The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans

Microtubules are involved in mechanical support, cytoplasmic organization, and several cellular processes by interacting with diverse microtubule-associated proteins such as plus-end tracking proteins, motor proteins, and tubulin-folding cofactors. A number of the cytoskeleton-associated proteins (C...
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Autor*in:	Li Li Wang [verfasserIn] Kyung-Tae Lee [verfasserIn] Kwang-Woo Jung [verfasserIn] Dong-Gi Lee [verfasserIn] Yong-Sun Bahn [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2018

Schlagwörter:	Bik1 CAP-glycine human fungal pathogen meningoencephalitis SPEC Spc7 tubulin

Übergeordnetes Werk:	In: Virulence - Taylor & Francis Group, 2018, 9(2018), 1, Seite 566-584
Übergeordnetes Werk:	volume:9 ; year:2018 ; number:1 ; pages:566-584

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc Journal toc

DOI / URN:	10.1080/21505594.2017.1423189

Katalog-ID:	DOAJ019613628

Internformat


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245	1	4	\|a The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans
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520			\|a Microtubules are involved in mechanical support, cytoplasmic organization, and several cellular processes by interacting with diverse microtubule-associated proteins such as plus-end tracking proteins, motor proteins, and tubulin-folding cofactors. A number of the cytoskeleton-associated proteins (CAPs) contain the CAP-glycine-rich (CAP-Gly) domain, which is evolutionarily conserved and generally considered to bind to α-tubulin to regulate the function of microtubules. However, there has been a dearth of research on CAP-Gly proteins in fungal pathogens, including Cryptococcus neoformans, which is a global cause of fatal meningoencephalitis in immunocompromised patients. In this study, we identified five CAP-Gly protein-encoding genes in C. neoformans. Among these, Cgp1 encoded by CNAG_06352 has a unique domain structure containing CAP-Gly, SPEC, and Spc7 domains that is not orthologous to CAPs in other eukaryotes. Supporting the role of Cgp1 in microtubule-related function, we demonstrate that deletion or overexpression of CGP1 alters cellular susceptibility to thiabendazole, a microtubule destabilizer and that Cgp1 is co-localized with cytoplasmic microtubules. Related to the cellular function of microtubules, Cgp1 governs the maintenance of membrane stability and genotoxic stress responses. Deletion of CGP1 also reduces production of melanin pigment and attenuates the virulence of C. neoformans. Furthermore, we demonstrate that Cgp1 uniquely regulates the sexual differentiation of C. neoformans with distinct roles in the early and late stage of mating. Domain analysis revealed that the CAP-Gly domain plays a major role in all Cgp1 functions examined. In conclusion, this novel CAP-Gly protein, Cgp1, has pleotropic roles in regulating growth, stress responses, differentiation, and virulence in C. neoformans.
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Indexfelder

