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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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Related in: MedlinePlus

The evolutionary origins of WHAMM and JMY proteins. (A) Full-length WHAMM/JMY protein sequences from indicated organisms were aligned in ClustalX, and a distance tree was calculated from the results. Bootstrap values (1000 trials) are given for the branches that separate the different colored groups. (B) Schematic showing the most likely chronological order of the mutation of the C-terminal phenylalanine and the gene duplication of WHAMY, based on the phylogenetic tree in A. The F indicates the presence of a phenylalanine near the C-terminus, and W indicates the presence of a tryptophan at this position.
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Figure 7: The evolutionary origins of WHAMM and JMY proteins. (A) Full-length WHAMM/JMY protein sequences from indicated organisms were aligned in ClustalX, and a distance tree was calculated from the results. Bootstrap values (1000 trials) are given for the branches that separate the different colored groups. (B) Schematic showing the most likely chronological order of the mutation of the C-terminal phenylalanine and the gene duplication of WHAMY, based on the phylogenetic tree in A. The F indicates the presence of a phenylalanine near the C-terminus, and W indicates the presence of a tryptophan at this position.

Mentions: An alignment and a phylogenetic tree were generated from the identified WHAMM/JMY sequences (Figure 7). All invertebrate homologues group together on a separate branch, distinct from vertebrate WHAMM and JMY, indicating that the ancestral gene first evolved in invertebrates and that the split between the present day WHAMM and JMY occurred later at the onset of vertebrates. Because the invertebrate homologues are equally similar to WHAMM and JMY, we term this group WHAMY.


WASP family proteins: their evolution and its physiological implications.

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

The evolutionary origins of WHAMM and JMY proteins. (A) Full-length WHAMM/JMY protein sequences from indicated organisms were aligned in ClustalX, and a distance tree was calculated from the results. Bootstrap values (1000 trials) are given for the branches that separate the different colored groups. (B) Schematic showing the most likely chronological order of the mutation of the C-terminal phenylalanine and the gene duplication of WHAMY, based on the phylogenetic tree in A. The F indicates the presence of a phenylalanine near the C-terminus, and W indicates the presence of a tryptophan at this position.
© Copyright Policy
Related In: Results  -  Collection

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

Figure 7: The evolutionary origins of WHAMM and JMY proteins. (A) Full-length WHAMM/JMY protein sequences from indicated organisms were aligned in ClustalX, and a distance tree was calculated from the results. Bootstrap values (1000 trials) are given for the branches that separate the different colored groups. (B) Schematic showing the most likely chronological order of the mutation of the C-terminal phenylalanine and the gene duplication of WHAMY, based on the phylogenetic tree in A. The F indicates the presence of a phenylalanine near the C-terminus, and W indicates the presence of a tryptophan at this position.
Mentions: An alignment and a phylogenetic tree were generated from the identified WHAMM/JMY sequences (Figure 7). All invertebrate homologues group together on a separate branch, distinct from vertebrate WHAMM and JMY, indicating that the ancestral gene first evolved in invertebrates and that the split between the present day WHAMM and JMY occurred later at the onset of vertebrates. Because the invertebrate homologues are equally similar to WHAMM and JMY, we term this group WHAMY.

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