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2016 ; 44
(5
): 1339-1345
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WASP family proteins, more than Arp2/3 activators
#MMPMID27911716
Tyler JJ
; Allwood EG
; Ayscough KR
Biochem Soc Trans
2016[Oct]; 44
(5
): 1339-1345
PMID27911716
show ga
Wiskott-Aldrich syndrome protein (WASP) family proteins have been extensively
characterized as factors that promote the nucleation of actin through the
activation of the protein complex Arp2/3. While yeast mostly have a single member
of the family, mammalian cells have at least six different members, often with
multiple isoforms. Members of the family are characterized by a common structure.
Their N-termini are varied and are considered to confer spatial and temporal
regulation of Arp2/3-activating activity, whereas their C-terminal half contains
a polyproline-rich region, one or more WASP homology-2 (WH2) actin-binding
domains and motifs that bind directly to Arp2/3. Recent studies, however,
indicate that the yeast WASP homologue Las17 is able to nucleate actin
independently of Arp2/3 through the function of novel G-actin-binding activities
in its polyproline region. This allows Las17 to generate the mother filaments
that are needed for subsequent Arp2/3 recruitment and activation during the actin
polymerization that drives endocytic invagination in yeast. In this review, we
consider how motifs within the polyproline region of Las17 support nucleation of
actin filaments, and whether similar mechanisms might exist among other family
members.
|Actin Cytoskeleton/metabolism
[MESH]
|Actin-Related Protein 2-3 Complex/genetics/*metabolism
[MESH]
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