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WASP family proteins: their evolution and its physiological implications.

Veltman DM, Insall RH - Mol. Biol. Cell (2010)

Bottom Line: Finally, each subfamily has a distinctive C motif, indicating that this motif plays a specific role in each subfamily's function, unlike the generic V and A motifs.Our analysis identifies which features are universally conserved, and thus essential, and which are branch-specific modifications.It also shows the WASP family is more widespread and diverse than currently appreciated and unexpectedly biases the physiological role of the Arp2/3 complex toward vesicle traffic.

View Article: PubMed Central - PubMed

Affiliation: Beatson Institute for Cancer Research, Glasgow, United Kingdom.

ABSTRACT
WASP family proteins control actin polymerization by activating the Arp2/3 complex. Several subfamilies exist, but their regulation and physiological roles are not well understood, nor is it even known if all subfamilies have been identified. Our extensive search reveals few novel WASP family proteins. The WASP, WASH, and SCAR/WAVE subfamilies are evolutionarily ancient, with WASH the most universally present, whereas WHAMM/JMY first appears in invertebrates. An unusual Dictyostelium WASP homologue that has lost the WH1 domain has retained its function in clathrin-mediated endocytosis, demonstrating that WASPs can function with a remarkably diverse domain topology. The WASH and SCAR/WAVE regulatory complexes are much more rigidly maintained; their domain topology is highly conserved, and all subunits are present or lost together, showing that the complexes are ancient and functionally interdependent. Finally, each subfamily has a distinctive C motif, indicating that this motif plays a specific role in each subfamily's function, unlike the generic V and A motifs. Our analysis identifies which features are universally conserved, and thus essential, and which are branch-specific modifications. It also shows the WASP family is more widespread and diverse than currently appreciated and unexpectedly biases the physiological role of the Arp2/3 complex toward vesicle traffic.

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Domain topology diagrams of WASH orthologues from several organisms in each kingdom. The WASH homology domain is the largest region on the N-terminus that shows sequence similarity when comparing orthologues from different kingdoms. The regions in between domains show no sequence similarity when comparing orthologues across different kingdoms.
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Figure 6: Domain topology diagrams of WASH orthologues from several organisms in each kingdom. The WASH homology domain is the largest region on the N-terminus that shows sequence similarity when comparing orthologues from different kingdoms. The regions in between domains show no sequence similarity when comparing orthologues across different kingdoms.

Mentions: A domain structure diagram of WASH that was drawn on the basis of a sequence alignment (Supplementary Figure 5) shows that the overall domain topology of WASH homologues from organisms out of all four kingdoms is remarkably similar (Figure 6). The most notable variation on the common theme is the replacement of the VCA domain by a poly-proline region in Trypanosoma. Curiously, Trypanosoma does encode all Arp2/3 complex subunits, but no WASP family proteins other than WASH, which poses the interesting question of how Trypanosoma WASH regulates Arp2/3. Another notable variation on the common theme is the loss of the acidic region in the VCA domains of WASH in land plants such as Physcomitrella and Selaginella. This loss is specific for WASH as all SCAR homologues in land plants have well conserved VCA domains that include the acidic region.


WASP family proteins: their evolution and its physiological implications.

Veltman DM, Insall RH - Mol. Biol. Cell (2010)

Domain topology diagrams of WASH orthologues from several organisms in each kingdom. The WASH homology domain is the largest region on the N-terminus that shows sequence similarity when comparing orthologues from different kingdoms. The regions in between domains show no sequence similarity when comparing orthologues across different kingdoms.
© Copyright Policy
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC2921111&req=5

Figure 6: Domain topology diagrams of WASH orthologues from several organisms in each kingdom. The WASH homology domain is the largest region on the N-terminus that shows sequence similarity when comparing orthologues from different kingdoms. The regions in between domains show no sequence similarity when comparing orthologues across different kingdoms.
Mentions: A domain structure diagram of WASH that was drawn on the basis of a sequence alignment (Supplementary Figure 5) shows that the overall domain topology of WASH homologues from organisms out of all four kingdoms is remarkably similar (Figure 6). The most notable variation on the common theme is the replacement of the VCA domain by a poly-proline region in Trypanosoma. Curiously, Trypanosoma does encode all Arp2/3 complex subunits, but no WASP family proteins other than WASH, which poses the interesting question of how Trypanosoma WASH regulates Arp2/3. Another notable variation on the common theme is the loss of the acidic region in the VCA domains of WASH in land plants such as Physcomitrella and Selaginella. This loss is specific for WASH as all SCAR homologues in land plants have well conserved VCA domains that include the acidic region.

Bottom Line: Finally, each subfamily has a distinctive C motif, indicating that this motif plays a specific role in each subfamily's function, unlike the generic V and A motifs.Our analysis identifies which features are universally conserved, and thus essential, and which are branch-specific modifications.It also shows the WASP family is more widespread and diverse than currently appreciated and unexpectedly biases the physiological role of the Arp2/3 complex toward vesicle traffic.

View Article: PubMed Central - PubMed

Affiliation: Beatson Institute for Cancer Research, Glasgow, United Kingdom.

ABSTRACT
WASP family proteins control actin polymerization by activating the Arp2/3 complex. Several subfamilies exist, but their regulation and physiological roles are not well understood, nor is it even known if all subfamilies have been identified. Our extensive search reveals few novel WASP family proteins. The WASP, WASH, and SCAR/WAVE subfamilies are evolutionarily ancient, with WASH the most universally present, whereas WHAMM/JMY first appears in invertebrates. An unusual Dictyostelium WASP homologue that has lost the WH1 domain has retained its function in clathrin-mediated endocytosis, demonstrating that WASPs can function with a remarkably diverse domain topology. The WASH and SCAR/WAVE regulatory complexes are much more rigidly maintained; their domain topology is highly conserved, and all subunits are present or lost together, showing that the complexes are ancient and functionally interdependent. Finally, each subfamily has a distinctive C motif, indicating that this motif plays a specific role in each subfamily's function, unlike the generic V and A motifs. Our analysis identifies which features are universally conserved, and thus essential, and which are branch-specific modifications. It also shows the WASP family is more widespread and diverse than currently appreciated and unexpectedly biases the physiological role of the Arp2/3 complex toward vesicle traffic.

Show MeSH
Related in: MedlinePlus