Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58)

Background MSP58 is a nucleolar protein associated with rRNA transcription and cell proliferation. Its mechanism of translocation into the nucleus or the nucleolus, however, is not entirely known. In order to address this lack, the present study aims to determine a crucial part of this mechanism: th...
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Autor*in:	Yang, Chuan-Pin [verfasserIn] Chiang, Chi-Wu Chen, Chang-Han Lee, Yi-Chao Wu, Mei-Hsiang Tsou, Yi-Huan Yang, Yu-San Chang, Wen-Chang Lin, Ding-Yen

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2015

Schlagwörter:	58-kDa Microspherule Protein Nucleolus Nuclear localization signal Nucleolar localization signal Importins

Anmerkung:	© Yang et al.; licensee BioMed Central. 2015. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (

Übergeordnetes Werk:	Enthalten in: Journal of biomedical science - London : BioMed Central, 1994, 22(2015), 1 vom: 16. Mai
Übergeordnetes Werk:	volume:22 ; year:2015 ; number:1 ; day:16 ; month:05

Links:	Volltext

DOI / URN:	10.1186/s12929-015-0136-0

Katalog-ID:	SPR028493303

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520			\|a Background MSP58 is a nucleolar protein associated with rRNA transcription and cell proliferation. Its mechanism of translocation into the nucleus or the nucleolus, however, is not entirely known. In order to address this lack, the present study aims to determine a crucial part of this mechanism: the nuclear localization signal (NLS) and the nucleolar localization signal (NoLS) associated with the MSP58 protein. Results We have identified and characterized two NLSs in MSP58. The first is located between residues 32 and 56 (NLS1) and constitutes three clusters of basic amino acids (KRASSQALGTIPKRRSSSRFIKRKK); the second is situated between residues 113 and 123 (NLS2) and harbors a monopartite signal (PGLTKRVKKSK). Both NLS1 and NLS2 are highly conserved among different vertebrate species. Notably, one bipartite motif within the NLS1 (residues 44–56) appears to be absolutely necessary for MSP58 nucleolar localization. By yeast two-hybrid, pull-down, and coimmunoprecipitation analysis, we show that MSP58 binds to importin α1 and α6, suggesting that nuclear targeting of MSP58 utilizes a receptor-mediated and energy-dependent import mechanism. Functionally, our data show that both nuclear and nucleolar localization of MSP58 are crucial for transcriptional regulation on p21 and ribosomal RNA genes, and context-dependent effects on cell proliferation. Conclusions Results suggest that MSP58 subnuclear localization is regulated by two nuclear import signals, and that proper subcellular localization of MSP58 is critical for its role in transcriptional regulation. Our study reveals a molecular mechanism that controls nuclear and nucleolar localization of MSP58, a finding that might help future researchers understand the MSP58 biological signaling pathway.
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author_variant	c p y cpy c w c cwc c h c chc y c l ycl m h w mhw y h t yht y s y ysy w c c wcc d y l dyl
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publishDate	2015
allfields	10.1186/s12929-015-0136-0 doi (DE-627)SPR028493303 (SPR)s12929-015-0136-0-e DE-627 ger DE-627 rakwb eng Yang, Chuan-Pin verfasserin aut Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58) 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Yang et al.; licensee BioMed Central. 2015. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background MSP58 is a nucleolar protein associated with rRNA transcription and cell proliferation. Its mechanism of translocation into the nucleus or the nucleolus, however, is not entirely known. In order to address this lack, the present study aims to determine a crucial part of this mechanism: the nuclear localization signal (NLS) and the nucleolar localization signal (NoLS) associated with the MSP58 protein. Results We have identified and characterized two NLSs in MSP58. The first is located between residues 32 and 56 (NLS1) and constitutes three clusters of basic amino acids (KRASSQALGTIPKRRSSSRFIKRKK); the second is situated between residues 113 and 123 (NLS2) and harbors a monopartite signal (PGLTKRVKKSK). Both NLS1 and NLS2 are highly conserved among different vertebrate species. Notably, one bipartite motif within the NLS1 (residues 44–56) appears to be absolutely necessary for MSP58 nucleolar localization. By yeast two-hybrid, pull-down, and coimmunoprecipitation analysis, we show that