Tertiary Structure of Destrin and Structural Similarity between Two Actin-Regulating Protein Families

Hatanaka, Hideki; Ogura, Kenji; Moriyama, Kenji; Ichikawa, Saori; Yahara, Ichiro; Inagaki, Fuyuhiko

doi:10.1016/s0092-8674(00)81305-7

Cited by 136 publications

(139 citation statements)

References 66 publications

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“…Both mutant proteins inhibit the assembly and disassembly of actin as compared with maize ADF3. These data are discussed in relation to the tertiary structures of destrin (32) and yeast cofilin (33).…”

mentioning

confidence: 96%

“…Phosphorylation inhibits interaction with actin, whereas dephosphorylation promotes interaction. Under certain conditions, cofilin and actin form intranuclear cofilin:actin rods and a nuclear localization signal has been identified between Lys-19 and Lys-34 (32,35,36). Cofilin is dephosphorylated prior to translocation into the nucleus.…”

mentioning

confidence: 99%

“…Ser-3 is located close to the actin binding long ␣-helix in the tertiary structure of destrin, and it has been proposed that phosphorylation of this residue may perturb the function of Lys-112 (32). The nuclear localization signal is located at the opposite side of the actin contact in the tertiary structure, and phosphorylation of Ser-3 appears to inhibit its action (32).…”

mentioning

confidence: 99%

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F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF)

Jiang

Weeds

Khan

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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Actin depolymerizing factors (ADF) are stimulus responsive actin cytoskeleton modulating proteins. They bind both monomeric actin (G-actin) and filamentous actin (F-actin) and, under certain conditions, F-actin binding is followed by filament severing. In this paper, using mutant maize ADF3 proteins, we demonstrate that the maize ADF3 binding of F-actin can be spatially distinguished from that of G-actin. One mutant, zmadf3-1, in which Tyr-103 and Ala-104 (equivalent to destrin Tyr-117 and Ala-118) have been replaced by phenylalanine and glycine, respectively, binds more weakly to both G-actin and F-actin compared with maize ADF3. A second mutant, zmadf3-2, in which both Tyr-67 and Tyr-70 are replaced by phenylalanine, shows an affinity for G-actin similar to maize ADF3, but F-actin binding is abolished. The two tyrosines, Tyr-67 and Tyr-70, are in the equivalent position to Tyr-82 and Tyr-85 of destrin, respectively. Using the tertiary structure of destrin, yeast cofilin, and Acanthamoeba actophorin, we discuss the implications of removing the aromatic hydroxyls of Tyr-82 and Tyr-85 (i.e., the effect of substituting phenylalanine for tyrosine) and conclude that Tyr-82 plays a critical role in stabilizing the tertiary structure that is essential for F-actin binding. We propose that this tertiary structure is maintained as a result of a hydrogen bond between the hydroxyl of Tyr-82 and the carbonyl of Tyr-117, which is located in the long ␣-helix; amino acid components of this helix (Leu-111 to Phe-128) have been implicated in G-actin and F-actin binding. The structures of human destrin and yeast cofilin indicate a hydrogen distance of 2.61 and 2.77 Å, respectively, with corresponding bond angles of 99.5°and 113°, close to the optimum for a strong hydrogen bond.

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confidence: 96%

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confidence: 99%

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confidence: 99%

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F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF)

Jiang

Weeds

Khan

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

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“…) family, is a possible source for the single-domain gene that was duplicated to form the multi-domain actin-severing proteins (Hofmann et al, 1993). Comparison of the sequences of destrin and villin 14T, aligned by structural elements (Hatanaka et al, 1996) and allowing conservative replacements in the sets (R, K), (V, I, L, F, Y, W, H), and (E, Q), shows that the sequence similarity is about 21 %, consistent with the similarity in the fold. Two of the proposed calcium binding ligands for villin 14T are not conserved in destrin, consistent with destrin's calcium-independent affinity for actin.…”

