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Neurotransmitters are used by the nervous system to transmit messages between neurons. The abnormal levels of the neurotransmitters may lead to neurological disorders. It is very important to monitor their levels in patients. Herein, we report a polymer nanostructured electrode-enabled electrochemical sensing microchip for detecting dopamine and serotonin. The nanostructures on the electrode can enhance the surface area of the electrode dramatically. As a result, the measured electrical signals increased in comparison with those of an electrochemical sensor with an electrode of a flat surface. It has been found that this microchip can detect neurotransmitters with a level as low as ~120 nM with high specificity and can be used to monitor the dopamine and serotonin in a mixed sample successfully in both static and dynamic conditions. Finally, the real-time measurements of dopamine released from N27-A dopaminergic neural cells using the microchip have been demonstrated. 

Kinesin-mediated transport along microtubules is critical for axon development and health. Mutations in the kinesin Kif21a, or the microtubule subunit β-tubulin, inhibit axon growth and/or maintenance resulting in the eye-movement disorder congenital fibrosis of the extraocular muscles (CFEOM). While most examined CFEOM-causing β-tubulin mutations inhibit kinesin–microtubule interactions, Kif21a mutations activate the motor protein. These contrasting observations have led to opposed models of inhibited or hyperactive Kif21a in CFEOM. We show that, contrary to other CFEOM-causing β-tubulin mutations, R380C enhances kinesin activity. Expression of β-tubulin-R380C increases kinesin-mediated peroxisome transport in S2 cells. The binding frequency, percent motile engagements, run length and plus-end dwell time of Kif21a are also elevated on β-tubulin-R380C compared with wildtype microtubules in vitro. This conserved effect persists across tubulins from multiple species and kinesins from different families. The enhanced activity is independent of tail-mediated kinesin autoinhibition and thus utilizes a mechanism distinct from CFEOM-causing Kif21a mutations. Using molecular dynamics, we visualize how β-tubulin-R380C allosterically alters critical structural elements within the kinesin motor domain, suggesting a basis for the enhanced motility. These findings resolve the disparate models and confirm that inhibited or increased kinesin activity can both contribute to CFEOM. They also demonstrate the microtubule’s role in regulating kinesins and highlight the importance of balanced transport for cellular and organismal health.