The actin cytoskeleton orchestra in Entamoeba histolytica.
Actin Cytoskeleton
/ chemistry
Actins
/ classification
Amino Acid Sequence
Calcium-Binding Proteins
/ genetics
Databases, Protein
Entamoeba histolytica
/ classification
Formins
/ classification
Gene Expression
Microfilament Proteins
/ classification
Molecular Sequence Annotation
Multigene Family
Phagocytosis
/ physiology
Phylogeny
Profilins
/ classification
Protein Isoforms
/ classification
Protozoan Proteins
/ classification
Virulence Factors
/ classification
Calponins
actin-binding proteins
characterization
classification
domain architecture
identification
Journal
Proteins
ISSN: 1097-0134
Titre abrégé: Proteins
Pays: United States
ID NLM: 8700181
Informations de publication
Date de publication:
10 2020
10 2020
Historique:
received:
19
02
2020
revised:
17
04
2020
accepted:
27
05
2020
pubmed:
9
6
2020
medline:
7
2
2021
entrez:
8
6
2020
Statut:
ppublish
Résumé
Years of evolution have kept actin conserved throughout various clades of life. It is an essential protein starring in many cellular processes. In a primitive eukaryote named Entamoeba histolytica, actin directs the process of phagocytosis. A finely tuned coordination between various actin-binding proteins (ABPs) choreographs this process and forms one of the virulence factors for this protist pathogen. The ever-expanding world of ABPs always has space to accommodate new and varied types of proteins to the earlier existing repertoire. In this article, we report the identification of 390 ABPs from Entamoeba histolytica. These proteins are part of diverse families that have been known to regulate actin dynamics. Most of the proteins are primarily uncharacterized in this organism; however, this study aims to annotate the ABPs based on their domain arrangements. A unique characteristic about some of the ABPs found is the combination of domains present in them unlike any other reported till date. Calponin domain-containing proteins formed the largest group among all types with 38 proteins, followed by 29 proteins with the infamous BAR domain in them, and 23 proteins belonging to actin-related proteins. The other protein families had a lesser number of members. Presence of exclusive domain arrangements in these proteins could guide us to yet unknown actin regulatory mechanisms prevalent in nature. This article is the first step to unraveling them.
Substances chimiques
Actins
0
Calcium-Binding Proteins
0
Formins
0
Microfilament Proteins
0
Profilins
0
Protein Isoforms
0
Protozoan Proteins
0
Virulence Factors
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
1361-1375Informations de copyright
© 2020 Wiley Periodicals LLC.
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