Two related subpellicular cytoskeleton-associated proteins in Trypanosoma brucei stabilize microtubules. 2002

Cécile Vedrenne, and Christiane Giroud, and Derrick R Robinson, and Sébastien Besteiro, and Christophe Bosc, and Frédéric Bringaud, and Théo Baltz
Laboratoire de Parasitologie Moléculaire, Université Victor Segalen de Bordeaux II, Unité Mixte Recherche-5016 Centre National de la Recherche Scientifique, 33076 Bordeaux, France.

The subpellicular microtubules of the trypanosome cytoskeleton are cross-linked to each other and the plasma membrane, creating a cage-like structure. We have isolated, from Trypanosoma brucei, two related low-molecular-weight cytoskeleton-associated proteins (15- and 17-kDa), called CAP15 and CAP17, which are differentially expressed during the life cycle. Immunolabeling shows a corset-like colocalization of both CAPs and tubulin. Western blot and electron microscope analyses show CAP15 and CAP17 labeling on detergent-extracted cytoskeletons. However, the localization of both proteins is restricted to the anterior, microtubule minus, and less dynamic half of the corset. CAP15 and CAP17 share properties of microtubule-associated proteins when expressed in heterologous cells (Chinese hamster ovary and HeLa), colocalization with their microtubules, induction of microtubule bundle formation, cold resistance, and insensitivity to nocodazole. When overexpressed in T. brucei, both CAP15 and CAP17 cover the whole subpellicular corset and induce morphological disorders, cell cycle-based abnormalities, and subsequent asymmetric cytokinesis.

UI MeSH Term Description Entries
D008854 Microscopy, Electron Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen. Electron Microscopy
D008869 Microtubule-Associated Proteins High molecular weight proteins found in the MICROTUBULES of the cytoskeletal system. Under certain conditions they are required for TUBULIN assembly into the microtubules and stabilize the assembled microtubules. Ensconsin,Epithelial MAP, 115 kDa,Epithelial Microtubule-Associate Protein, 115 kDa,MAP4,Microtubule Associated Protein,Microtubule Associated Protein 4,Microtubule Associated Protein 7,Microtubule-Associated Protein,Microtubule-Associated Protein 7,E-MAP-115,MAP1 Microtubule-Associated Protein,MAP2 Microtubule-Associated Protein,MAP3 Microtubule-Associated Protein,Microtubule Associated Proteins,Microtubule-Associated Protein 1,Microtubule-Associated Protein 2,Microtubule-Associated Protein 3,7, Microtubule-Associated Protein,Associated Protein, Microtubule,E MAP 115,Epithelial Microtubule Associate Protein, 115 kDa,MAP1 Microtubule Associated Protein,MAP2 Microtubule Associated Protein,MAP3 Microtubule Associated Protein,Microtubule Associated Protein 1,Microtubule Associated Protein 2,Microtubule Associated Protein 3,Microtubule-Associated Protein, MAP1,Microtubule-Associated Protein, MAP2,Microtubule-Associated Protein, MAP3,Protein 7, Microtubule-Associated,Protein, Microtubule Associated,Protein, Microtubule-Associated
D008870 Microtubules Slender, cylindrical filaments found in the cytoskeleton of plant and animal cells. They are composed of the protein TUBULIN and are influenced by TUBULIN MODULATORS. Microtubule
D008969 Molecular Sequence Data Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories. Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D011994 Recombinant Proteins Proteins prepared by recombinant DNA technology. Biosynthetic Protein,Biosynthetic Proteins,DNA Recombinant Proteins,Recombinant Protein,Proteins, Biosynthetic,Proteins, Recombinant DNA,DNA Proteins, Recombinant,Protein, Biosynthetic,Protein, Recombinant,Proteins, DNA Recombinant,Proteins, Recombinant,Recombinant DNA Proteins,Recombinant Proteins, DNA
D003599 Cytoskeleton The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm. Cytoplasmic Filaments,Cytoskeletal Filaments,Microtrabecular Lattice,Cytoplasmic Filament,Cytoskeletal Filament,Cytoskeletons,Filament, Cytoplasmic,Filament, Cytoskeletal,Filaments, Cytoplasmic,Filaments, Cytoskeletal,Lattice, Microtrabecular,Lattices, Microtrabecular,Microtrabecular Lattices
D004318 Doxycycline A synthetic tetracycline derivative with similar antimicrobial activity. 2-Naphthacenecarboxamide, 4-(dimethylamino)-1,4,4a,5,5a,6,11,12a-octahydro-3,5,10,12,12a-pentahydroxy-6-methyl-1,11-dioxo-, (4S-(4alpha,4aalpha,5alpha,5aalpha,6alpha,12aalpha))-,Alpha-6-Deoxyoxytetracycline,Atridox,BMY-28689,BU-3839T,Doryx,Doxycycline Calcium,Doxycycline Calcium Salt (1:2),Doxycycline Hemiethanolate,Doxycycline Hyclate,Doxycycline Monohydrate,Doxycycline Monohydrochloride, 6-epimer,Doxycycline Monohydrochloride, Dihydrate,Doxycycline Phosphate (1:1),Doxycycline-Chinoin,Hydramycin,Oracea,Periostat,Vibra-Tabs,Vibramycin,Vibramycin Novum,Vibravenos,Alpha 6 Deoxyoxytetracycline,BMY 28689,BMY28689,BU 3839T,BU3839T,Doxycycline Chinoin,Doxycycline Monohydrochloride, 6 epimer,Vibra Tabs
D005407 Flagella A whiplike motility appendage present on the surface cells. Prokaryote flagella are composed of a protein called FLAGELLIN. Bacteria can have a single flagellum, a tuft at one pole, or multiple flagella covering the entire surface. In eukaryotes, flagella are threadlike protoplasmic extensions used to propel flagellates and sperm. Flagella have the same basic structure as CILIA but are longer in proportion to the cell bearing them and present in much smaller numbers. (From King & Stansfield, A Dictionary of Genetics, 4th ed) Flagellum
D006224 Cricetinae A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS. Cricetus,Hamsters,Hamster
D006367 HeLa Cells The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for, among other things, VIRUS CULTIVATION and PRECLINICAL DRUG EVALUATION assays. Cell, HeLa,Cells, HeLa,HeLa Cell

