A comparative sequence analysis reveals a common GBD/FH3-FH1-FH2-DAD architecture in formins from Dictyostelium, fungi and metazoa

Rivero, Francisco; Muramoto, Tetsuya; Meyer, Ann; Urushihara, Hideko; Uyeda, Taro Q.P.; Kitayama, Chikako

doi:10.1186/1471-2164-6-28

Cited by 79 publications

(65 citation statements)

References 48 publications

(81 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The mammalian mDia formin proteins constitute a subfamily of Rho GTPase-binding formin homology (FH) proteins [12,13]. The mDia formins nucleate and assemble unbranched actin structures, and therefore are implicated in numerous actin-based cellular functions, including cytokinesis, cell morphogenesis, cell polarity and cell migration.…”

Section: Regulating Chromosome Alignmentmentioning

confidence: 99%

FORMIN a link between kinetochores and microtubule ends

Mao

2011

Trends in Cell Biology

View full text Add to dashboard Cite

The mammalian diaphanous-related (mDia) formin proteins are well known for their actin-nucleation and filament-elongation activities in mediating actin dynamics. They also directly bind to microtubules and regulate microtubule stabilization at the leading edge of the cell during cell migration. Recently, the formin mDia3 was shown to associate with the kinetochore and to contribute to metaphase chromosome alignment, a process in which kinetochores form stable attachments with growing and shrinking microtubules. We suggest that the formin mDia3 could contribute to the regulation of kinetochore-bound microtubule dynamics, in coordination with attachment via its own microtubule-binding activity, as well as via its interaction with the tip-tracker EB1 (end-binding protein 1).

show abstract

Section: Regulating Chromosome Alignmentmentioning

confidence: 99%

FORMIN a link between kinetochores and microtubule ends

Mao

2011

Trends in Cell Biology

View full text Add to dashboard Cite

show abstract

“…The position of non-yeast fungi was not resolved, and the yeast formins were the outgroup of all taxonomic groups including plants. Rivero et al resolved the formin subfamilies but did not find sufficient bootstrap support for defining the relationship among them 6 . Out of the fungi genomes, only the yeast formins were included, which built a clade on their own.…”

Section: Introductionmentioning

confidence: 99%

Formin’ cellular structures

Bogdan

Schultz

Großhans

2013

Communicative & Integrative Biology

View full text Add to dashboard Cite

Members of the Diaphanous (Dia) protein family are key regulators of fundamental actin driven cellular processes, which are conserved from yeast to humans. Researchers have uncovered diverse physiological roles in cell morphology, cell motility, cell polarity, and cell division, which are involved in shaping cells into tissues and organs. The identification of numerous binding partners led to substantial progress in our understanding of the differential functions of Dia proteins. Genetic approaches and new microscopy techniques allow important new insights into their localization, activity, and molecular principles of regulation.

show abstract

“…poly(Q), poly(N), poly(T), and poly(KE)) that are found in front of and within the FH2 domain. Besides ForC, Dictyostelium cells contain nine additional formins, most of which convey to the domain organization of vertebrate Diaphanous-related formins (9,11). The mammalian homologue with the most similar domain organization to ForC is human FHOD1 (3).…”

mentioning

confidence: 99%

Structure, Dynamics, Lipid Binding, and Physiological Relevance of the Putative GTPase-binding Domain of Dictyostelium Formin C

Dames

Junemann

Sass

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

Dictyostelium Formin C (ForC) is involved in the regulation of local actin cytoskeleton reorganization (e.g. during cellular adhesion or migration). ForC contains formin homology 2 and 3 (FH2 and -3) domains and an N-terminal putative GTPase-binding domain (GBD) but lacks a canonical FH1 region. To better understand the role of the GBD, its structure, dynamics, lipid-binding properties, and cellular functions were analyzed by NMR and CD spectroscopy and by in vivo fluorescence microscopy. Moreover, the program CS-Rosetta was tested for the structure prediction based on chemical shift data only. The ForC GBD adopts an ubiquitinlike ␣/␤-roll fold with an unusually long loop between ␤-strands 1 and 2. Based on the lipid-binding data, the presence of DPC micelles induces the formation of ␣-helical secondary structure and a rearrangement of the tertiary structure. Lipid-binding studies with a mutant protein and a peptide suggest that the ␤1-␤2 loop is not relevant for these conformational changes. Whereas small amounts of negatively charged phosphoinositides (1,2-dioctanoyl-sn-glycero-3-(phosphoinositol 4,5-bisphosphate) and 1,2-dihexanoyl-sn-glycero-3-(phosphoinositol 3,4,5-trisphosphate)) lower the micelle concentration necessary to induce the observed spectral changes, other negatively charged phospholipids (1,2-dihexanoyl-sn-glycero-3-(phospho-L-serine) and 1,2-dihexanoyl-snglycero-3-phospho-(1 -rac-glycerol)) had no such effect. Interestingly, bicelles and micelles composed of diacylphosphocholines had no effect on the GBD structure. Our data suggest a model in which part of the large positively charged surface area of the GBD mediates localization to specific membrane patches, thereby regulating interactions with signaling proteins. Our cellular localization studies show that both the GBD and the FH3 domain are required for ForC targeting to cell-cell contacts and early phagocytic cups and macropinosomes.Formins are widely expressed multidomain proteins that regulate the spatial and temporal organization of the actin and microtubule cytoskeleton, thereby affecting important cellular functions, such as cytokinesis and cell-cell adhesion (1-3). The defining element is the ϳ400-amino acid-encompassing "formin homology 2" (FH2) 2 domain that can tightly associate with the barbed end of elongating actin filaments (4). In nearly all formins, the FH2 domain is preceded by a prolinerich "formin homology 1" (FH1) region that varies in length and the number of binding sites for profilin and that is used to recruit profilin-actin complexes for filament elongation. The influence of the FH2 domain on the rate of filament elongation depends on the length and composition of the FH1 region and the connecting linker (2, 4, 5). Most formins contain additional regulatory domains. The N-terminal "formin homology 3" (FH3) domain mediates interactions with autoinhibitory regulatory elements in the C terminus as well as with other formin regulators. The FH3 domain can be further divided into functional subdomains, such as an armadill...

show abstract

A comparative sequence analysis reveals a common GBD/FH3-FH1-FH2-DAD architecture in formins from Dictyostelium, fungi and metazoa

Cited by 79 publications

References 48 publications

FORMIN a link between kinetochores and microtubule ends

FORMIN a link between kinetochores and microtubule ends

Formin’ cellular structures

Structure, Dynamics, Lipid Binding, and Physiological Relevance of the Putative GTPase-binding Domain of Dictyostelium Formin C

Contact Info

Product

Resources

About