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Pre-metazoan origins and evolution of the cadherin adhesome.

Murray PS, Zaidel-Bar R - Biol Open (2014)

Bottom Line: We found that the transition to multicellularity was accompanied by the appearance of a small number of adaptor proteins, and we show how these proteins may have helped to integrate pre-metazoan sub-networks via PDZ domain-peptide interactions.Finally, we found the increase in network complexity in higher metazoans to have been driven primarily by expansion of paralogs.In summary, our analysis helps to explain how the complex protein network associated with cadherin at adherens junctions first came together in the first metazoan and how it evolved into the even more complex mammalian cadhesome.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA Center of Computational Biology and Bioinformatics, Department of Systems Biology, Columbia University, Irving Cancer Research Center, New York, NY 10032, USA.

No MeSH data available.


Related in: MedlinePlus

Expansion of cadhesome gene families throughout evolution.“Classical” cadherin-like proteins, cadherin-binding adaptors, actin-binding adaptors, and adaptors are portrayed. These categories were divided up into the same groups as the “simplified” cadhesome, except for ACTN1/4/SPTBN1 and the MAGUK proteins, which were more broadly clustered (see Materials and Methods). The total number of members in each group (y-axis) was plotted over evolutionary time (x-axis), as represented by the evolutionary ages of the phyla/kingdoms, which are ordered from left to right by increasing age. The dashed line represents the transition from uni- to multicellularity. Gene families are colored according to the legend.
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f06: Expansion of cadhesome gene families throughout evolution.“Classical” cadherin-like proteins, cadherin-binding adaptors, actin-binding adaptors, and adaptors are portrayed. These categories were divided up into the same groups as the “simplified” cadhesome, except for ACTN1/4/SPTBN1 and the MAGUK proteins, which were more broadly clustered (see Materials and Methods). The total number of members in each group (y-axis) was plotted over evolutionary time (x-axis), as represented by the evolutionary ages of the phyla/kingdoms, which are ordered from left to right by increasing age. The dashed line represents the transition from uni- to multicellularity. Gene families are colored according to the legend.

Mentions: We found that ∼87% (97/112) of the “simplified” cadhesome existed in the most basal metazoa. Fig. 4 shows that only 15 novel proteins or protein families appeared since sponges diverged from the other metazoa, including Tara (TRIOBP), SHROOM3, palladin (PALLD), and paracingulin (CGNL1), all of which are either actin- or myosin-binding proteins. This suggests an increased variety of cytoskeletal attachment. Though only a few novel protein families appeared in higher metazoa, the total number of known cadhesome components nearly doubled, from ∼100 in basal metazoa to ∼170 in vertebrates (supplementary material Fig. S3). To analyze this expansion in more detail, we focused our attention on cadherins, cadherin-binding adaptors, actin-binding adaptors, and other adaptors. Fig. 6 shows the total number of members per group in each phylum, from amoebozoa/apusuzoa to vertebrates. Significant vertebrate expansion is exhibited by all three adaptor groups, including proteins characterized by three LIM domains (LPP, TRIP6, FBLIM1, JUB, and ZYX), which have been implicated in mechano-sensing (Schiller et al., 2011). The most striking example of expansion is experienced by the cadherins. Outside of vertebrates, all metazoa examined have at most three “classical”-like cadherins; within vertebrates there are between 12 and 18 “classical” cadherins of type I and II.


Pre-metazoan origins and evolution of the cadherin adhesome.

Murray PS, Zaidel-Bar R - Biol Open (2014)

Expansion of cadhesome gene families throughout evolution.“Classical” cadherin-like proteins, cadherin-binding adaptors, actin-binding adaptors, and adaptors are portrayed. These categories were divided up into the same groups as the “simplified” cadhesome, except for ACTN1/4/SPTBN1 and the MAGUK proteins, which were more broadly clustered (see Materials and Methods). The total number of members in each group (y-axis) was plotted over evolutionary time (x-axis), as represented by the evolutionary ages of the phyla/kingdoms, which are ordered from left to right by increasing age. The dashed line represents the transition from uni- to multicellularity. Gene families are colored according to the legend.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4265756&req=5

f06: Expansion of cadhesome gene families throughout evolution.“Classical” cadherin-like proteins, cadherin-binding adaptors, actin-binding adaptors, and adaptors are portrayed. These categories were divided up into the same groups as the “simplified” cadhesome, except for ACTN1/4/SPTBN1 and the MAGUK proteins, which were more broadly clustered (see Materials and Methods). The total number of members in each group (y-axis) was plotted over evolutionary time (x-axis), as represented by the evolutionary ages of the phyla/kingdoms, which are ordered from left to right by increasing age. The dashed line represents the transition from uni- to multicellularity. Gene families are colored according to the legend.
Mentions: We found that ∼87% (97/112) of the “simplified” cadhesome existed in the most basal metazoa. Fig. 4 shows that only 15 novel proteins or protein families appeared since sponges diverged from the other metazoa, including Tara (TRIOBP), SHROOM3, palladin (PALLD), and paracingulin (CGNL1), all of which are either actin- or myosin-binding proteins. This suggests an increased variety of cytoskeletal attachment. Though only a few novel protein families appeared in higher metazoa, the total number of known cadhesome components nearly doubled, from ∼100 in basal metazoa to ∼170 in vertebrates (supplementary material Fig. S3). To analyze this expansion in more detail, we focused our attention on cadherins, cadherin-binding adaptors, actin-binding adaptors, and other adaptors. Fig. 6 shows the total number of members per group in each phylum, from amoebozoa/apusuzoa to vertebrates. Significant vertebrate expansion is exhibited by all three adaptor groups, including proteins characterized by three LIM domains (LPP, TRIP6, FBLIM1, JUB, and ZYX), which have been implicated in mechano-sensing (Schiller et al., 2011). The most striking example of expansion is experienced by the cadherins. Outside of vertebrates, all metazoa examined have at most three “classical”-like cadherins; within vertebrates there are between 12 and 18 “classical” cadherins of type I and II.

Bottom Line: We found that the transition to multicellularity was accompanied by the appearance of a small number of adaptor proteins, and we show how these proteins may have helped to integrate pre-metazoan sub-networks via PDZ domain-peptide interactions.Finally, we found the increase in network complexity in higher metazoans to have been driven primarily by expansion of paralogs.In summary, our analysis helps to explain how the complex protein network associated with cadherin at adherens junctions first came together in the first metazoan and how it evolved into the even more complex mammalian cadhesome.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032, USA Center of Computational Biology and Bioinformatics, Department of Systems Biology, Columbia University, Irving Cancer Research Center, New York, NY 10032, USA.

No MeSH data available.


Related in: MedlinePlus