An adapted particle swarm optimization algorithm as a model for exploring premyofibril formation
While the fundamental steps outlining myofibril formation share a similar scheme for different cell and species types, various granular details involved in the development of a functional contractile muscle are not well understood. Many studies of myofibrillogenesis focus on the protein interactions...
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doaj-78e33f5ee029494287dda9db530053ca2020-11-25T04:05:15ZengAIP Publishing LLCAIP Advances2158-32262020-04-01104045126045126-1110.1063/1.5145010An adapted particle swarm optimization algorithm as a model for exploring premyofibril formationWilliam Sherman0Anna Grosberg1Center for Complex Biological Systems, University of California Irvine, Irvine, California 92697-2280, USACenter for Complex Biological Systems, University of California Irvine, Irvine, California 92697-2280, USAWhile the fundamental steps outlining myofibril formation share a similar scheme for different cell and species types, various granular details involved in the development of a functional contractile muscle are not well understood. Many studies of myofibrillogenesis focus on the protein interactions that are involved in myofibril maturation with the assumption that there is a fully formed premyofibril at the start of the process. However, there is little known regarding how the premyofibril is initially constructed. Fortunately, the protein α-actinin, which has been consistently identified throughout the maturation process, is found in premyofibrils as punctate aggregates known as z-bodies. We propose a theoretical model based on the particle swarm optimization algorithm that can explore how these α-actinin clusters form into the patterns observed experimentally. Our algorithm can produce different pattern configurations by manipulating specific parameters that can be related to α-actinin mobility and binding affinity. These patterns, which vary experimentally according to species and muscle cell type, speak to the versatility of α-actinin and demonstrate how its behavior may be altered through interactions with various regulatory, signaling, and metabolic proteins. The results of our simulations invite speculation that premyofibrils can be influenced toward developing different patterns by altering the behavior of individual α-actinin molecules, which may be linked to key differences present in different cell types.http://dx.doi.org/10.1063/1.5145010 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
William Sherman Anna Grosberg |
spellingShingle |
William Sherman Anna Grosberg An adapted particle swarm optimization algorithm as a model for exploring premyofibril formation AIP Advances |
author_facet |
William Sherman Anna Grosberg |
author_sort |
William Sherman |
title |
An adapted particle swarm optimization algorithm as a model for exploring premyofibril formation |
title_short |
An adapted particle swarm optimization algorithm as a model for exploring premyofibril formation |
title_full |
An adapted particle swarm optimization algorithm as a model for exploring premyofibril formation |
title_fullStr |
An adapted particle swarm optimization algorithm as a model for exploring premyofibril formation |
title_full_unstemmed |
An adapted particle swarm optimization algorithm as a model for exploring premyofibril formation |
title_sort |
adapted particle swarm optimization algorithm as a model for exploring premyofibril formation |
publisher |
AIP Publishing LLC |
series |
AIP Advances |
issn |
2158-3226 |
publishDate |
2020-04-01 |
description |
While the fundamental steps outlining myofibril formation share a similar scheme for different cell and species types, various granular details involved in the development of a functional contractile muscle are not well understood. Many studies of myofibrillogenesis focus on the protein interactions that are involved in myofibril maturation with the assumption that there is a fully formed premyofibril at the start of the process. However, there is little known regarding how the premyofibril is initially constructed. Fortunately, the protein α-actinin, which has been consistently identified throughout the maturation process, is found in premyofibrils as punctate aggregates known as z-bodies. We propose a theoretical model based on the particle swarm optimization algorithm that can explore how these α-actinin clusters form into the patterns observed experimentally. Our algorithm can produce different pattern configurations by manipulating specific parameters that can be related to α-actinin mobility and binding affinity. These patterns, which vary experimentally according to species and muscle cell type, speak to the versatility of α-actinin and demonstrate how its behavior may be altered through interactions with various regulatory, signaling, and metabolic proteins. The results of our simulations invite speculation that premyofibrils can be influenced toward developing different patterns by altering the behavior of individual α-actinin molecules, which may be linked to key differences present in different cell types. |
url |
http://dx.doi.org/10.1063/1.5145010 |
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