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Yoshiyuki Matsuura

Publications and source records attributed to Yoshiyuki Matsuura.

6 recordsLinked to original sources
PubMed2005

Nup50/Npap60 function in nuclear protein import complex disassembly and importin recycling.

Nuclear import of proteins containing classical nuclear localization signals (NLS) is mediated by the importin-alpha:beta complex that binds cargo in the cytoplasm and facilitates its passage through nuclear pores, after which nuclear RanGTP dissociates the import complex and the importins are recycled. In vertebrates, import is stimulated by nucleoporin Nup50, which has been proposed to accompany the import complex through nuclear pores. However, we show here that the Nup50 N-terminal domain actively displaces NLSs from importin-alpha, which would be more consistent with Nup50 functioning to coordinate import complex disassembly and importin recycling. The crystal structure of the importin-alpha:Nup50 complex shows that Nup50 binds at two sites on importin-alpha. One site overlaps the secondary NLS-binding site, whereas the second extends along the importin-alpha C-terminus. Mutagenesis indicates that interaction at both sites is required for Nup50 to displace NLSs. The Cse1p:Kap60p:RanGTP complex structure suggests how Nup50 is then displaced on formation of the importin-alpha export complex. These results provide a rationale for understanding the series of interactions that orchestrate the terminal steps of nuclear protein import.

Amino Acid Sequence↗
PubMed2005

Structural basis for nuclear import complex dissociation by RanGTP.

Nuclear protein import is mediated mainly by the transport factor importin-beta that binds cytoplasmic cargo, most often via the importin-alpha adaptor, and then transports it through nuclear pore complexes. This active transport is driven by disassembly of the import complex by nuclear RanGTP. The switch I and II loops of Ran change conformation with nucleotide state, and regulate its interactions with nuclear trafficking components. Importin-beta consists of 19 HEAT repeats that are based on a pair of antiparallel alpha-helices (referred to as the A- and B-helices). The HEAT repeats stack to yield two C-shaped arches, linked together to form a helicoidal molecule that has considerable conformational flexibility. Here we present the structure of full-length yeast importin-beta (Kap95p or karyopherin-beta) complexed with RanGTP, which provides a basis for understanding the crucial cargo-release step of nuclear import. We identify a key interaction site where the RanGTP switch I loop binds to the carboxy-terminal arch of Kap95p. This interaction produces a change in helicoidal pitch that locks Kap95p in a conformation that cannot bind importin-alpha or cargo. We suggest an allosteric mechanism for nuclear import complex disassembly by RanGTP.

Active Transport, Cell Nucleus↗
PubMed2004

Structural basis for the assembly of a nuclear export complex.

The nuclear import and export of macromolecular cargoes through nuclear pore complexes is mediated primarily by carriers such as importin-beta. Importins carry cargoes into the nucleus, whereas exportins carry cargoes to the cytoplasm. Transport is orchestrated by nuclear RanGTP, which dissociates cargoes from importins, but conversely is required for cargo binding to exportins. Here we present the 2.0 A crystal structure of the nuclear export complex formed by exportin Cse1p complexed with its cargo (Kap60p) and RanGTP, thereby providing a structural framework for understanding nuclear protein export and the different functions of RanGTP in export and import. In the complex, Cse1p coils around both RanGTP and Kap60p, stabilizing the RanGTP-state and clamping the Kap60p importin-beta-binding domain, ensuring that only cargo-free Kap60p is exported. Mutagenesis indicated that conformational changes in exportins couple cargo binding to high affinity for RanGTP, generating a spring-loaded molecule to facilitate disassembly of the export complex following GTP hydrolysis in the cytoplasm.

Active Transport, Cell Nucleus↗
PubMed2003

Structural basis for Nup2p function in cargo release and karyopherin recycling in nuclear import.

The yeast nucleoporin Nup2p is associated primarily with the nuclear basket of nuclear pore complexes and is required for efficient importin-alpha:beta-mediated nuclear protein import as well as efficient nuclear export of Kap60p/importin-alpha. Residues 1-51 of Nup2p bind tightly to Kap60p and are required for Nup2p function in vivo. We have determined the 2.6 A resolution crystal structure of a complex between this region of Nup2p and the armadillo repeat domain of Kap60p. Nup2p binds along the inner concave groove of Kap60p, but its interaction interface is different from that employed for nuclear localization signal (NLS) recognition although there is some overlap between them. Nup2p binds Kap60p more strongly than NLSs and accelerates release of NLSs from Kap60p. Nup2p itself is released from Kap60p by Cse1p:RanGTP only in the presence of the importin-beta binding (IBB) domain of Kap60p. These data indicate that Nup2p increases the overall rate of nuclear trafficking by coordinating nuclear import termination and importin recycling as a concerted process.

Active Transport, Cell Nucleus↗
PubMed1999

Analysis of the velocity curve for height by the wavelet interpolation method in children classified by maturity rate.

The Wavelet Interpolation Method (WIM) developed by Meyer ([1992] Wavelets and Operators. Cambridge: Cambridge University Press) has been proposed as an analytical method for the accurate description of longitudinal growth velocity in height and identification of the age at maximum peak velocity (MPV) in the curve. The distance curve in height was determined by interpolating the longitudinal records of 98 boys and 88 girls, 6-17 years old, with the WIM. The distance curve was then differentiated to obtain a velocity curve. Age at MPV estimated from the velocity curve was utilized as a criterion of maturity rate (timing), and five maturity groups (early, little early, average, little late and late) were defined in both sexes. Four type models were derived from the occurrence of secondary peaks (mid-growth spurt and after-growth spurt): type model A, appearance of a mid-growth spurt and MPV; type model B, appearance of an after-growth spurt and MPV; type model C, appearance of a mid-growth spurt, an after-growth spurt and MPV; and type model D, appearance of MPV only. The individual growth data of boys and girls classified by maturity rate were sorted into the four type models. The frequency of occurrence of the four type models in groups classified by maturity rate was then analyzed, and the characteristics of height growth velocity was examined in boys and girls. Am. J. Hum. Biol. 11:13-30, 1999. Copyright 1999 Wiley-Liss, Inc.

Journal Article↗