author_variant	l l w llw k t l ktl k w j kwj d g l dgl y s b ysb
matchkey_str	article:21505608:2018----::hnvlirtblascaecplcnpoeng1oengotdfeetainnvr
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allfields	10.1080/21505594.2017.1423189 doi (DE-627)DOAJ019613628 (DE-599)DOAJb8d0bf0a3e7142d2ae0792c412efefd0 DE-627 ger DE-627 rakwb eng RC109-216 Li Li Wang verfasserin aut The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Microtubules are involved in mechanical support, cytoplasmic organization, and several cellular processes by interacting with diverse microtubule-associated proteins such as plus-end tracking proteins, motor proteins, and tubulin-folding cofactors. A number of the cytoskeleton-associated proteins (CAPs) contain the CAP-glycine-rich (CAP-Gly) domain, which is evolutionarily conserved and generally considered to bind to α-tubulin to regulate the function of microtubules. However, there has been a dearth of research on CAP-Gly proteins in fungal pathogens, including Cryptococcus neoformans, which is a global cause of fatal meningoencephalitis in immunocompromised patients. In this study, we identified five CAP-Gly protein-encoding genes in C. neoformans. Among these, Cgp1 encoded by CNAG_06352 has a unique domain structure containing CAP-Gly, SPEC, and Spc7 domains that is not orthologous to CAPs in other eukaryotes. Supporting the role of Cgp1 in microtubule-related function, we demonstrate that deletion or overexpression of CGP1 alters cellular susceptibility to thiabendazole, a microtubule destabilizer and that Cgp1 is co-localized with cytoplasmic microtubules. Related to the cellular function of microtubules, Cgp1 governs the maintenance of membrane stability and genotoxic stress responses. Deletion of CGP1 also reduces production of melanin pigment and attenuates the virulence of C. neoformans. Furthermore, we demonstrate that Cgp1 uniquely regulates the sexual differentiation of C. neoformans with distinct roles in the early and late stage of mating. Domain analysis revealed that the CAP-Gly domain plays a major role in all Cgp1 functions examined. In conclusion, this novel CAP-Gly protein, Cgp1, has pleotropic roles in regulating growth, stress responses, differentiation, and virulence in C. neoformans. Bik1 CAP-glycine human fungal pathogen meningoencephalitis SPEC Spc7 tubulin Infectious and parasitic diseases Kyung-Tae Lee verfasserin aut Kwang-Woo Jung verfasserin aut Dong-Gi Lee verfasserin aut Yong-Sun Bahn verfasserin aut In Virulence Taylor & Francis Group, 2018 9(2018), 1, Seite 566-584 (DE-627)689717296 (DE-600)2657572-3 21505608 nnns volume:9 year:2018 number:1 pages:566-584 https://doi.org/10.1080/21505594.2017.1423189 kostenfrei https://doaj.org/article/b8d0bf0a3e7142d2ae0792c412efefd0 kostenfrei http://dx.doi.org/10.1080/21505594.2017.1423189 kostenfrei https://doaj.org/toc/2150-5594 Journal toc kostenfrei https://doaj.org/toc/2150-5608 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA 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_65 GBV_ILN_69 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_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2018 1 566-584
spelling	10.1080/21505594.2017.1423189 doi (DE-627)DOAJ019613628 (DE-599)DOAJb8d0bf0a3e7142d2ae0792c412efefd0 DE-627 ger DE-627 rakwb eng RC109-216 Li Li Wang verfasserin aut The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Microtubules are involved in mechanical support, cytoplasmic organization, and several cellular processes by interacting with diverse microtubule-associated proteins such as plus-end tracking proteins, motor proteins, and tubulin-folding cofactors. A number of the cytoskeleton-associated proteins (CAPs) contain the CAP-glycine-rich (CAP-Gly) domain, which is evolutionarily conserved and generally considered to bind to α-tubulin to regulate the function of microtubules. However, there has been a dearth of research on CAP-Gly proteins in fungal pathogens, including Cryptococcus neoformans, which is a global cause of fatal meningoencephalitis in immunocompromised patients. In this study, we identified five CAP-Gly protein-encoding genes in C. neoformans. Among these, Cgp1 encoded by CNAG_06352 has a unique domain structure containing CAP-Gly, SPEC, and Spc7 domains that is not orthologous to CAPs in other eukaryotes. Supporting the role of Cgp1 in microtubule-related function, we demonstrate that deletion or overexpression of CGP1 alters cellular susceptibility to thiabendazole, a microtubule destabilizer and that Cgp1 is co-localized with cytoplasmic microtubules. Related to the cellular function of microtubules, Cgp1 governs the maintenance of membrane stability and genotoxic stress responses. Deletion of CGP1 also reduces production of melanin pigment and attenuates the virulence of C. neoformans. Furthermore, we demonstrate that Cgp1 uniquely regulates the sexual differentiation of C. neoformans with distinct roles in the early and late stage of mating. Domain analysis revealed that the CAP-Gly domain plays a major role in all Cgp1 functions examined. In conclusion, this novel CAP-Gly protein, Cgp1, has pleotropic roles in regulating growth, stress responses, differentiation, and virulence