MSP58 binds to importin α1 and α6, suggesting that nuclear targeting of MSP58 utilizes a receptor-mediated and energy-dependent import mechanism. Functionally, our data show that both nuclear and nucleolar localization of MSP58 are crucial for transcriptional regulation on p21 and ribosomal RNA genes, and context-dependent effects on cell proliferation. Conclusions Results suggest that MSP58 subnuclear localization is regulated by two nuclear import signals, and that proper subcellular localization of MSP58 is critical for its role in transcriptional regulation. Our study reveals a molecular mechanism that controls nuclear and nucleolar localization of MSP58, a finding that might help future researchers understand the MSP58 biological signaling pathway. 58-kDa Microspherule Protein (dpeaa)DE-He213 Nucleolus (dpeaa)DE-He213 Nuclear localization signal (dpeaa)DE-He213 Nucleolar localization signal (dpeaa)DE-He213 Importins (dpeaa)DE-He213 Chiang, Chi-Wu aut Chen, Chang-Han aut Lee, Yi-Chao aut Wu, Mei-Hsiang aut Tsou, Yi-Huan aut Yang, Yu-San aut Chang, Wen-Chang aut Lin, Ding-Yen aut Enthalten in Journal of biomedical science London : BioMed Central, 1994 22(2015), 1 vom: 16. Mai (DE-627)300593724 (DE-600)1482918-6 1423-0127 nnns volume:22 year:2015 number:1 day:16 month:05 https://dx.doi.org/10.1186/s12929-015-0136-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4328 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 22 2015 1 16 05
spelling	10.1186/s12929-015-0136-0 doi (DE-627)SPR028493303 (SPR)s12929-015-0136-0-e DE-627 ger DE-627 rakwb eng Yang, Chuan-Pin verfasserin aut Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58) 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Yang et al.; licensee BioMed Central. 2015. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background MSP58 is a nucleolar protein associated with rRNA transcription and cell proliferation. Its mechanism of translocation into the nucleus or the nucleolus, however, is not entirely known. In order to address this lack, the present study aims to determine a crucial part of this mechanism: the nuclear localization signal (NLS) and the nucleolar localization signal (NoLS) associated with the MSP58 protein. Results We have identified and characterized two NLSs in MSP58. The first is located between residues 32 and 56 (NLS1) and constitutes three clusters of basic amino acids (KRASSQALGTIPKRRSSSRFIKRKK); the second is situated between residues 113 and 123 (NLS2) and harbors a monopartite signal (PGLTKRVKKSK). Both NLS1 and NLS2 are highly conserved among different vertebrate species. Notably, one bipartite motif within the NLS1 (residues 44–56) appears to be absolutely necessary for MSP58 nucleolar localization. By yeast two-hybrid, pull-down, and coimmunoprecipitation analysis, we show that MSP58 binds to importin α1 and α6, suggesting that nuclear targeting of MSP58 utilizes a receptor-mediated and energy-dependent import mechanism. Functionally, our data show that both nuclear and nucleolar localization of MSP58 are crucial for transcriptional regulation on p21 and ribosomal RNA genes, and context-dependent effects on cell proliferation. Conclusions Results suggest that MSP58 subnuclear localization is regulated by two nuclear import signals, and that proper subcellular localization of MSP58 is critical for its role in transcriptional regulation. Our study reveals a molecular mechanism that controls nuclear and nucleolar localization of MSP58, a finding that might help future researchers understand the MSP58 biological signaling pathway. 58-kDa Microspherule Protein (dpeaa)DE-He213 Nucleolus (dpeaa)DE-He213 Nuclear localization signal (dpeaa)DE-He213 Nucleolar localization signal (dpeaa)DE-He213 Importins (dpeaa)DE-He213 Chiang, Chi-Wu aut Chen, Chang-Han aut Lee, Yi-Chao aut Wu, Mei-Hsiang aut Tsou, Yi-Huan aut Yang, Yu-San aut Chang, Wen-Chang aut Lin, Ding-Yen aut Enthalten in Journal of biomedical science London : BioMed Central, 1994 22(2015), 1 vom: 16. Mai (DE-627)300593724 (DE-600)1482918-6 1423-0127 nnns volume:22 year:2015 number:1 day:16 month:05 https://dx.doi.org/10.1186/s12929-015-0136-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4328 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 22 2015 1 16 05
