Conservation of the TRAPPII-specific subunits of a Ypt/Rab exchanger complex

<p>Abstract</p> <p>Background</p> <p>Ypt/Rab GTPases and their GEF activators regulate intra-cellular trafficking in all eukaryotic cells. In <it>S. cerivisiae</it>, the modular TRAPP complex acts as a GEF for the Golgi gatekeepers: Ypt1 and the functional p...

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Main Authors: Yoo Eunice, Chen Shu, Cox Randal, Segev Nava
Format: Article
Language:English
Published: BMC 2007-02-01
Series:BMC Evolutionary Biology
Online Access:http://www.biomedcentral.com/1471-2148/7/12
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spelling doaj-bf850f26e381400489ec6fbae1c319a72021-09-02T08:07:26ZengBMCBMC Evolutionary Biology1471-21482007-02-01711210.1186/1471-2148-7-12Conservation of the TRAPPII-specific subunits of a Ypt/Rab exchanger complexYoo EuniceChen ShuCox RandalSegev Nava<p>Abstract</p> <p>Background</p> <p>Ypt/Rab GTPases and their GEF activators regulate intra-cellular trafficking in all eukaryotic cells. In <it>S. cerivisiae</it>, the modular TRAPP complex acts as a GEF for the Golgi gatekeepers: Ypt1 and the functional pair Ypt31/32. While TRAPPI, which acts in early Golgi, is conserved from fungi to animals, not much is known about TRAPPII, which acts in late Golgi and consists of TRAPPI plus three additional subunits.</p> <p>Results</p> <p>Here, we show a phylogenetic analysis of the three TRAPPII-specific subunits. One copy of each of the two essential subunits, Trs120 and Trs130, is present in almost every fully sequenced eukaryotic genome. Moreover, the primary, as well as the predicted secondary, structure of the Trs120- and Trs130-related sequences are conserved from fungi to animals. The mammalian orthologs of Trs120 and Trs130, NIBP and TMEM1, respectively, are candidates for human disorders. Currently, NIBP is implicated in signaling, and TMEM1 is suggested to have trans-membrane domains (TMDs) and to function as a membrane channel. However, we show here that the yeast Trs130 does not function as a trans-membrane protein, and the human TMEM1 does not contain putative TMDs. The non-essential subunit, Trs65, is conserved only among many fungi and some unicellular eukaryotes. Multiple alignment analysis of each TRAPPII-specific subunit revealed conserved domains that include highly conserved amino acids.</p> <p>Conclusion</p> <p>We suggest that the function of both NIBP and TMEM1 in the regulation of intra-cellular trafficking is conserved from yeast to man. The conserved domains and amino acids discovered here can be used for functional analysis that should help to resolve the differences in the assigned functions of these proteins in fungi and animals.</p> http://www.biomedcentral.com/1471-2148/7/12
collection DOAJ
language English
format Article
sources DOAJ
author Yoo Eunice
Chen Shu
Cox Randal
Segev Nava
spellingShingle Yoo Eunice
Chen Shu
Cox Randal
Segev Nava
Conservation of the TRAPPII-specific subunits of a Ypt/Rab exchanger complex
BMC Evolutionary Biology
author_facet Yoo Eunice
Chen Shu
Cox Randal
Segev Nava
author_sort Yoo Eunice
title Conservation of the TRAPPII-specific subunits of a Ypt/Rab exchanger complex
title_short Conservation of the TRAPPII-specific subunits of a Ypt/Rab exchanger complex
title_full Conservation of the TRAPPII-specific subunits of a Ypt/Rab exchanger complex
title_fullStr Conservation of the TRAPPII-specific subunits of a Ypt/Rab exchanger complex
title_full_unstemmed Conservation of the TRAPPII-specific subunits of a Ypt/Rab exchanger complex
title_sort conservation of the trappii-specific subunits of a ypt/rab exchanger complex
publisher BMC
series BMC Evolutionary Biology
issn 1471-2148
publishDate 2007-02-01
description <p>Abstract</p> <p>Background</p> <p>Ypt/Rab GTPases and their GEF activators regulate intra-cellular trafficking in all eukaryotic cells. In <it>S. cerivisiae</it>, the modular TRAPP complex acts as a GEF for the Golgi gatekeepers: Ypt1 and the functional pair Ypt31/32. While TRAPPI, which acts in early Golgi, is conserved from fungi to animals, not much is known about TRAPPII, which acts in late Golgi and consists of TRAPPI plus three additional subunits.</p> <p>Results</p> <p>Here, we show a phylogenetic analysis of the three TRAPPII-specific subunits. One copy of each of the two essential subunits, Trs120 and Trs130, is present in almost every fully sequenced eukaryotic genome. Moreover, the primary, as well as the predicted secondary, structure of the Trs120- and Trs130-related sequences are conserved from fungi to animals. The mammalian orthologs of Trs120 and Trs130, NIBP and TMEM1, respectively, are candidates for human disorders. Currently, NIBP is implicated in signaling, and TMEM1 is suggested to have trans-membrane domains (TMDs) and to function as a membrane channel. However, we show here that the yeast Trs130 does not function as a trans-membrane protein, and the human TMEM1 does not contain putative TMDs. The non-essential subunit, Trs65, is conserved only among many fungi and some unicellular eukaryotes. Multiple alignment analysis of each TRAPPII-specific subunit revealed conserved domains that include highly conserved amino acids.</p> <p>Conclusion</p> <p>We suggest that the function of both NIBP and TMEM1 in the regulation of intra-cellular trafficking is conserved from yeast to man. The conserved domains and amino acids discovered here can be used for functional analysis that should help to resolve the differences in the assigned functions of these proteins in fungi and animals.</p>
url http://www.biomedcentral.com/1471-2148/7/12
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AT coxrandal conservationofthetrappiispecificsubunitsofayptrabexchangercomplex
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