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The Diversification of the LIM Superclass at the Base of the Metazoa Increased Subcellular Complexity and Promoted Multicellular Specialization

Overview
Journal PLoS One
Date 2012 Mar 23
PMID 22438907
Citations 29
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Abstract

Background: Throughout evolution, the LIM domain has been deployed in many different domain configurations, which has led to the formation of a large and distinct group of proteins. LIM proteins are involved in relaying stimuli received at the cell surface to the nucleus in order to regulate cell structure, motility, and division. Despite their fundamental roles in cellular processes and human disease, little is known about the evolution of the LIM superclass.

Results: We have identified and characterized all known LIM domain-containing proteins in six metazoans and three non-metazoans. In addition, we performed a phylogenetic analysis on all LIM domains and, in the process, have identified a number of novel non-LIM domains and motifs in each of these proteins. Based on these results, we have formalized a classification system for LIM proteins, provided reasonable timing for class and family origin events; and identified lineage-specific loss events. Our analysis is the first detailed description of the full set of LIM proteins from the non-bilaterian species examined in this study.

Conclusion: Six of the 14 LIM classes originated in the stem lineage of the Metazoa. The expansion of the LIM superclass at the base of the Metazoa undoubtedly contributed to the increase in subcellular complexity required for the transition from a unicellular to multicellular lifestyle and, as such, was a critically important event in the history of animal multicellularity.

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References
1.
Zhang Y, Chen K, Guo L, Wu C . Characterization of PINCH-2, a new focal adhesion protein that regulates the PINCH-1-ILK interaction, cell spreading, and migration. J Biol Chem. 2002; 277(41):38328-38. DOI: 10.1074/jbc.M205576200. View

2.
Holaska J, Rais-Bahrami S, Wilson K . Lmo7 is an emerin-binding protein that regulates the transcription of emerin and many other muscle-relevant genes. Hum Mol Genet. 2006; 15(23):3459-72. DOI: 10.1093/hmg/ddl423. View

3.
Jang H, Greenwood J . Glycine-rich region regulates cysteine-rich protein 1 binding to actin cytoskeleton. Biochem Biophys Res Commun. 2009; 380(3):484-8. DOI: 10.1016/j.bbrc.2009.01.125. View

4.
Putnam N, Srivastava M, Hellsten U, Dirks B, Chapman J, Salamov A . Sea anemone genome reveals ancestral eumetazoan gene repertoire and genomic organization. Science. 2007; 317(5834):86-94. DOI: 10.1126/science.1139158. View

5.
Knoll R, Hoshijima M, Hoffman H, Person V, Lorenzen-Schmidt I, Bang M . The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy. Cell. 2003; 111(7):943-55. DOI: 10.1016/s0092-8674(02)01226-6. View