated that contractile forces are generated and transferred along the entire length of the axon in a serial fashion. Thus, a local force disruption results in a collapse of tension of the entire axon. This mechanism potentially provides a pathway for rapid tension regulation to facilitate physiological processes that are influenced by axonal tension.
AB - Axons of neurons are contractile, i.e., they actively maintain a rest tension. However, the spatial origin of this contractility along the axon and the role of the cytoskeleton in generating tension and sustaining rigidity are unknown. Here, using a microfluidic platform, we exposed a small segment of the axons of embryonic Drosophila motor neurons to specific cytoskeletal disruption drugs. We observed that a local actomyosin disruption led to a total loss in axonal tension, with the stiffness of the axon remaining unchanged. A local disruption of microtubules led to a local reduction in bending stiffness, while tension remained unchanged. These observations demonstrated that contractile forces are generated and transferred along the entire length of the axon in a serial fashion. Thus, a local force disruption results in a collapse of tension of the entire axon. This mechanism potentially provides a pathway for rapid tension regulation to facilitate physiological processes that are influenced by axonal tension.
UR - http://www.scopus.com/inward/record.url?scp=85071998442&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85071998442&partnerID=8YFLogxK
U2 - 10.1039/c9lc00243j
DO - 10.1039/c9lc00243j
M3 - Article
C2 - 31435630
AN - SCOPUS:85071998442
VL - 19
SP - 3133
EP - 3139
JO - Lab on a Chip - Miniaturisation for Chemistry and Biology
JF - Lab on a Chip - Miniaturisation for Chemistry and Biology
SN - 1473-0197
IS - 18
ER -