FEZ2 has acquired additional protein interaction partners relative to FEZ1: functional and evolutionary implications.

<h4>Background</h4>The FEZ (fasciculation and elongation protein zeta) family designation was purposed by Bloom and Horvitz by genetic analysis of C. elegans unc-76. Similar human sequences were identified in the expressed sequence tag database as FEZ1 and FEZ2. The unc-76 function is ne...

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Autores principales:	Marcos R Alborghetti, Ariane S Furlan, Jörg Kobarg
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2011
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e6ab85667cfa404fa4aa8c69db03e54a
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spelling	oai:doaj.org-article:e6ab85667cfa404fa4aa8c69db03e54a2021-11-18T06:57:36ZFEZ2 has acquired additional protein interaction partners relative to FEZ1: functional and evolutionary implications.1932-620310.1371/journal.pone.0017426https://doaj.org/article/e6ab85667cfa404fa4aa8c69db03e54a2011-03-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/21408165/pdf/?tool=EBIhttps://doaj.org/toc/1932-6203<h4>Background</h4>The FEZ (fasciculation and elongation protein zeta) family designation was purposed by Bloom and Horvitz by genetic analysis of C. elegans unc-76. Similar human sequences were identified in the expressed sequence tag database as FEZ1 and FEZ2. The unc-76 function is necessary for normal axon fasciculation and is required for axon-axon interactions. Indeed, the loss of UNC-76 function results in defects in axonal transport. The human FEZ1 protein has been shown to rescue defects caused by unc-76 mutations in nematodes, indicating that both UNC-76 and FEZ1 are evolutionarily conserved in their function. Until today, little is known about FEZ2 protein function.<h4>Methodology/principal findings</h4>Using the yeast two-hybrid system we demonstrate here conserved evolutionary features among orthologs and non-conserved features between paralogs of the FEZ family of proteins, by comparing the interactome profiles of the C-terminals of human FEZ1, FEZ2 and UNC-76 from C. elegans. Furthermore, we correlate our data with an analysis of the molecular evolution of the FEZ protein family in the animal kingdom.<h4>Conclusions/significance</h4>We found that FEZ2 interacted with 59 proteins and that of these only 40 interacted with FEZ1. Of the 40 FEZ1 interacting proteins, 36 (90%), also interacted with UNC-76 and none of the 19 FEZ2 specific proteins interacted with FEZ1 or UNC-76. This together with the duplication of unc-76 gene in the ancestral line of chordates suggests that FEZ2 is in the process of acquiring new additional functions. The results provide also an explanation for the dramatic difference between C. elegans and D. melanogaster unc-76 mutants on one hand, which cause serious defects in the nervous system, and the mouse FEZ1 -/- knockout mice on the other, which show no morphological and no strong behavioural phenotype. Likely, the ubiquitously expressed FEZ2 can completely compensate the lack of neuronal FEZ1, since it can interact with all FEZ1 interacting proteins and additional 19 proteins.Marcos R AlborghettiAriane S FurlanJörg KobargPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 6, Iss 3, p e17426 (2011)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Marcos R Alborghetti Ariane S Furlan Jörg Kobarg FEZ2 has acquired additional protein interaction partners relative to FEZ1: functional and evolutionary implications.
description	<h4>Background</h4>The FEZ (fasciculation and elongation protein zeta) family designation was purposed by Bloom and Horvitz by genetic analysis of C. elegans unc-76. Similar human sequences were identified in the expressed sequence tag database as FEZ1 and FEZ2. The unc-76 function is necessary for normal axon fasciculation and is required for axon-axon interactions. Indeed, the loss of UNC-76 function results in defects in axonal transport. The human FEZ1 protein has been shown to rescue defects caused by unc-76 mutations in nematodes, indicating that both UNC-76 and FEZ1 are evolutionarily conserved in their function. Until today, little is known about FEZ2 protein function.<h4>Methodology/principal findings</h4>Using the yeast two-hybrid system we demonstrate here conserved evolutionary features among orthologs and non-conserved features between paralogs of the FEZ family of proteins, by comparing the interactome profiles of the C-terminals of human FEZ1, FEZ2 and UNC-76 from C. elegans. Furthermore, we correlate our data with an analysis of the molecular evolution of the FEZ protein family in the animal kingdom.<h4>Conclusions/significance</h4>We found that FEZ2 interacted with 59 proteins and that of these only 40 interacted with FEZ1. Of the 40 FEZ1 interacting proteins, 36 (90%), also interacted with UNC-76 and none of the 19 FEZ2 specific proteins interacted with FEZ1 or UNC-76. This together with the duplication of unc-76 gene in the ancestral line of chordates suggests that FEZ2 is in the process of acquiring new additional functions. The results provide also an explanation for the dramatic difference between C. elegans and D. melanogaster unc-76 mutants on one hand, which cause serious defects in the nervous system, and the mouse FEZ1 -/- knockout mice on the other, which show no morphological and no strong behavioural phenotype. Likely, the ubiquitously expressed FEZ2 can completely compensate the lack of neuronal FEZ1, since it can interact with all FEZ1 interacting proteins and additional 19 proteins.
format	article
author	Marcos R Alborghetti Ariane S Furlan Jörg Kobarg
author_facet	Marcos R Alborghetti Ariane S Furlan Jörg Kobarg
author_sort	Marcos R Alborghetti
title	FEZ2 has acquired additional protein interaction partners relative to FEZ1: functional and evolutionary implications.
title_short	FEZ2 has acquired additional protein interaction partners relative to FEZ1: functional and evolutionary implications.
title_full	FEZ2 has acquired additional protein interaction partners relative to FEZ1: functional and evolutionary implications.
title_fullStr	FEZ2 has acquired additional protein interaction partners relative to FEZ1: functional and evolutionary implications.
title_full_unstemmed	FEZ2 has acquired additional protein interaction partners relative to FEZ1: functional and evolutionary implications.
title_sort	fez2 has acquired additional protein interaction partners relative to fez1: functional and evolutionary implications.
publisher	Public Library of Science (PLoS)
publishDate	2011
url	https://doaj.org/article/e6ab85667cfa404fa4aa8c69db03e54a
work_keys_str_mv	AT marcosralborghetti fez2hasacquiredadditionalproteininteractionpartnersrelativetofez1functionalandevolutionaryimplications AT arianesfurlan fez2hasacquiredadditionalproteininteractionpartnersrelativetofez1functionalandevolutionaryimplications AT jorgkobarg fez2hasacquiredadditionalproteininteractionpartnersrelativetofez1functionalandevolutionaryimplications
_version_	1718424201700835328

FEZ2 has acquired additional protein interaction partners relative to FEZ1: functional and evolutionary implications.

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