Section: Comparison With the Actin-regulating Protein Destrinmentioning

confidence: 70%

“…The structure of severin domain 2 in solution is also available (Schnuchel et al, 1995). These studies have revealed that the conserved repeated domain has a unique fold, comprised of both /?-sheet and a-helix, observed so far only in the actin-severing proteins and the single-domain actin regulating protein destrin (Hatanaka et al, 1996). Many of the residues within the most strongly conserved region contribute to the hydrophobic core of the molecule and to the turns between elements of secondary structure and thus are conserved for structural rather than functional reasons.…”

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confidence: 99%

Refined structure of villin 14T and a detailed comparison with other actin‐severing domains

1997

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Villin 14T is the amino terminal actin monomer binding domain from the actin-severing and bundling protein villin. Its structure has been determined in solution using heteronuclear multidimensional nuclear magnetic resonance (NMR) spectroscopy (Markus MA, Nakayama T, Matsudaira P, Wagner G. 1994. Solution structure of villin 14T, a domain conserved among actin-severing proteins. Protein Science 3:70-81). An additional nuclear Overhauser effect (NOE) spectroscopy data set, acquired using improved gradient techniques, and further detailed analysis of existing data sets, produced an additional 601 NOE restraints for structure calculations. The overall fold does not change significantly with the additional NOE restraints but the definition of the structure is improved, as judged by smaller deviations among an ensemble of calculated structures that adequately satisfy the NMR restraints. Some of the side chains, especially those in the hydrophobic core of the domain, are much more defined. This improvement in the detail of the solution structure of villin 14T makes it interesting to compare the structure with the crystal structure of gelsolin segment 1, which shares 58% sequence identity with villin 14T, in an effort to gain insight into villin 14T's weaker affinity for actin monomers. Villin 14T has smaller side chains at several positions that make hydrophobic contacts with actin in the context of gelsolin segment 1. The structure is also compared with the structure of the related actin-severing domain, severin domain 2.

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Dictyostelium as model system for studies of the actin cytoskeleton by molecular genetics

Eichinger

Lee

Schleicher

1999

Microsc. Res. Tech.

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The actin cytoskeleton is an essential structure for most movements at the cellular and intracellular level. Whereas for contraction a muscle cell requires a rather static organisation of cytoskeletal proteins, cell motility of amoeboid cells relies on a tremendously dynamic turnover of filamentous networks in a matter of seconds and at distinct regions inside the cell. The best model system for studying cell motility is Dictyostelium discoideum. The cells live as single amoebae but can also start a developmental program that leads to multicellular stages and differentiation into simple types of tissues. Thus, cell motility can be studied on single cells and on cells in a tissue‐like aggregate. The ability to combine protein purification and biochemistry with fairly easy molecular genetics is a unique feature for investigation of the cytoskeleton and cell motility. The actin cytoskeleton in Dictyostelium harbours essentially all classes of actin‐binding proteins that have been found throughout eukaryotes. By conventional mutagenesis, gene disruption, antisense approaches, or gene replacements many genes that code for cytoskeletal proteins have been disrupted, and altered phenotypes in transformants that lacked one or more of those cytoskeletal proteins allowed solid conclusions about their in vivo function. In addition, tagging the proteins or selected domains with green fluorescent protein allows the monitoring of protein redistribution during cell movement. Gene tagging by restriction enzyme mediated integration of vectors and the ongoing international genome and cDNA sequencing projects offer the chance to understand the dynamics of the cytoskeleton by identification and functional characterisation of all proteins involved. Microsc. Res. Tech. 47:124–134, 1999. © 1999 Wiley‐Liss, Inc.

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Tertiary Structure of Destrin and Structural Similarity between Two Actin-Regulating Protein Families

Cited by 136 publications

References 66 publications

F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF)

F-actin and G-actin binding are uncoupled by mutation of conserved tyrosine residues in maize actin depolymerizing factor (ZmADF)

Refined structure of villin 14T and a detailed comparison with other actin‐severing domains

Dictyostelium as model system for studies of the actin cytoskeleton by molecular genetics

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