in C. neoformans. Bik1 CAP-glycine human fungal pathogen meningoencephalitis SPEC Spc7 tubulin Infectious and parasitic diseases Kyung-Tae Lee verfasserin aut Kwang-Woo Jung verfasserin aut Dong-Gi Lee verfasserin aut Yong-Sun Bahn verfasserin aut In Virulence Taylor & Francis Group, 2018 9(2018), 1, Seite 566-584 (DE-627)689717296 (DE-600)2657572-3 21505608 nnns volume:9 year:2018 number:1 pages:566-584 https://doi.org/10.1080/21505594.2017.1423189 kostenfrei https://doaj.org/article/b8d0bf0a3e7142d2ae0792c412efefd0 kostenfrei http://dx.doi.org/10.1080/21505594.2017.1423189 kostenfrei https://doaj.org/toc/2150-5594 Journal toc kostenfrei https://doaj.org/toc/2150-5608 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA 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_65 GBV_ILN_69 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_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2018 1 566-584
allfields_unstemmed	10.1080/21505594.2017.1423189 doi (DE-627)DOAJ019613628 (DE-599)DOAJb8d0bf0a3e7142d2ae0792c412efefd0 DE-627 ger DE-627 rakwb eng RC109-216 Li Li Wang verfasserin aut The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Microtubules are involved in mechanical support, cytoplasmic organization, and several cellular processes by interacting with diverse microtubule-associated proteins such as plus-end tracking proteins, motor proteins, and tubulin-folding cofactors. A number of the cytoskeleton-associated proteins (CAPs) contain the CAP-glycine-rich (CAP-Gly) domain, which is evolutionarily conserved and generally considered to bind to α-tubulin to regulate the function of microtubules. However, there has been a dearth of research on CAP-Gly proteins in fungal pathogens, including Cryptococcus neoformans, which is a global cause of fatal meningoencephalitis in immunocompromised patients. In this study, we identified five CAP-Gly protein-encoding genes in C. neoformans. Among these, Cgp1 encoded by CNAG_06352 has a unique domain structure containing CAP-Gly, SPEC, and Spc7 domains that is not orthologous to CAPs in other eukaryotes. Supporting the role of Cgp1 in microtubule-related function, we demonstrate that deletion or overexpression of CGP1 alters cellular susceptibility to thiabendazole, a microtubule destabilizer and that Cgp1 is co-localized with cytoplasmic microtubules. Related to the cellular function of microtubules, Cgp1 governs the maintenance of membrane stability and genotoxic stress responses. Deletion of CGP1 also reduces production of melanin pigment and attenuates the virulence of C. neoformans. Furthermore, we demonstrate that Cgp1 uniquely regulates the sexual differentiation of C. neoformans with distinct roles in the early and late stage of mating. Domain analysis revealed that the CAP-Gly domain plays a major role in all Cgp1 functions examined. In conclusion, this novel CAP-Gly protein, Cgp1, has pleotropic roles in regulating growth, stress responses, differentiation, and virulence in C. neoformans. Bik1 CAP-glycine human fungal pathogen meningoencephalitis SPEC Spc7 tubulin Infectious and parasitic diseases Kyung-Tae Lee verfasserin aut Kwang-Woo Jung verfasserin aut Dong-Gi Lee verfasserin aut Yong-Sun Bahn verfasserin aut In Virulence Taylor & Francis Group, 2018 9(2018), 1, Seite 566-584 (DE-627)689717296 (DE-600)2657572-3 21505608 nnns volume:9 year:2018 number:1 pages:566-584 https://doi.org/10.1080/21505594.2017.1423189 kostenfrei https://doaj.org/article/b8d0bf0a3e7142d2ae0792c412efefd0 kostenfrei http://dx.doi.org/10.1080/21505594.2017.1423189 kostenfrei https://doaj.org/toc/2150-5594 Journal toc kostenfrei https://doaj.org/toc/2150-5608 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA 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_65 GBV_ILN_69 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_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2018 1 566-584
allfieldsGer	10.1080/21505594.2017.1423189 doi (DE-627)DOAJ019613628 (DE-599)DOAJb8d0bf0a3e7142d2ae0792c412efefd0 DE-627 ger DE-627 rakwb eng RC109-216 Li Li Wang verfasserin aut The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Microtubules are involved in mechanical support, cytoplasmic organization, and several cellular processes by interacting with diverse microtubule-associated proteins such as plus-end tracking proteins, motor proteins, and tubulin-folding cofactors. A number of the cytoskeleton-associated proteins (CAPs) contain the CAP-glycine-rich (CAP-Gly) domain, which is evolutionarily conserved and generally considered to bind to α-tubulin to regulate the function of microtubules. However, there has been a dearth of research on CAP-Gly proteins in fungal pathogens, including Cryptococcus neoformans, which is a global cause of fatal meningoencephalitis in immunocompromised patients. In this study, we identified five CAP-Gly protein-encoding genes in C. neoformans. Among these, Cgp1 encoded by CNAG_06352 has a unique domain structure containing CAP-Gly, SPEC, and Spc7 domains that is not orthologous to CAPs in other eukaryotes. Supporting the role of Cgp1 in microtubule-related function, we demonstrate that deletion or overexpression of CGP1 alters cellular susceptibility to