title: Membrane trafficking in protozoa SNARE proteins, H+-ATPase, actin, and other key players in ciliates.
abstract: Due to their well-defined pathways of vesicle trafficking and manyfold mutants ciliates have served as good model systems. Further studies required the development of databases, now available for Paramecium and Tetrahymena. A variety of key players have been identified and characterized based on BLAST search, domain analysis, localization, and gene-silencing studies. They include NSF (N-ethylmaleimide sensitive factor), SNAREs (soluble NSF attachment protein [SNAP] receptors), the H(+)-ATPase (V-ATPase) and actin, while Arf (ADP-ribosylation factor) and Rab-type small GTPases, COPs (coatamer proteins) and many others remain to be elucidated. The number of SNAREs, H(+)-ATPase subunits, and actins ever found within one cell type are unexpectedly high and most of the manifold vesicle types seem to be endowed with specific molecular components pertinent to trafficking. As in higher eukaryotes, multifactorial targeting likely occurs. It appears that, in parallel to higher organisms, ciliates have evolved a similar structural and molecular complexity of vesicle trafficking.
authors.affiliation: Department of Biology, University of Konstanz, Konstanz, Germany.
authors.forename: Helmut
authors.initials: H
authors.lastname: Plattner
mesh_terms: D000199:Actins / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D001692:Biological Transport / Q000502:physiology; D002118:Calcium / Q000378:metabolism; D002462:Cell Membrane / Q000378:metabolism*; D016798:Ciliophora / Q000145:classification / Q000166:cytology* / Q000502:physiology*; D004705:Endocytosis / Q000502:physiology; D004721:Endoplasmic Reticulum / Q000378:metabolism / Q000648:ultrastructure; D005089:Exocytosis / Q000502:physiology; D019204:GTP-Binding Proteins / Q000378:metabolism; D006056:Golgi Apparatus / Q000378:metabolism / Q000648:ultrastructure; D006801:Humans; D008561:Membrane Fusion / Q000502:physiology; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010247:Paramecium / Q000166:cytology / Q000502:physiology; D010587:Phagocytosis / Q000502:physiology; D010802:Phylogeny; D011487:Protein Conformation; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D015800:Protozoan Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D050600:SNARE Proteins / Q000378:metabolism*; D013768:Tetrahymena / Q000166:cytology / Q000502:physiology; D022161:Transport Vesicles / Q000378:metabolism
chemical_list: D000199:Actins; D015800:Protozoan Proteins; D050600:SNARE Proteins; D019204:GTP-Binding Proteins; D006180:Proton-Translocating ATPases; D002118:Calcium