Publication: Are non-muscle actin isoforms functionally equivalent?
Authors
Simiczyjew, Aleksandra ; Pietraszek Gremplewicz, Katarzyna ; Mazur, Antonina Joanna ; Nowak, Dorota
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Publisher
Universidad de Murcia. Departamento de Biología Celular e Histología
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DOI
DOI: 10.14670/HH-11-896
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info:eu-repo/semantics/article
Description
Abstract
Actin is highly conserved and it is the most
widespread protein in eukaryotic cells. One of the most
important features of actin, which allows it to have many
different functions, is its ability to polymerize and
interact with many other proteins. Actins are the major
constituent of the actin cytoskeleton, which is an
important system that is involved in various aspects of
cell function, including cell motility, structure, integrity,
regulation of signal transduction and transcription. Six
mammal actin isoforms are highly conserved and share
common functions. Two of them, β and γ non-muscle
actin isoforms, which differ only by four amino acids
located at the N-terminus of the polypeptide chain, are
required for survival and proper cell functioning. We
also summarized data about actbl2, which is suggested
to be a newly discovered isoactin. Here, we review the
current knowledge about tissue-specific expression of
the non-muscle actin isoforms and possible functional
differences between them. We also discuss molecular
tools, which in recent years have allowed for a better
understanding of the role of these proteins in cell
functioning.
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