In vivo evidence for involvement of a 58 kDa component of nuclear pore-targeting complex in nuclear protein import.

Imamoto, Naoko; Shimamoto, Takuya; Takao, Toshifumi; Tachibana, Taro; Kose, Shingo; Matsubae, Masami; Sekimoto, Takeyuki; Shimonishi, Yasutsugu; Yoneda, Yoshihiro

doi:10.1002/j.1460-2075.1995.tb00031.x

Cited by 288 publications

(271 citation statements)

References 42 publications

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“…Anti-PTAC58 antibody was prepared as described (Imamoto et al 1995). Recombinant p10 protein (Tachibana et al 1996) and Ran protein were expressed in E. coli strain BL21(DE3) and purified as described.…”

Section: Methodsmentioning

confidence: 99%

“…The GTP hydrolysis of Ran-GTP appears to be required in active nuclear transport, because the microinjection of excess amounts of the Ran-binding unhydrolysable GTP analogue, GTPgS (Ran-GTPgS), inhibits active nuclear transport, probably through the functional inhibition of endogenous Ran (Melchior et al 1993). Anti-PTAC58 antibody inhibits the function of PTAC58 in active nuclear transport (Imamoto et al 1995).…”

Section: Prevention Of Fas-induced Apoptotic Nuclear Change By Other mentioning

confidence: 99%

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Essential role of active nuclear transport in apoptosis

Yasuhara¹,

Eguchi²,

Tachibana³

et al. 1997

Genes to Cells

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Background: Apoptosis is defined by chromatin condensation, nuclear fragmentation and the formation of apoptotic bodies. Because apoptotic signals are transmitted through a common pathway that includes the target steps of death-driving ICEfamily proteases and anti-cell death protein Bcl-2 in the cytoplasm, the signals must be transferred from the cytoplasm to the nucleus, at least to induce the apoptotic manifestation of the nucleus. Small signal molecules might diffuse across nuclear pores, but larger molecules are transported by active mechanisms requiring ATP and GTP hydrolysis. It is not known whether apoptotic signals are transmitted into the nucleus by the mechanisms of active nuclear transport.

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Section: Methodsmentioning

confidence: 99%

Section: Prevention Of Fas-induced Apoptotic Nuclear Change By Other mentioning

confidence: 99%

Essential role of active nuclear transport in apoptosis

Yasuhara¹,

Eguchi²,

Tachibana³

et al. 1997

Genes to Cells

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“…Recombinant PTAC58 and PTAC97 (Imamoto et al, 1995a) were expressed in BL21 as GST fusion proteins as described previously (Imamoto et al, 1995b). The fusion proteins were puri®ed using glutathione-Sepharose a nity chromatography.…”

Section: Recombinant Expression and Puri®cation Of Ptac58 And Ptac97mentioning

confidence: 99%

Ku80 can translocate to the nucleus independent of the translocation of Ku70 using its own nuclear localization signal

Koike¹,

Ikuta

Miyasaka³

et al. 1999

Oncogene

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Ku antigen is a complex of Ku70 and Ku80 subunits and plays an important role in not only DNA double-strand breaks (DSB) repair and V(D)J recombination, but also in growth regulation. Ku is generally believed to always form and function as heterodimers on the basis of in vitro observations. Here we demonstrate that the localization of Ku80 does not completely coincide with that of Ku70. Ku70 and Ku80 were colocalized in the nucleus in the interphase but not in the late telophase/early G1 phase of the cell cycle. Since the in vivo function of Ku might be partially regulated by the control of its transport, we attempted to investigate the molecular mechanisms underlying the nuclear translocation of Ku. The nuclear translocation of Ku80 started during the late telophase/ early G1 phase after the nuclear envelope was formed and this was preceded by the nuclear translocation of Ku70. Furthermore, we found that the Ku80 protein was transported to the nucleus without heterodimerization with Ku70. To understand in detail the mechanism of transport of Ku80, we attempted to identify the nuclear localization signal (NLS) of Ku80 and de®ned to a region spanning nine amino acid residues (positions 561 ± 569). The Ku80 NLS was demonstrated to be mediated to the nuclear rim by two components of PTAC58 and PTAC97. All these ®ndings support the idea that Ku80 can translocate to the nucleus using its own NLS independent of the translocation of Ku70.

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“…NRa from yeast, also termed Srplp or Kap60p [18,21], is most likely identical to the previously characterized NLS-binding protein NBP70 [22,23]. While there is only one yeast gene encoding NRa, higher eukaryotes contain a group of similar genes, which suggests differences in substrate specificity [11,20,24-281. NRc~ binds directly to nuclear localization sequences [14,22,17,20,26,29,30]. NR[3 was found to have weak [17] or no NLS-binding activity by itself [31,32] but it cooperates with NRc~ in NLS-recognition and binding of import substrate to the NE [16,17,32].…”

Section: Nls-reeeptor (Nr)mentioning

confidence: 99%

“…Thus translocation through the NPC is mediated only by NR[3. Mammalian NRct was observed both in the cytoplasm and in the nucleus [19,30,36]. Yeast NRct was localized to the nucleus, or the NE, or the cytoplasm [21,22,[37][38][39].…”

Section: Nls-reeeptor (Nr)mentioning

confidence: 99%

Protein import into the nucleus

Schlenstedt

1996

FEBS Letters

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The transport of proteins from the cytoplasm into the nucleus is a multistep process. The nuclear localization sequence (NLS) of a transport substrate associates with the heterodimeric NLS-receptor which binds to a subset of proteins of the nuclear pore complex (NPC). Translocation through the NPC is energydependent and requires the small GTPase Ran. Proteins that interact with Ran in either the GDP-bound or the GTP-bound state coordinate transfer through the NPC. Lastly, the NLSreeeptorlsubstrate complex and Ran reach the nuclear side of the NPC where the complex disassembles.

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In vivo evidence for involvement of a 58 kDa component of nuclear pore-targeting complex in nuclear protein import.

Cited by 288 publications

References 42 publications

Essential role of active nuclear transport in apoptosis

Essential role of active nuclear transport in apoptosis

Ku80 can translocate to the nucleus independent of the translocation of Ku70 using its own nuclear localization signal

Protein import into the nucleus

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