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Natalies Natalies
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7 years ago
How would neurons have to be different if there were no cytoskeleton to transport neurotransmitters or synthesis enzymes to the presynaptic terminals of axons from their production areas in the cell body?
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Valued Member
7 years ago
Kind of an odd question since without the cytoskeleton the neuron would basically become useless. As you know the ions and neurotransmitters are what communicates between all the neurons without those transmitters each signal would be stuck at the original neuron. There would be no communication. So how they would have to be different? well they would need specific production areas at each presynamptic terminal for each neurotransmitter. Or if you could just have 1 neuron for each specific signal. So you would have one neuron going from the brain all the way down to each separate function. Which still would not ever happen because the neuron still needs those neurotransmitters to synapse on whatever it is talking to. Essentially Idk the answer to your question. Definitely need someone with a neuro background to help you out.
Orthopedic Physical Therapist 
B.S. Kinesiology and Human Performance
DPT
wrote...
6 years ago
Synapses are the junctions where neurons pass signals to other neurons, muscle cells, or gland cells. Most nerve-to-nerve signaling and all known nerve-to-muscle and nerve-to-gland signaling rely on chemical synapses at which the synaptic neuron releases a chemical neurotransmitter that acts on the post-synaptic target cell In this section we discuss the types of molecules that function as transmitters at chemical synapses, their origin and fate, and their effects on post-synaptic cells. Since the capacity of neurotransmitters to impel a reaction relies on upon their official to particular receptors in the post synaptic film, we present the real classes of receptors in this area; singular receptors are inspected in more detail in the following segment. We likewise quickly talk about electric neurotransmitters, which are much rarer, however more straightforward in capacity, than substance neurotransmitters.
wrote...
6 years ago
Neuronal MTs are structurally similar to those found in other eukaryotic cells . The core structure is a polymer of 50- kDa tubulin subunits. Heterodimers of α- and β-tubulin align end to end to form protofilaments, 13 of which join laterally to form a hollow tube with an outer diameter of 25 nm. Examples also exist of MTs with 12 and 14 protofilaments. The α- and β-tubulins are the best known members of a unique protein family, the members of which have significant sequence similarity . There is approximately 40% sequence identity between α- and β-tubulins and even greater identity within the α and β gene subfamilies. Conservation of the primary sequence for tubulins is also high across species so that tubulins from yeast can readily co-assemble with tubulins from human brain. Tubular dimers bind two molecules of GTP and exhibit GTPase activity that is closely linked to assembly and disassembly of MTs. While many questions remain about tubulin and its interactions, the structure of the αβ-tubulin dimer has recently been derived from electron diffraction studies, providing a basis for dissection of the functional architecture of MTs.
Thus, without cytpskeletons the cells would develop other means of transportation and architecture.
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