Identification of novel homologues of mouse importin α, the α subunit of the nuclear pore-targeting complex, and their tissue-specific expression
Transport of karyophilic proteins into the nucleus is mediated by nuclear localization signals (NLSs) via a multistep process. The karyophiles are recognized by the importin α subunit in the cytoplasm to form a stable complex, termed the nuclear pore-targeting complex (PTAC). To date, three differen...
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Published in: | FEBS letters Vol. 416; no. 1; pp. 30 - 34 |
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13-10-1997
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Abstract | Transport of karyophilic proteins into the nucleus is mediated by nuclear localization signals (NLSs) via a multistep process. The karyophiles are recognized by the importin α subunit in the cytoplasm to form a stable complex, termed the nuclear pore-targeting complex (PTAC). To date, three different mammalian α subunits (mSRP1/NPI-1, PTAC58/mPendulin/Rch1 and Qip1) have been identified. In this study, we report the identification of three additional mouse genes homologous to the known α subunits using RT-PCR methodology and show that the mouse α subunits can be classified into at least three subfamilies, α-P, α-Q and α-S families, each composed of closely related members (more than 80% amino acid sequence identity). These three subfamilies, however, have ∼50% amino acid identity to one another. Northern blot analysis showed that all were differentially expressed in various mouse tissues. These results suggest that the function of these proteins may be controlled in a tissue-specific manner and that their combinatorial expression may play a role in differentiation and organogenesis. |
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AbstractList | Transport of karyophilic proteins into the nucleus is mediated by nuclear localization signals (NLSs) via a multistep process. The karyophiles are recognized by the importin alpha subunit in the cytoplasm to form a stable complex, termed the nuclear pore-targeting complex (PTAC). To date, three different mammalian alpha subunits (mSRP1/NPI-1, PTAC58/mPendulin/Rch1 and Qip1) have been identified. In this study, we report the identification of three additional mouse genes homologous to the known alpha subunits using RT-PCR methodology and show that the mouse alpha subunits can be classified into at least three subfamilies, alpha-P, alpha-Q and alpha-S families, each composed of closely related members (more than 80% amino acid sequence identity). These three subfamilies, however, have approximately 50% amino acid identity to one another. Northern blot analysis showed that all were differentially expressed in various mouse tissues. These results suggest that the function of these proteins may be controlled in a tissue-specific manner and that their combinatorial expression may play a role in differentiation and organogenesis. Transport of karyophilic proteins into the nucleus is mediated by nuclear localization signals (NLSs) via a multistep process. The karyophiles are recognized by the importin α subunit in the cytoplasm to form a stable complex, termed the nuclear pore‐targeting complex (PTAC). To date, three different mammalian α subunits (mSRP1/NPI‐1, PTAC58/mPendulin/Rch1 and Qip1) have been identified. In this study, we report the identification of three additional mouse genes homologous to the known α subunits using RT‐PCR methodology and show that the mouse α subunits can be classified into at least three subfamilies, α‐P, α‐Q and α‐S families, each composed of closely related members (more than 80% amino acid sequence identity). These three subfamilies, however, have ∼50% amino acid identity to one another. Northern blot analysis showed that all were differentially expressed in various mouse tissues. These results suggest that the function of these proteins may be controlled in a tissue‐specific manner and that their combinatorial expression may play a role in differentiation and organogenesis. |
Author | Imamoto, Naoko Tsuji, Lyuji Yoneda, Yoshihiro Takumi, Toru |
Author_xml | – sequence: 1 givenname: Lyuji surname: Tsuji fullname: Tsuji, Lyuji organization: Department of Anatomy and Cell Biology, Osaka University Medical School, 2-2 Yamada-oka, Suita, Osaka 565, Japan – sequence: 2 givenname: Toru surname: Takumi fullname: Takumi, Toru organization: Department of Anatomy and Brain Science, Kobe University School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe 650, Japan – sequence: 3 givenname: Naoko surname: Imamoto fullname: Imamoto, Naoko organization: Department of Anatomy and Cell Biology, Osaka University Medical School, 2-2 Yamada-oka, Suita, Osaka 565, Japan – sequence: 4 givenname: Yoshihiro surname: Yoneda fullname: Yoneda, Yoshihiro organization: Department of Anatomy and Cell Biology, Osaka University Medical School, 2-2 Yamada-oka, Suita, Osaka 565, Japan |
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Copyright | 1997 Federation of European Biochemical Societies FEBS Letters 416 (1997) 1873-3468 © 2015 Federation of European Biochemical Societies |
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Keywords | Nuclear localization signal Importin α Nuclear pore-targeting complex Nuclear protein import |
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Snippet | Transport of karyophilic proteins into the nucleus is mediated by nuclear localization signals (NLSs) via a multistep process. The karyophiles are recognized... |
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SubjectTerms | alpha Karyopherins Amino Acid Sequence Animals Blotting, Northern Cell Differentiation - genetics DNA, Complementary Embryonic and Fetal Development - genetics Importin α Mice Molecular Sequence Data Nuclear Envelope - metabolism Nuclear localization signal Nuclear pore-targeting complex Nuclear protein import Nuclear Proteins - chemistry Nuclear Proteins - genetics Nuclear Proteins - metabolism Protein Binding Sequence Homology, Amino Acid |
Title | Identification of novel homologues of mouse importin α, the α subunit of the nuclear pore-targeting complex, and their tissue-specific expression |
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