Cortexillins, major determinants of cell shape and size, are actin-bundling proteins with a parallel coiled-coil tail
Article Abstract:
Dictyostelium discoideum has two cortexillins that are necessary for cell shape maintenance and for regular cytokinesis. Cortexillins I and II of Dictyostelium discoideum differ from the known members of the alpha-actinin/spectrin superfamily because of the presence of a two-stranded coiled-coil tail domain by which two subunits are assembled in a parallel and unstaggered way. The actin-binding sites of the subunits are brought in juxtaposition, which makes possible the cross-linking of actin filaments into bundles. Cortexillins were named as such because they are usually found in the highly motile Dictyostelium cell's cortical region, where actin filaments form high order, variably shaped structures.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
User Contributions:
Comment about this article or add new information about this topic:
Coronin involved in phagocytosis: dynamics of particle-induced relocalization visualized by a green fluorescent protein tag
Article Abstract:
The coronin protein of Dictyostelium discoideum controls phagocytosis of yeast particles. Coronin joined to a green fluorescent protein accumulates in the phagocytotic cups formed after a particle attaches to the cell surface. Coronin is released after the particle is engulfed. The rate of phagocytosis decreases in mutants which lack coronin. Coronin also controls the speed of locomotion. The protein changes signals generated by different activities into cytoskeletal processes. Phagocytosis occurs by a zipper mechanism and is dynamically controlled.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1995
User Contributions:
Comment about this article or add new information about this topic:
The role of tricorn protease and its aminopeptidase-interacting factors in cellular protein degradation
Article Abstract:
Tricorn protease is known to be the primary enzyme of a modular proteolytic system with multicatalytic activity. The mode of cooperation between Tricorn and its interacting factors were examined and two additional factors, F2 and F3, were identified. In relation to these three factors, Tricorn breaks down oligopeptides in a sequential fashion, producing free amino acids. A proteolytic pathway composed of the proteasome, Tricorn, and its interacting factors, F1, F2 and F3, were reconstituted.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1998
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: The microevolution of mouse salivary androgen-binding protein (ABP) paralleled subspeciation of Mus musculus. Reduced female gene flow in the European flat oyster Ostrea edulis
- Abstracts: Cell cycle-dependent polar localization of chromosome partitioning proteins in Caulobacter crescentus. Separation of sister chromatids in mitosis requires the Drosophila pimples product, a protein degraded after the metaphase/anaphase transition
- Abstracts: Inheritance of crippled trifoliolate leaves occurring in interracial crosses of common bean and its relationship with hybrid dwarfism
- Abstracts: Fermentation, purification, and characterization of protective antigen from a recombinant, avirulent strain of Bacillus anthracis
- Abstracts: Black Brant from Alaska staging and wintering in Japan. Ecological consequences of nest site fidelity in black brant