RRC ID 28984
Author Faix J, Steinmetz M, Boves H, Kammerer RA, Lottspeich F, Mintert U, Murphy J, Stock A, Aebi U, Gerisch G.
Title Cortexillins, major determinants of cell shape and size, are actin-bundling proteins with a parallel coiled-coil tail.
Journal Cell
Abstract Cortexillins I and II of D. discoideum constitute a novel subfamily of proteins with actin-binding sites of the alpha-actinin/spectrin type. The C-terminal halves of these dimeric proteins contain a heptad repeat domain by which the two subunits are joined to form a two-stranded, parallel coiled coil, giving rise to a 19 nm tail. The N-terminal domains that encompass a consensus actin-binding sequence are folded into globular heads. Cortexillin-linked actin filaments form preferentially anti-parallel bundles that associate into meshworks. Both cortexillins are enriched in the cortex of locomoting cells, primarily at the anterior and posterior ends. Elimination of the two isoforms by gene disruption gives rise to large, flattened cells with rugged boundaries, portions of which are often connected by thin cytoplasmic bridges. The double-mutant cells are multinucleate owing to a severe impairment of cytokinesis.
Volume 86(4)
Pages 631-42
Published 1996-8-23
DOI 10.1016/s0092-8674(00)80136-1
PII S0092-8674(00)80136-1
PMID 8752217
MeSH Actins / metabolism Amino Acid Sequence Animals Base Sequence Cell Compartmentation Cell Size* DNA Primers / chemistry Dictyostelium Fungal Proteins / physiology Microfilament Proteins / physiology* Microscopy, Electron Molecular Sequence Data Mutagenesis, Insertional Protein Structure, Tertiary Protozoan Proteins Repetitive Sequences, Nucleic Acid Sequence Alignment Sequence Homology, Amino Acid
IF 38.637
Times Cited 143
WOS Category BIOCHEMISTRY & MOLECULAR BIOLOGY CELL BIOLOGY
Resource
Cellular slime molds S00404