Crystallization and Preliminary X-Ray Diffraction Analysis of the 190-Å-Long Coiled-Coil Dimerization Domain of the Actin-Bundling Protein Cortexillin I fromDictyostelium discoideum

Burkhard, Peter; Steinmetz, Michel O.; Schulthess, Therese; Landwehr, Ruth; Aebi, Ueli; Kammerer, Richard A.

doi:10.1006/jsbi.1998.4005

Cited by 8 publications

(4 citation statements)

References 21 publications

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“…Based on the crystal structure of this rod, an atomic model indicates that both the N‐ and C‐terminal end segments of the rod region, i.e. residues 227–242 and residues 344–352, are disordered (Burkhard et al ., 1998). The flexibility of these segments may allow the N‐ and C‐terminal domains of cortexillin I to bend and swivel so as to interact with actin filaments optimally.…”

Section: Discussionsupporting

confidence: 56%

“…The crystal structure of this type of domain has been determined in fimbrin (Goldsmith et al ., 1997). The central region consisting of 18 contiguous heptad repeats dimerizes to form a parallel two‐stranded coiled coil (Burkhard et al ., 1998; Steinmetz et al ., 1998). The C‐terminal domain of cortexillin I comprising 92 amino acid residues includes a basic stretch of nine residues at its end, which is reminiscent of a phosphatidylinositol 4,5‐bisphosphate (PIP 2 ) binding motif found in other actin regulatory proteins (Janmey et al ., 1992).…”

Section: Introductionmentioning

confidence: 99%

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Domain analysis of cortexillin I: actin-bundling, PIP2-binding and the rescue of cytokinesis

et al. 1999

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Cortexillins are actin-bundling proteins that form a parallel two-stranded coiled-coil rod. Actin-binding domains of the α-actinin/spectrin type are located N-terminal to the rod and unique sequence elements are found in the C-terminal region. Domain analysis in vitro revealed that the N-terminal domains are not responsible for the strong actin-filament bundling activity of cortexillin I. The strongest activity resides in the C-terminal region. Phosphatidylinositol 4,5-bisphosphate (PIP 2 ) suppresses this bundling activity by binding to a C-terminal nonapeptide sequence. These data define a new PIP 2 -regulated actin-bundling site. In vivo the PIP 2 -binding motif enhances localization of a C-terminal cortexillin I fragment to the cell cortex and improves the rescue of cytokinesis. This motif is not required, however, for translocation to the cleavage furrow. A model is presented proposing that cortexillin translocation is based on a mitotic cycle of polar actin polymerization and midzone depolymerization. Keywords: actin-based membrane flow/cortexillin/green fluorescent protein/mitotic cleavage/phosphatidylinositol 4,5-bisphosphate

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Section: Discussionsupporting

confidence: 56%

Section: Introductionmentioning

confidence: 99%

Domain analysis of cortexillin I: actin-bundling, PIP2-binding and the rescue of cytokinesis

et al. 1999

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“…We have now solved the atomic structure of the 18heptad-repeat coiled-coil domain of the actin-bundling protein cortexillin I from Dictyostelium discoideum [8,14]. The domain extends from amino acid residue 227 to 352 and is predicted to form a two-stranded α-helical coiledcoil dimer [11].…”

Section: Description Of the Overall Structurementioning

confidence: 99%

“…The recombinant cortexillin I coiled-coil oligomerization domain Ir from D. discoideum was prepared as previously described [11] and crystallized according to [14].…”

Section: Enzyme Preparation and Crystallizationmentioning

confidence: 99%

The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges

et al. 2000

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A new twist in the coil: functions of the coiled-coil domain of structural maintenance of chromosome (SMC) proteins

Matityahu

Onn

2017

Curr Genet

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The higher-order organization of chromosomes ensures their stability and functionality. However, the molecular mechanism by which higher order structure is established is poorly understood. Dissecting the activity of the relevant proteins provides information essential for achieving a comprehensive understanding of chromosome structure. Proteins of the structural maintenance of chromosome (SMC) family of ATPases are the core of evolutionary conserved complexes. SMC complexes are involved in regulating genome dynamics and in maintaining genome stability. The structure of all SMC proteins resembles an elongated rod that contains a central coiled-coil domain, a common protein structural motif in which two α-helices twist together. In recent years, the imperative role of the coiled-coil domain to SMC protein activity and regulation has become evident. Here, we discuss recent advances in the function of the SMC coiled coils. We describe the structure of the coiled-coil domain of SMC proteins, modifications and interactions that are mediated by it. Furthermore, we assess the role of the coiled-coil domain in conformational switches of SMC proteins, and in determining the architecture of the SMC dimer. Finally, we review the interplay between mutations in the coiled-coil domain and human disorders. We suggest that distinctive properties of coiled coils of different SMC proteins contribute to their distinct functions. The discussion clarifies the mechanisms underlying the activity of SMC proteins, and advocates future studies to elucidate the function of the SMC coiled coil domain.

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Crystallization and Preliminary X-Ray Diffraction Analysis of the 190-Å-Long Coiled-Coil Dimerization Domain of the Actin-Bundling Protein Cortexillin I fromDictyostelium discoideum

Cited by 8 publications

References 21 publications

Domain analysis of cortexillin I: actin-bundling, PIP2-binding and the rescue of cytokinesis

Domain analysis of cortexillin I: actin-bundling, PIP2-binding and the rescue of cytokinesis

The coiled-coil trigger site of the rod domain of cortexillin I unveils a distinct network of interhelical and intrahelical salt bridges

A new twist in the coil: functions of the coiled-coil domain of structural maintenance of chromosome (SMC) proteins

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