Ancient origin of reggie (flotillin), reggie-like, and other lipid-raft proteins: convergent evolution of the SPFH domain
info:eu-repo/classification/ddc/570
0303 health sciences
Sequence Homology, Amino Acid
Protein Conformation
Molecular Sequence Data
Membrane Proteins
flotillin
lipid raft
oligomerization
SPFH
Evolution, Molecular
03 medical and health sciences
Membrane Microdomains
evolution
Animals
Humans
Amino Acid Sequence
Reggie
Conserved Sequence
Phylogeny
DOI:
10.1007/s00018-005-5434-3
Publication Date:
2006-01-02T10:08:29Z
AUTHORS (3)
ABSTRACT
Reggies (flotillins) are detergent-resistant microdomains involved in the scaffolding of large heteromeric complexes that signal across the plasma membrane. Based on the presence of an evolutionarily widespread motif, reggies/flotillins have been included within the SPFH (stomatin-prohibitin-flotillin-HflC/K) protein superfamily. To better understand the origin and evolution of reggie/flotillin structure and function, we searched databases for reggie/flotillin and SPFH-like proteins in organisms at the base and beyond the animal kingdom, and used the resulting dataset to compare their structural and functional domains. Our analysis shows that the SPFH grouping has little phylogenetic support, probably due to convergent evolution of its members. We also find that reggie/flotillin homologues are highly conserved among metazoans but are absent in plants, fungi and bacteria, where only proteins with "reggie-like" domains can be found. However, despite their low sequence similarities, reggie/flotillin and "reggie-like" domains appear to subserve related functions, suggesting that their basic biological role was acquired independently during evolution.
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