allfields_unstemmed	10.1186/s12929-015-0136-0 doi (DE-627)SPR028493303 (SPR)s12929-015-0136-0-e DE-627 ger DE-627 rakwb eng Yang, Chuan-Pin verfasserin aut Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58) 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Yang et al.; licensee BioMed Central. 2015. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background MSP58 is a nucleolar protein associated with rRNA transcription and cell proliferation. Its mechanism of translocation into the nucleus or the nucleolus, however, is not entirely known. In order to address this lack, the present study aims to determine a crucial part of this mechanism: the nuclear localization signal (NLS) and the nucleolar localization signal (NoLS) associated with the MSP58 protein. Results We have identified and characterized two NLSs in MSP58. The first is located between residues 32 and 56 (NLS1) and constitutes three clusters of basic amino acids (KRASSQALGTIPKRRSSSRFIKRKK); the second is situated between residues 113 and 123 (NLS2) and harbors a monopartite signal (PGLTKRVKKSK). Both NLS1 and NLS2 are highly conserved among different vertebrate species. Notably, one bipartite motif within the NLS1 (residues 44–56) appears to be absolutely necessary for MSP58 nucleolar localization. By yeast two-hybrid, pull-down, and coimmunoprecipitation analysis, we show that MSP58 binds to importin α1 and α6, suggesting that nuclear targeting of MSP58 utilizes a receptor-mediated and energy-dependent import mechanism. Functionally, our data show that both nuclear and nucleolar localization of MSP58 are crucial for transcriptional regulation on p21 and ribosomal RNA genes, and context-dependent effects on cell proliferation. Conclusions Results suggest that MSP58 subnuclear localization is regulated by two nuclear import signals, and that proper subcellular localization of MSP58 is critical for its role in transcriptional regulation. Our study reveals a molecular mechanism that controls nuclear and nucleolar localization of MSP58, a finding that might help future researchers understand the MSP58 biological signaling pathway. 58-kDa Microspherule Protein (dpeaa)DE-He213 Nucleolus (dpeaa)DE-He213 Nuclear localization signal (dpeaa)DE-He213 Nucleolar localization signal (dpeaa)DE-He213 Importins (dpeaa)DE-He213 Chiang, Chi-Wu aut Chen, Chang-Han aut Lee, Yi-Chao aut Wu, Mei-Hsiang aut Tsou, Yi-Huan aut Yang, Yu-San aut Chang, Wen-Chang aut Lin, Ding-Yen aut Enthalten in Journal of biomedical science London : BioMed Central, 1994 22(2015), 1 vom: 16. Mai (DE-627)300593724 (DE-600)1482918-6 1423-0127 nnns volume:22 year:2015 number:1 day:16 month:05 https://dx.doi.org/10.1186/s12929-015-0136-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4328 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 22 2015 1 16 05
allfieldsGer	10.1186/s12929-015-0136-0 doi (DE-627)SPR028493303 (SPR)s12929-015-0136-0-e DE-627 ger DE-627 rakwb eng Yang, Chuan-Pin verfasserin aut Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58) 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Yang et al.; licensee BioMed Central. 2015. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background MSP58 is a nucleolar protein associated with rRNA transcription and cell proliferation. Its mechanism of translocation into the nucleus or the nucleolus, however, is not entirely known. In order to address this lack, the present study aims to determine a crucial part of this mechanism: the nuclear localization signal (NLS) and the nucleolar localization signal (NoLS) associated with the MSP58 protein. Results We have identified and characterized two NLSs in MSP58. The first is located between residues 32 and 56 (NLS1) and constitutes three clusters of basic amino acids (KRASSQALGTIPKRRSSSRFIKRKK); the second is situated between residues 113 and 123 (NLS2) and harbors a monopartite signal (PGLTKRVKKSK). Both NLS1 and NLS2 are highly conserved among different vertebrate species. Notably, one bipartite motif within the NLS1 (residues 44–56) appears to be absolutely necessary for MSP58 nucleolar localization. By yeast two-hybrid, pull-down, and coimmunoprecipitation analysis, we show that MSP58 binds to importin α1 and α6, suggesting that nuclear targeting of MSP58 utilizes a receptor-mediated and energy-dependent import mechanism. Functionally, our data show that both nuclear and nucleolar localization of MSP58 are crucial for transcriptional regulation on p21 and ribosomal RNA genes, and context-dependent effects on cell proliferation. Conclusions Results suggest that MSP58 subnuclear localization is regulated by two nuclear import signals, and that proper subcellular localization of MSP58 is critical for its role in transcriptional regulation. Our study reveals a molecular mechanism that controls nuclear and nucleolar localization of MSP58, a finding that might help future researchers understand the MSP58 biological signaling pathway. 