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Scientists determine
specific areas in protein structure
Science
responsible for inducing infectious nature of multi-complex
Modern
Science
Moreover,
the
cytoskeleton is essentially similar to the
structure of the
human skeletal system in that it provides
structural support
for the cell and gives it shape (Freeman et
al.,
2013).
However, the cytoskeleton also plays a
major role in transporting various materials throughout the entire fluid matrix in the cell
(Freeman et al., 2013). Thus, the cytoskeleton is of utmost importance to the proper growth and
functioning of a cell, especially if that cell is specialized within a multicellular organism.
In this experiment conducted by
Kandel and his colleagues, two
proteins, namely Tia1/Pub1 and Sup35,
were of particular interest not only
because they contained prion-rich
domains but also for the reason that in
their normal state they are associated
with a cells cytoskeleton framework
(Kandel et al., 2014).
Line structures are a visual indication
that aggregation is occurring at the
molecular level (Kandel et al., 2014).
Figure 5B adequately represents the
influence of various prion regions,
found in both Sup35 and Tia1, on the
formation of line structures within the
cytoskeleton (Kandel et al., 2014).
Specifically, it conveys that the entire
N region and amino acids 166-220 in
M region, containing the previously
mentioned glutamine and asparagine
side chains, are both necessary to form
line structures as indicated by the
fluorescent images (Kandel et al.,
2014). These two domains, however,
are not sufficient to produce line
structures,
because
subsequent
fluorescent images depict that one
domain without the other does not
produce line structures in the cytoskeleton (Kandel et al., 2014). This pattern of line formation is
true for Sup35 and Tia1/Pub1 as indicated by the last two fluorescent images of the figure
(Kandel
et
al.,
2014).
This relates back to the process of aggregation by which infectious proteins clump together. In
the case of Tia1/Pub1 and Sup35, which are directly associated with the cells cytoskeleton,
aggregation would drastically disrupt the integrity of the cytoskeleton structure, thereby severely
hindering proper cell growth and functioning (Kandel et al., 2014).
Modern
Science
On a small scale if
a few cells died it would not produce a
noticeable effect on a multicellular organism. However, imagine the drastic complications that
could occur if aggregation were to disrupt cytoskeleton structure of thousands of cells. This
would result in death of tissues which would consequently produce illness in the multicellular
organism, especially observed in various neurodegenerative diseases such as Alzheimers
(Kandel et al., 2014).
New discoveries integrating the research produced by the scientists of Colombia University
could one day identify new remedies for neurodegenerative disorders caused by prions.
References:
Freeman, S., Harrington, M., & Sharp, J. (2013). Biological Science (3rd ed., Vol. 1). Toronto,
Ontario: Pearson Learning Solutions.
Kandel, E., Li, X., Rayman, J., & Derkatch, I. (2014). Functional Role of Tia1/Pub1 and Sup35
Prion Domains: Directing Protein Synthesis Machinery to the Tubulin Cytoskeleton. Molecular
Cell, (55), 305-318.