The expanding superfamily of gelsolin homology domain proteins
The gelsolin homology (GH) domain has been found to date exclusively in actin-binding proteins. In humans, three copies of the domain are present in CapG, five copies in supervillin, and six copies each in adseverin, gelsolin, flightless I and the villins: villin, advillin and villin-like protein. C...
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sg-ntu-dr.10356-816612020-03-07T12:18:04Z The expanding superfamily of gelsolin homology domain proteins Ghoshdastider, Umesh Popp, David Burtnick, Leslie D. Robinson, Robert C. School of Biological Sciences actin gelsolin The gelsolin homology (GH) domain has been found to date exclusively in actin-binding proteins. In humans, three copies of the domain are present in CapG, five copies in supervillin, and six copies each in adseverin, gelsolin, flightless I and the villins: villin, advillin and villin-like protein. Caenorhabditis elegans contains a four-GH-domain protein, GSNL-1. These architectures are predicted to have arisen from gene triplication followed by gene duplication to result in the six-domain protein. The subsequent loss of one, two or three domains produced the five-, four-, and three-domain proteins, respectively. Here we conducted BLAST and hidden Markov based searches of UniProt and NCBI databases to identify novel gelsolin domain containing proteins. The variety in architectures suggests that the GH domain has been tested in many molecular constructions during evolution. Of particular note is flightless-like I protein (FLIIL1) from Entamoeba histolytica, which combines a leucine rich repeats (LRR) domain, seven GH domains, and a headpiece domain, thus combining many of the features of flightless I with those of villin or supervillin. As such, the GH domain superfamily appears to have developed along complex routes. The distribution of these proteins was analyzed in the 343 completely sequenced genomes, mapped onto the tree of life, and phylogenetic trees of the proteins were constructed to gain insight into their evolution. ASTAR (Agency for Sci., Tech. and Research, S’pore) 2016-07-04T08:05:26Z 2019-12-06T14:35:45Z 2016-07-04T08:05:26Z 2019-12-06T14:35:45Z 2013 Journal Article Ghoshdastider, U., Popp, D., Burtnick, L. D., & Robinson, R. C. (2013). The expanding superfamily of gelsolin homology domain proteins. Cytoskeleton, 70(11), 775-795. 1949-3584 https://hdl.handle.net/10356/81661 http://hdl.handle.net/10220/40888 10.1002/cm.21149 en Cytoskeleton © 2013 Wiley Periodicals, Inc. |
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actin gelsolin Ghoshdastider, Umesh Popp, David Burtnick, Leslie D. Robinson, Robert C. The expanding superfamily of gelsolin homology domain proteins |
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The gelsolin homology (GH) domain has been found to date exclusively in actin-binding proteins. In humans, three copies of the domain are present in CapG, five copies in supervillin, and six copies each in adseverin, gelsolin, flightless I and the villins: villin, advillin and villin-like protein. Caenorhabditis elegans contains a four-GH-domain protein, GSNL-1. These architectures are predicted to have arisen from gene triplication followed by gene duplication to result in the six-domain protein. The subsequent loss of one, two or three domains produced the five-, four-, and three-domain proteins, respectively. Here we conducted BLAST and hidden Markov based searches of UniProt and NCBI databases to identify novel gelsolin domain containing proteins. The variety in architectures suggests that the GH domain has been tested in many molecular constructions during evolution. Of particular note is flightless-like I protein (FLIIL1) from Entamoeba histolytica, which combines a leucine rich repeats (LRR) domain, seven GH domains, and a headpiece domain, thus combining many of the features of flightless I with those of villin or supervillin. As such, the GH domain superfamily appears to have developed along complex routes. The distribution of these proteins was analyzed in the 343 completely sequenced genomes, mapped onto the tree of life, and phylogenetic trees of the proteins were constructed to gain insight into their evolution. |
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School of Biological Sciences |
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School of Biological Sciences Ghoshdastider, Umesh Popp, David Burtnick, Leslie D. Robinson, Robert C. |
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Article |
author |
Ghoshdastider, Umesh Popp, David Burtnick, Leslie D. Robinson, Robert C. |
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Ghoshdastider, Umesh |
title |
The expanding superfamily of gelsolin homology domain proteins |
title_short |
The expanding superfamily of gelsolin homology domain proteins |
title_full |
The expanding superfamily of gelsolin homology domain proteins |
title_fullStr |
The expanding superfamily of gelsolin homology domain proteins |
title_full_unstemmed |
The expanding superfamily of gelsolin homology domain proteins |
title_sort |
expanding superfamily of gelsolin homology domain proteins |
publishDate |
2016 |
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https://hdl.handle.net/10356/81661 http://hdl.handle.net/10220/40888 |
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1681043830081585152 |