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Septin structure and filament assembly
#MMPMID28905266
Valadares NF
; d' Muniz Pereira H
; Ulian Araujo AP
; Garratt RC
Biophys Rev
2017[Oct]; 9
(5
): 481-500
PMID28905266
show ga
Septins are able to polymerize into long apolar filaments and have long been
considered to be a component of the cytoskeleton alongside intermediate filaments
(which are also apolar in nature), microtubules and actin filaments (which are
not). Their central guanosine triphosphate (GTP)-binding domain, which is
essential for stabilizing the filament itself, is flanked by N- and C-terminal
domains for which no direct structural information is yet available. In most
cases, physiological filaments are built from a number of different septin
monomers, and in the case of mammalian septins this is most commonly either three
or four. Comprehending the structural basis for the spontaneous assembly of such
filaments requires a deeper understanding of the interfaces between individual
GTP-binding domains than is currently available. Nevertheless, in this review we
will summarize the considerable progress which has been made over the course of
the last 10 years. We will provide a brief description of each structure
determined to date and comment on how it has added to the body of knowledge which
is rapidly growing. Rather than simply repeat data which have already been
described in the literature, as far as is possible we will try to take advantage
of the full set of information now available (mostly derived from human septins)
and draw the reader's attention to some of the details of the structures
themselves and the filaments they form which have not be commented on previously.
An additional aim is to clarify some misconceptions.
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