58-kDa Microspherule Protein (dpeaa)DE-He213 Nucleolus (dpeaa)DE-He213 Nuclear localization signal (dpeaa)DE-He213 Nucleolar localization signal (dpeaa)DE-He213 Importins (dpeaa)DE-He213 Chiang, Chi-Wu aut Chen, Chang-Han aut Lee, Yi-Chao aut Wu, Mei-Hsiang aut Tsou, Yi-Huan aut Yang, Yu-San aut Chang, Wen-Chang aut Lin, Ding-Yen aut Enthalten in Journal of biomedical science London : BioMed Central, 1994 22(2015), 1 vom: 16. Mai (DE-627)300593724 (DE-600)1482918-6 1423-0127 nnns volume:22 year:2015 number:1 day:16 month:05 https://dx.doi.org/10.1186/s12929-015-0136-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4328 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 22 2015 1 16 05
allfieldsSound	10.1186/s12929-015-0136-0 doi (DE-627)SPR028493303 (SPR)s12929-015-0136-0-e DE-627 ger DE-627 rakwb eng Yang, Chuan-Pin verfasserin aut Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58) 2015 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © Yang et al.; licensee BioMed Central. 2015. This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( Background MSP58 is a nucleolar protein associated with rRNA transcription and cell proliferation. Its mechanism of translocation into the nucleus or the nucleolus, however, is not entirely known. In order to address this lack, the present study aims to determine a crucial part of this mechanism: the nuclear localization signal (NLS) and the nucleolar localization signal (NoLS) associated with the MSP58 protein. Results We have identified and characterized two NLSs in MSP58. The first is located between residues 32 and 56 (NLS1) and constitutes three clusters of basic amino acids (KRASSQALGTIPKRRSSSRFIKRKK); the second is situated between residues 113 and 123 (NLS2) and harbors a monopartite signal (PGLTKRVKKSK). Both NLS1 and NLS2 are highly conserved among different vertebrate species. Notably, one bipartite motif within the NLS1 (residues 44–56) appears to be absolutely necessary for MSP58 nucleolar localization. By yeast two-hybrid, pull-down, and coimmunoprecipitation analysis, we show that MSP58 binds to importin α1 and α6, suggesting that nuclear targeting of MSP58 utilizes a receptor-mediated and energy-dependent import mechanism. Functionally, our data show that both nuclear and nucleolar localization of MSP58 are crucial for transcriptional regulation on p21 and ribosomal RNA genes, and context-dependent effects on cell proliferation. Conclusions Results suggest that MSP58 subnuclear localization is regulated by two nuclear import signals, and that proper subcellular localization of MSP58 is critical for its role in transcriptional regulation. Our study reveals a molecular mechanism that controls nuclear and nucleolar localization of MSP58, a finding that might help future researchers understand the MSP58 biological signaling pathway. 58-kDa Microspherule Protein (dpeaa)DE-He213 Nucleolus (dpeaa)DE-He213 Nuclear localization signal (dpeaa)DE-He213 Nucleolar localization signal (dpeaa)DE-He213 Importins (dpeaa)DE-He213 Chiang, Chi-Wu aut Chen, Chang-Han aut Lee, Yi-Chao aut Wu, Mei-Hsiang aut Tsou, Yi-Huan aut Yang, Yu-San aut Chang, Wen-Chang aut Lin, Ding-Yen aut Enthalten in Journal of biomedical science London : BioMed Central, 1994 22(2015), 1 vom: 16. Mai (DE-627)300593724 (DE-600)1482918-6 1423-0127 nnns volume:22 year:2015 number:1 day:16 month:05 https://dx.doi.org/10.1186/s12929-015-0136-0 kostenfrei Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2056 GBV_ILN_2057 GBV_ILN_2061 GBV_ILN_2111 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4328 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 22 2015 1 16 05
language	English
source	Enthalten in Journal of biomedical science 22(2015), 1 vom: 16. Mai volume:22 year:2015 number:1 day:16 month:05
sourceStr	Enthalten in Journal of biomedical science 22(2015), 1 vom: 16. Mai volume:22 year:2015 number:1 day:16 month:05
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	58-kDa Microspherule Protein Nucleolus Nuclear localization signal Nucleolar localization signal Importins
isfreeaccess_bool	true
container_title	Journal of biomedical science
authorswithroles_txt_mv	Yang, Chuan-Pin @@aut@@ Chiang, Chi-Wu @@aut@@ Chen, Chang-Han @@aut@@ Lee, Yi-Chao @@aut@@ Wu, Mei-Hsiang @@aut@@ Tsou, Yi-Huan @@aut@@ Yang, Yu-San @@aut@@ Chang, Wen-Chang @@aut@@ Lin, Ding-Yen @@aut@@
publishDateDaySort_date	2015-05-16T00:00:00Z
hierarchy_top_id	300593724
id	SPR028493303
