Phylogenetic and bioinformatic analysis of gap junction-related proteins, innexins, pannexins and connexins
All multi-cellular animals, including hydra, insects and vertebrates, develop gap junctions, which communicate directly with neighboring cells. Gap junctions consist of protein families called connexins in vertebrates and innexins in invertebrates. Connexins and innexins have no homology in their am...
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Veröffentlicht in: | Biomedical Research 2010, Vol.31(2), pp.133-142 |
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description | All multi-cellular animals, including hydra, insects and vertebrates, develop gap junctions, which communicate directly with neighboring cells. Gap junctions consist of protein families called connexins in vertebrates and innexins in invertebrates. Connexins and innexins have no homology in their amino acid sequence, but both are thought to have some similar characteristics, such as a tetra-membrane-spanning structure, formation of a channel by hexamer, and transmission of small molecules (e.g. ions) to neighboring cells. Pannexins were recently identified as a homolog of innexins in vertebrate genomes. Although pannexins are thought to share the function of intercellular communication with connexins and innexins, there is little information about the relationship among these three protein families of gap junctions. We phylgenetically and bioinformatically examined these protein families and other tetra-membrane-spanning proteins using a database and three analytical softwares. The clades formed by pannexin families do not belong to the species classification but do to paralogs of each member of pannexins. Amino acid sequences of pannexins are closely related to those of innexins but less to those of connexins. These data suggest that innexins and pannexins have a common origin, but the relationship between innexins/pannexins and connexins is as slight as that of other tetra-membrane-spanning members. |
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Gap junctions consist of protein families called connexins in vertebrates and innexins in invertebrates. Connexins and innexins have no homology in their amino acid sequence, but both are thought to have some similar characteristics, such as a tetra-membrane-spanning structure, formation of a channel by hexamer, and transmission of small molecules (e.g. ions) to neighboring cells. Pannexins were recently identified as a homolog of innexins in vertebrate genomes. Although pannexins are thought to share the function of intercellular communication with connexins and innexins, there is little information about the relationship among these three protein families of gap junctions. We phylgenetically and bioinformatically examined these protein families and other tetra-membrane-spanning proteins using a database and three analytical softwares. The clades formed by pannexin families do not belong to the species classification but do to paralogs of each member of pannexins. Amino acid sequences of pannexins are closely related to those of innexins but less to those of connexins. 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Res.</addtitle><description>All multi-cellular animals, including hydra, insects and vertebrates, develop gap junctions, which communicate directly with neighboring cells. Gap junctions consist of protein families called connexins in vertebrates and innexins in invertebrates. Connexins and innexins have no homology in their amino acid sequence, but both are thought to have some similar characteristics, such as a tetra-membrane-spanning structure, formation of a channel by hexamer, and transmission of small molecules (e.g. ions) to neighboring cells. Pannexins were recently identified as a homolog of innexins in vertebrate genomes. Although pannexins are thought to share the function of intercellular communication with connexins and innexins, there is little information about the relationship among these three protein families of gap junctions. We phylgenetically and bioinformatically examined these protein families and other tetra-membrane-spanning proteins using a database and three analytical softwares. The clades formed by pannexin families do not belong to the species classification but do to paralogs of each member of pannexins. Amino acid sequences of pannexins are closely related to those of innexins but less to those of connexins. These data suggest that innexins and pannexins have a common origin, but the relationship between innexins/pannexins and connexins is as slight as that of other tetra-membrane-spanning members.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Botany</subject><subject>Cell Communication - genetics</subject><subject>Connexins - chemistry</subject><subject>Connexins - genetics</subject><subject>Connexins - metabolism</subject><subject>Gap Junctions - chemistry</subject><subject>Gap Junctions - genetics</subject><subject>Gap Junctions - metabolism</subject><subject>Genome</subject><subject>Hydra</subject><subject>Invertebrates - genetics</subject><subject>Invertebrates - metabolism</subject><subject>Vertebrates - genetics</subject><subject>Vertebrates - metabolism</subject><issn>0388-6107</issn><issn>1880-313X</issn><issn>1880-313X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9PHCEUx0nTpm7Vu6dmkh68dFYYmAGOjdG2iYk92KQ3wsBjZZ2FLcwk7n8vOttN6sXL-8H7vG_I-yJ0RvCyaRp80fu4AZsgLylZEkrfoQURAteU0D_v0QJTIeqOYH6EPuW8xqUngn5ERw1mHeaMLNDDr_vdEFcQYPSm0sFWRdMHF9NGzy962GWfq-iqld5W6ymY0cdQJxj0CLbapjiCD_lr5UOAx5dqq_fli6CJ--4EfXB6yHC6z8fo9_XV3eWP-ub2-8_Lbze16Vo61lbKvgEKTmpjsSW8I6bvMe8waa3sNRfMSctcL5kWVjjdc9sa3GHrDBcW6DE6n3XL3_5OkEe18dnAMOgAccpKtqwVstzvTZJT2mJJxTP55RW5jlMqx8mKsI7zjmHJCoVnyqSYcwKntslvdNopgtWzY-rgmKJEFcfKyue98NSXyWHhn0UFuJqBdR71Cg6ATsWfAf5XbOZQhA9zc6-TgkCfAFSrr9s</recordid><startdate>20100101</startdate><enddate>20100101</enddate><creator>Fushiki, Daisuke</creator><creator>Hamada, Yasuo</creator><creator>Yoshimura, Ryoichi</creator><creator>Endo, Yasuhisa</creator><general>Biomedical Research Press</general><general>Japan Science and Technology Agency</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QO</scope><scope>7QP</scope><scope>8FD</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20100101</creationdate><title>Phylogenetic and bioinformatic analysis of gap junction-related proteins, innexins, pannexins and connexins</title><author>Fushiki, Daisuke ; Hamada, Yasuo ; Yoshimura, Ryoichi ; Endo, Yasuhisa</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c653t-d99b2e3ef9acd0d1761cbb076015d9ba784f9d4fb94a8d8fab7d5c060dfc78de3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Botany</topic><topic>Cell Communication - genetics</topic><topic>Connexins - chemistry</topic><topic>Connexins - genetics</topic><topic>Connexins - metabolism</topic><topic>Gap Junctions - chemistry</topic><topic>Gap Junctions - genetics</topic><topic>Gap Junctions - metabolism</topic><topic>Genome</topic><topic>Hydra</topic><topic>Invertebrates - genetics</topic><topic>Invertebrates - metabolism</topic><topic>Vertebrates - genetics</topic><topic>Vertebrates - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fushiki, Daisuke</creatorcontrib><creatorcontrib>Hamada, Yasuo</creatorcontrib><creatorcontrib>Yoshimura, Ryoichi</creatorcontrib><creatorcontrib>Endo, Yasuhisa</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Biotechnology Research Abstracts</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biomedical Research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fushiki, Daisuke</au><au>Hamada, Yasuo</au><au>Yoshimura, Ryoichi</au><au>Endo, Yasuhisa</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phylogenetic and bioinformatic analysis of gap junction-related proteins, innexins, pannexins and connexins</atitle><jtitle>Biomedical Research</jtitle><addtitle>Biomed. 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subjects | Amino Acid Sequence Animals Botany Cell Communication - genetics Connexins - chemistry Connexins - genetics Connexins - metabolism Gap Junctions - chemistry Gap Junctions - genetics Gap Junctions - metabolism Genome Hydra Invertebrates - genetics Invertebrates - metabolism Vertebrates - genetics Vertebrates - metabolism |
title | Phylogenetic and bioinformatic analysis of gap junction-related proteins, innexins, pannexins and connexins |
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