thiabendazole, a microtubule destabilizer and that Cgp1 is co-localized with cytoplasmic microtubules. Related to the cellular function of microtubules, Cgp1 governs the maintenance of membrane stability and genotoxic stress responses. Deletion of CGP1 also reduces production of melanin pigment and attenuates the virulence of C. neoformans. Furthermore, we demonstrate that Cgp1 uniquely regulates the sexual differentiation of C. neoformans with distinct roles in the early and late stage of mating. Domain analysis revealed that the CAP-Gly domain plays a major role in all Cgp1 functions examined. In conclusion, this novel CAP-Gly protein, Cgp1, has pleotropic roles in regulating growth, stress responses, differentiation, and virulence in C. neoformans. Bik1 CAP-glycine human fungal pathogen meningoencephalitis SPEC Spc7 tubulin Infectious and parasitic diseases Kyung-Tae Lee verfasserin aut Kwang-Woo Jung verfasserin aut Dong-Gi Lee verfasserin aut Yong-Sun Bahn verfasserin aut In Virulence Taylor & Francis Group, 2018 9(2018), 1, Seite 566-584 (DE-627)689717296 (DE-600)2657572-3 21505608 nnns volume:9 year:2018 number:1 pages:566-584 https://doi.org/10.1080/21505594.2017.1423189 kostenfrei https://doaj.org/article/b8d0bf0a3e7142d2ae0792c412efefd0 kostenfrei http://dx.doi.org/10.1080/21505594.2017.1423189 kostenfrei https://doaj.org/toc/2150-5594 Journal toc kostenfrei https://doaj.org/toc/2150-5608 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA 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_65 GBV_ILN_69 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_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2018 1 566-584
allfieldsSound	10.1080/21505594.2017.1423189 doi (DE-627)DOAJ019613628 (DE-599)DOAJb8d0bf0a3e7142d2ae0792c412efefd0 DE-627 ger DE-627 rakwb eng RC109-216 Li Li Wang verfasserin aut The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans 2018 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Microtubules are involved in mechanical support, cytoplasmic organization, and several cellular processes by interacting with diverse microtubule-associated proteins such as plus-end tracking proteins, motor proteins, and tubulin-folding cofactors. A number of the cytoskeleton-associated proteins (CAPs) contain the CAP-glycine-rich (CAP-Gly) domain, which is evolutionarily conserved and generally considered to bind to α-tubulin to regulate the function of microtubules. However, there has been a dearth of research on CAP-Gly proteins in fungal pathogens, including Cryptococcus neoformans, which is a global cause of fatal meningoencephalitis in immunocompromised patients. In this study, we identified five CAP-Gly protein-encoding genes in C. neoformans. Among these, Cgp1 encoded by CNAG_06352 has a unique domain structure containing CAP-Gly, SPEC, and Spc7 domains that is not orthologous to CAPs in other eukaryotes. Supporting the role of Cgp1 in microtubule-related function, we demonstrate that deletion or overexpression of CGP1 alters cellular susceptibility to thiabendazole, a microtubule destabilizer and that Cgp1 is co-localized with cytoplasmic microtubules. Related to the cellular function of microtubules, Cgp1 governs the maintenance of membrane stability and genotoxic stress responses. Deletion of CGP1 also reduces production of melanin pigment and attenuates the virulence of C. neoformans. Furthermore, we demonstrate that Cgp1 uniquely regulates the sexual differentiation of C. neoformans with distinct roles in the early and late stage of mating. Domain analysis revealed that the CAP-Gly domain plays a major role in all Cgp1 functions examined. In conclusion, this novel CAP-Gly protein, Cgp1, has pleotropic roles in regulating growth, stress responses, differentiation, and virulence in C. neoformans. Bik1 CAP-glycine human fungal pathogen meningoencephalitis SPEC Spc7 tubulin Infectious and parasitic diseases Kyung-Tae Lee verfasserin aut Kwang-Woo Jung verfasserin aut Dong-Gi Lee verfasserin aut Yong-Sun Bahn verfasserin aut In Virulence Taylor & Francis Group, 2018 9(2018), 1, Seite 566-584 (DE-627)689717296 (DE-600)2657572-3 21505608 nnns volume:9 year:2018 number:1 pages:566-584 https://doi.org/10.1080/21505594.2017.1423189 kostenfrei https://doaj.org/article/b8d0bf0a3e7142d2ae0792c412efefd0 kostenfrei http://dx.doi.org/10.1080/21505594.2017.1423189 kostenfrei https://doaj.org/toc/2150-5594 Journal toc kostenfrei https://doaj.org/toc/2150-5608 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA 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_65 GBV_ILN_69 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_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 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_4338 GBV_ILN_4367 GBV_ILN_4700 AR 9 2018 1 566-584
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topic_title	RC109-216 The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans Bik1 CAP-glycine human fungal pathogen meningoencephalitis SPEC Spc7 tubulin
topic	misc RC109-216 misc Bik1 misc CAP-glycine misc human fungal pathogen misc meningoencephalitis misc SPEC misc Spc7 misc tubulin misc Infectious and parasitic diseases
