ArticleBMC evolutionary biology2007
Multiple domain insertions and losses in the evolution of the Rab prenylation complex.
Article in BMC evolutionary biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 24 citations in OpenAlex.
- Impact of C-terminal truncations in the Arabidopsis Rab escort protein (REP) on REP-Rab interaction and plant fertility.The Plant journal : for cell and molecular biology · 2021Article
- On the Archaeal Origins of Eukaryotes and the Challenges of Inferring Phenotype from Genotype.Trends in cell biology · 2016Review
- Arabidopsis Rab Geranylgeranyltransferases Demonstrate Redundancy and Broad Substrate Specificity in Vitro.The Journal of biological chemistry · 2016Article
- Evolutionary comparison of prenylation pathway in kinetoplastid Leishmania and its sister Leptomonas.BMC evolutionary biology · 2015Article
- Rab geranylgeranyl transferase β subunit is essential for male fertility and tip growth in Arabidopsis.Journal of experimental botany · 2015Article
- Consequences of domain insertion on sequence-structure divergence in a superfold.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The map-1 gene family in root-knot nematodes, Meloidogyne spp.: a set of taxonomically restricted genes specific to clonal species.PloS one · 2012Article
- Rab protein evolution and the history of the eukaryotic endomembrane system.Cellular and molecular life sciences : CMLS · 2010Review
- Modular architecture and evolution of the map-1 gene family in the root-knot nematode Meloidogyne incognita.Molecular genetics and genomics : MGG · 2009Article
- SUPERFAMILY--sophisticated comparative genomics, data mining, visualization and phylogeny.Nucleic acids research · 2009Article
- Structures of RabGGTase-substrate/product complexes provide insights into the evolution of protein prenylation.The EMBO journal · 2008Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundRab proteins are regulators of vesicular trafficking, requiring a lipid modification for proper function, prenylation of C-terminal cysteines. This is catalysed by a complex of a catalytic heterodimer (Rab Geranylgeranyl Transferase - RabGGTase) and an accessory protein (Rab Escort Protein. REP). Components of this complex display domain insertions relative to paralogous proteins. The function of these inserted domains is unclear.
resultsWe profiled the domain architecture of the components of the Rab prenylation complex in evolution. We identified the orthologues of the components of the Rab prenylation machinery in 43 organisms, representing the crown eukaryotic groups. We characterize in detail the domain structure of all these components and the phylogenetic relationships between the individual domains.
conclusionWe found different domain insertions in different taxa, in alpha-subunits of RGGTase and REP. Our results suggest that there were multiple insertions, expansions and contractions in the evolution of this prenylation complex.
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