Related Publications

Cécile Vedrenne, and Christiane Giroud, and Derrick R Robinson, and Sébastien Besteiro, and Christophe Bosc, and Frédéric Bringaud, and Théo Baltz
February 1997, Journal of cell science,
Cécile Vedrenne, and Christiane Giroud, and Derrick R Robinson, and Sébastien Besteiro, and Christophe Bosc, and Frédéric Bringaud, and Théo Baltz
March 1987, The Journal of cell biology,
Cécile Vedrenne, and Christiane Giroud, and Derrick R Robinson, and Sébastien Besteiro, and Christophe Bosc, and Frédéric Bringaud, and Théo Baltz
January 1989, Cell motility and the cytoskeleton,
Cécile Vedrenne, and Christiane Giroud, and Derrick R Robinson, and Sébastien Besteiro, and Christophe Bosc, and Frédéric Bringaud, and Théo Baltz
May 2021, PLoS pathogens,
Cécile Vedrenne, and Christiane Giroud, and Derrick R Robinson, and Sébastien Besteiro, and Christophe Bosc, and Frédéric Bringaud, and Théo Baltz
October 2021, Microorganisms,
Cécile Vedrenne, and Christiane Giroud, and Derrick R Robinson, and Sébastien Besteiro, and Christophe Bosc, and Frédéric Bringaud, and Théo Baltz
July 1999, Cell,
Cécile Vedrenne, and Christiane Giroud, and Derrick R Robinson, and Sébastien Besteiro, and Christophe Bosc, and Frédéric Bringaud, and Théo Baltz
July 1989, Microbial pathogenesis,
Cécile Vedrenne, and Christiane Giroud, and Derrick R Robinson, and Sébastien Besteiro, and Christophe Bosc, and Frédéric Bringaud, and Théo Baltz
August 2001, Molecular and biochemical parasitology,
Cécile Vedrenne, and Christiane Giroud, and Derrick R Robinson, and Sébastien Besteiro, and Christophe Bosc, and Frédéric Bringaud, and Théo Baltz
January 2002, Biochemical and biophysical research communications,
Cécile Vedrenne, and Christiane Giroud, and Derrick R Robinson, and Sébastien Besteiro, and Christophe Bosc, and Frédéric Bringaud, and Théo Baltz
March 1993, Molecular and biochemical parasitology,
Copied contents to your clipboard!