language_de	englisch
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This is an Open Access article distributed under the terms of the Creative Commons Attribution License (</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Background MSP58 is a nucleolar protein associated with rRNA transcription and cell proliferation. Its mechanism of translocation into the nucleus or the nucleolus, however, is not entirely known. In order to address this lack, the present study aims to determine a crucial part of this mechanism: the nuclear localization signal (NLS) and the nucleolar localization signal (NoLS) associated with the MSP58 protein. Results We have identified and characterized two NLSs in MSP58. The first is located between residues 32 and 56 (NLS1) and constitutes three clusters of basic amino acids (KRASSQALGTIPKRRSSSRFIKRKK); the second is situated between residues 113 and 123 (NLS2) and harbors a monopartite signal (PGLTKRVKKSK). Both NLS1 and NLS2 are highly conserved among different vertebrate species. 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author	Yang, Chuan-Pin
spellingShingle	Yang, Chuan-Pin misc 58-kDa Microspherule Protein misc Nucleolus misc Nuclear localization signal misc Nucleolar localization signal misc Importins Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58)
authorStr	Yang, Chuan-Pin
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topic_title	Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58) 58-kDa Microspherule Protein (dpeaa)DE-He213 Nucleolus (dpeaa)DE-He213 Nuclear localization signal (dpeaa)DE-He213 Nucleolar localization signal (dpeaa)DE-He213 Importins (dpeaa)DE-He213
topic	misc 58-kDa Microspherule Protein misc Nucleolus misc Nuclear localization signal misc Nucleolar localization signal misc Importins
topic_unstemmed	misc 58-kDa Microspherule Protein misc Nucleolus misc Nuclear localization signal misc Nucleolar localization signal misc Importins
topic_browse	misc 58-kDa Microspherule Protein misc Nucleolus misc Nuclear localization signal misc Nucleolar localization signal misc Importins
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title	Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58)
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title_full	Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58)
author_sort	Yang, Chuan-Pin
journal	Journal of biomedical science
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author_browse	Yang, Chuan-Pin Chiang, Chi-Wu Chen, Chang-Han Lee, Yi-Chao Wu, Mei-Hsiang Tsou, Yi-Huan Yang, Yu-San Chang, Wen-Chang Lin, Ding-Yen
container_volume	22
format_se	Elektronische Aufsätze
author-letter	Yang, Chuan-Pin
doi_str_mv	10.1186/s12929-015-0136-0
title_sort	identification and characterization of nuclear and nucleolar localization signals in 58-kda microspherule protein (msp58)
title_auth	Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58)
abstract	Background MSP58 is a nucleolar protein associated with rRNA transcription and cell proliferation. Its mechanism of translocation into the nucleus or the nucleolus, however, is not entirely known. In order to address this lack, the present study aims to determine a crucial part of this mechanism: the nuclear localization signal (NLS) and the nucleolar localization signal (NoLS) associated with the MSP58 protein. Results We have identified and characterized two NLSs in MSP58. The first is located between residues 32 and 56 (NLS1) and constitutes three clusters of basic amino acids (KRASSQALGTIPKRRSSSRFIKRKK); the second is situated between residues 113 and 123 (NLS2) and harbors a monopartite signal (PGLTKRVKKSK). Both NLS1 and NLS2 are highly conserved among different vertebrate species. Notably, one bipartite motif within the NLS1 (residues 44–56) appears to be absolutely necessary for MSP58 nucleolar localization. By yeast two-hybrid, pull-down, and coimmunoprecipitation analysis, we show that MSP58 binds to importin α1 and α6, suggesting that nuclear targeting of MSP58 utilizes a receptor-mediated and energy-dependent import mechanism. Functionally, our data show that both nuclear and nucleolar localization of MSP58 are crucial for transcriptional regulation on p21 and ribosomal RNA genes, and context-dependent effects on cell proliferation. Conclusions Results suggest that MSP58 subnuclear localization is regulated by two nuclear import signals, and that proper subcellular localization of MSP58 is critical for its role in transcriptional regulation. Our study reveals a molecular mechanism that controls nuclear and nucleolar localization of MSP58, a finding that might help future researchers understand the MSP58 biological signaling pathway. © Yang et al.; licensee BioMed Central. 2015. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
