High-resolution Structural Analysis of Mammalian Profilin 2a Complex Formation with Two Physiological Ligands: The Formin Homology 1 Domain of mDia1 and the Proline-rich Domain of VASP

Kursula, Petri; Kursula, Inari; Massimi, Marzia; Song, Young Ho; Downer, J.; Stanley, Will A.; Witke, Walter; Wilmanns, Matthias

doi:10.1016/j.jmb.2007.10.050

Cited by 63 publications

(101 citation statements)

References 96 publications

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“…Although we cannot conclusively determine whether each FH1 domain favors delivery to one actin long-pitch helix over the other, our interpretation of the crystal structure of profilin 2a bound to two contiguous polyproline tracks of formin mDia1 (27) is that binding of profilin-actin to polyproline tracks of the FH1 domain favors delivery of actin to the nearest long-pitch helix. The presence of two FH1 domains therefore facilitates efficient formin-mediated polymerization.…”

Section: Journal Of Biological Chemistrymentioning

confidence: 79%

Determinants of Formin Homology 1 (FH1) Domain Function in Actin Filament Elongation by Formins

Courtemanche

Pollard

2012

Journal of Biological Chemistry

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Background: Formin FH1 domains deliver subunits to actin filament barbed ends. Results: The transfer rate of formin Bni1p depends on FH1 polyproline track sequences and positions. Conclusion:The two FH1 domains of formin dimers deliver actin independently of one another. Significance: Sequence features of other FH1 domains are similar to Bni1p, suggesting a common strategy to maximize actin polymerization rates.

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Section: Journal Of Biological Chemistrymentioning

confidence: 79%

Determinants of Formin Homology 1 (FH1) Domain Function in Actin Filament Elongation by Formins

Courtemanche

Pollard

2012

Journal of Biological Chemistry

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“…50,51 The geometries for Pro-rich petides utilized fiber diffraction results for (Pro) n 40 and crystal structure data. [52][53][54][55] Polarizable groups were placed upon each of the bonds in the peptide backbone, the two lone pairs on the carbonyl oxygen, the C a À ÀH bond, the C b methyl group of Ala, and the CÀ ÀC and CÀ ÀH bonds of the Pro side chain. The polarizability tensors for these groups were approximated by axial tensors with longitudinal (a 33 ) and transverse (a 11 ) polarizabilities, orientations, and positions determined by the calculations of Walter Stevens, following the method of Garmer and Stevens.…”

Section: Resultsmentioning

confidence: 99%

“…CD spectra for (Pro) n predicted for four different conformations derived from X-ray diffraction. Sasisekaran structure from fiber diffraction on poly(Pro) 40 (n); (Pro) 10 from the crystal structure of a complex with profilin (PDB code 1AWI) 54 (~); oligoPro portion of the peptide Pro 10 -ITyr (ITyr 5 3-iodotyrosine) complexed with profilin (PDB code 1CF0) 55 (^); Pro-rich peptide (GlyPro 5 ) 3 GlyLeu complexed with profilin (PDB code 2V8C) 53 (! ); experimental CD spectrum of poly (Pro) 36 (l).…”

Section: Discussionmentioning

confidence: 99%

A significant role for high‐energy transitions in the ultraviolet circular dichroism spectra of polypeptides and proteins

Woody

2010

Chirality

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The nπ* and ππ* transitions of polypeptides mix significantly with very high energy transitions in the poly(Pro)II conformation, as evidenced by the strongly nonconservative CD spectrum in the 170-250 nm region. Because of this, the exciton model, the standard quantum mechanical model for predicting absorption and CD spectra of polypeptides, gives poor results for the poly(Pro) II (P(II)) conformation, although it works well for the α-helix, β-sheet, and β-turns. The exciton theory has been extended to include the effects of mixing of discrete peptide transitions near 200 nm with the large number of uncharacterized transitions in the deep ultraviolet. These latter transitions dominate the polarizability, and their mixing with the discrete transitions can be described via bond and lone-pair polarizability tensors, derivable by ab initio methods. This extended exciton method gives a good description of the CD spectrum of (Ala)(n) oligomers in the P(II) conformation. For this conformation, the polarizability contributions lead to a strong negative band near 200 nm that dominates the calculated and observed CD spectrum. The model does not give a good description of the CD of (Pro)(n) oligomers, probably because of conformational heterogeneity or nonadditive contributions of the Pro side chains. The model improves the calculated CD spectra of α-helical (Ala)(n) oligomers. Although the high-energy transitions make only a small net contribution to the CD of the α-helix in the 200 nm region, they enhance the negative exciton band at ∼205 nm and largely cancel the negative exciton band near 175 nm, substantially improving agreement with experiment.

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“…Like a mechanical jack, the FH1 serves as the lever and the FH2 serves as the ratchet. The lever of this formin ''jack'' is stacked by profilin-actins and according to the findings of Kursula's group, profilin dimerizes upon binding to FH1 peptide [25] which stiffens the elongated FH1. However, this formin ''jack'' does not have an equal quality on the FH1 lever, which elongates less with every subsequent profilin-actin added (Table 1) and this also correspond to less acceleration effect of formin motor in actin assembly with Fig.…”

Section: Conformational Elongation Of Fh1 and Formin Motor Behaviormentioning

confidence: 89%

A cooperative jack model of random coil‐to‐elongation transition of the FH1 domain by profilin binding explains formin motor behavior in actin polymerization

et al. 2014

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a b s t r a c tFilopodia are essential for the development of neuronal growth cones, cell polarity and cell migration. Their protrusions are powered by the polymerization of actin filaments linked to the plasma membrane, catalyzed by formin proteins. The acceleration of polymerization depends on the number of profilin-actins binding with the formin-FH1 domain. Biophysical characterization of the disordered formin-FH1 domain remains a challenge. We analyzed the conformational distribution of the diaphanous-related formin mDia1-FH1 bound with one to six profilins. We found a coil-to-elongation transition in the FH1 domain. We propose a cooperative ''jack'' model for the Formin-Homology-1 (FH1) domain of formins stacked by profilin-actins.

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High-resolution Structural Analysis of Mammalian Profilin 2a Complex Formation with Two Physiological Ligands: The Formin Homology 1 Domain of mDia1 and the Proline-rich Domain of VASP

Cited by 63 publications

References 96 publications

Determinants of Formin Homology 1 (FH1) Domain Function in Actin Filament Elongation by Formins

Determinants of Formin Homology 1 (FH1) Domain Function in Actin Filament Elongation by Formins

A significant role for high‐energy transitions in the ultraviolet circular dichroism spectra of polypeptides and proteins

A cooperative jack model of random coil‐to‐elongation transition of the FH1 domain by profilin binding explains formin motor behavior in actin polymerization

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