abstractGer	Background MSP58 is a nucleolar protein associated with rRNA transcription and cell proliferation. Its mechanism of translocation into the nucleus or the nucleolus, however, is not entirely known. In order to address this lack, the present study aims to determine a crucial part of this mechanism: the nuclear localization signal (NLS) and the nucleolar localization signal (NoLS) associated with the MSP58 protein. Results We have identified and characterized two NLSs in MSP58. The first is located between residues 32 and 56 (NLS1) and constitutes three clusters of basic amino acids (KRASSQALGTIPKRRSSSRFIKRKK); the second is situated between residues 113 and 123 (NLS2) and harbors a monopartite signal (PGLTKRVKKSK). Both NLS1 and NLS2 are highly conserved among different vertebrate species. Notably, one bipartite motif within the NLS1 (residues 44–56) appears to be absolutely necessary for MSP58 nucleolar localization. By yeast two-hybrid, pull-down, and coimmunoprecipitation analysis, we show that MSP58 binds to importin α1 and α6, suggesting that nuclear targeting of MSP58 utilizes a receptor-mediated and energy-dependent import mechanism. Functionally, our data show that both nuclear and nucleolar localization of MSP58 are crucial for transcriptional regulation on p21 and ribosomal RNA genes, and context-dependent effects on cell proliferation. Conclusions Results suggest that MSP58 subnuclear localization is regulated by two nuclear import signals, and that proper subcellular localization of MSP58 is critical for its role in transcriptional regulation. Our study reveals a molecular mechanism that controls nuclear and nucleolar localization of MSP58, a finding that might help future researchers understand the MSP58 biological signaling pathway. © Yang et al.; licensee BioMed Central. 2015. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
abstract_unstemmed	Background MSP58 is a nucleolar protein associated with rRNA transcription and cell proliferation. Its mechanism of translocation into the nucleus or the nucleolus, however, is not entirely known. In order to address this lack, the present study aims to determine a crucial part of this mechanism: the nuclear localization signal (NLS) and the nucleolar localization signal (NoLS) associated with the MSP58 protein. Results We have identified and characterized two NLSs in MSP58. The first is located between residues 32 and 56 (NLS1) and constitutes three clusters of basic amino acids (KRASSQALGTIPKRRSSSRFIKRKK); the second is situated between residues 113 and 123 (NLS2) and harbors a monopartite signal (PGLTKRVKKSK). Both NLS1 and NLS2 are highly conserved among different vertebrate species. Notably, one bipartite motif within the NLS1 (residues 44–56) appears to be absolutely necessary for MSP58 nucleolar localization. By yeast two-hybrid, pull-down, and coimmunoprecipitation analysis, we show that MSP58 binds to importin α1 and α6, suggesting that nuclear targeting of MSP58 utilizes a receptor-mediated and energy-dependent import mechanism. Functionally, our data show that both nuclear and nucleolar localization of MSP58 are crucial for transcriptional regulation on p21 and ribosomal RNA genes, and context-dependent effects on cell proliferation. Conclusions Results suggest that MSP58 subnuclear localization is regulated by two nuclear import signals, and that proper subcellular localization of MSP58 is critical for its role in transcriptional regulation. Our study reveals a molecular mechanism that controls nuclear and nucleolar localization of MSP58, a finding that might help future researchers understand the MSP58 biological signaling pathway. © Yang et al.; licensee BioMed Central. 2015. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (
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title_short	Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58)
url	https://dx.doi.org/10.1186/s12929-015-0136-0
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author2	Chiang, Chi-Wu Chen, Chang-Han Lee, Yi-Chao Wu, Mei-Hsiang Tsou, Yi-Huan Yang, Yu-San Chang, Wen-Chang Lin, Ding-Yen
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Identification and characterization of nuclear and nucleolar localization signals in 58-kDa microspherule protein (MSP58)

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