topic_unstemmed	misc RC109-216 misc Bik1 misc CAP-glycine misc human fungal pathogen misc meningoencephalitis misc SPEC misc Spc7 misc tubulin misc Infectious and parasitic diseases
topic_browse	misc RC109-216 misc Bik1 misc CAP-glycine misc human fungal pathogen misc meningoencephalitis misc SPEC misc Spc7 misc tubulin misc Infectious and parasitic diseases
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title	The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans
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title_full	The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans
author_sort	Li Li Wang
journal	Virulence
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author_browse	Li Li Wang Kyung-Tae Lee Kwang-Woo Jung Dong-Gi Lee Yong-Sun Bahn
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class	RC109-216
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author-letter	Li Li Wang
doi_str_mv	10.1080/21505594.2017.1423189
author2-role	verfasserin
title_sort	novel microtubule-associated cap-glycine protein cgp1 governs growth, differentiation, and virulence of cryptococcus neoformans
callnumber	RC109-216
title_auth	The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans
abstract	Microtubules are involved in mechanical support, cytoplasmic organization, and several cellular processes by interacting with diverse microtubule-associated proteins such as plus-end tracking proteins, motor proteins, and tubulin-folding cofactors. A number of the cytoskeleton-associated proteins (CAPs) contain the CAP-glycine-rich (CAP-Gly) domain, which is evolutionarily conserved and generally considered to bind to α-tubulin to regulate the function of microtubules. However, there has been a dearth of research on CAP-Gly proteins in fungal pathogens, including Cryptococcus neoformans, which is a global cause of fatal meningoencephalitis in immunocompromised patients. In this study, we identified five CAP-Gly protein-encoding genes in C. neoformans. Among these, Cgp1 encoded by CNAG_06352 has a unique domain structure containing CAP-Gly, SPEC, and Spc7 domains that is not orthologous to CAPs in other eukaryotes. Supporting the role of Cgp1 in microtubule-related function, we demonstrate that deletion or overexpression of CGP1 alters cellular susceptibility to thiabendazole, a microtubule destabilizer and that Cgp1 is co-localized with cytoplasmic microtubules. Related to the cellular function of microtubules, Cgp1 governs the maintenance of membrane stability and genotoxic stress responses. Deletion of CGP1 also reduces production of melanin pigment and attenuates the virulence of C. neoformans. Furthermore, we demonstrate that Cgp1 uniquely regulates the sexual differentiation of C. neoformans with distinct roles in the early and late stage of mating. Domain analysis revealed that the CAP-Gly domain plays a major role in all Cgp1 functions examined. In conclusion, this novel CAP-Gly protein, Cgp1, has pleotropic roles in regulating growth, stress responses, differentiation, and virulence in C. neoformans.
abstractGer	Microtubules are involved in mechanical support, cytoplasmic organization, and several cellular processes by interacting with diverse microtubule-associated proteins such as plus-end tracking proteins, motor proteins, and tubulin-folding cofactors. A number of the cytoskeleton-associated proteins (CAPs) contain the CAP-glycine-rich (CAP-Gly) domain, which is evolutionarily conserved and generally considered to bind to α-tubulin to regulate the function of microtubules. However, there has been a dearth of research on CAP-Gly proteins in fungal pathogens, including Cryptococcus neoformans, which is a global cause of fatal meningoencephalitis in immunocompromised patients. In this study, we identified five CAP-Gly protein-encoding genes in C. neoformans. Among these, Cgp1 encoded by CNAG_06352 has a unique domain structure containing CAP-Gly, SPEC, and Spc7 domains that is not orthologous to CAPs in other eukaryotes. Supporting the role of Cgp1 in microtubule-related function, we demonstrate that deletion or overexpression of CGP1 alters cellular susceptibility to thiabendazole, a microtubule destabilizer and that Cgp1 is co-localized with cytoplasmic microtubules. Related to the cellular function of microtubules, Cgp1 governs the maintenance of membrane stability and genotoxic stress responses. Deletion of CGP1 also reduces production of melanin pigment and attenuates the virulence of C. neoformans. Furthermore, we demonstrate that Cgp1 uniquely regulates the sexual differentiation of C. neoformans with distinct roles in the early and late stage of mating. Domain analysis revealed that the CAP-Gly domain plays a major role in all Cgp1 functions examined. In conclusion, this novel CAP-Gly protein, Cgp1, has pleotropic roles in regulating growth, stress responses, differentiation, and virulence in C. neoformans.
abstract_unstemmed	Microtubules are involved in mechanical support, cytoplasmic organization, and several cellular processes by interacting with diverse microtubule-associated proteins such as plus-end tracking proteins, motor proteins, and tubulin-folding cofactors. A number of the cytoskeleton-associated proteins (CAPs) contain the CAP-glycine-rich (CAP-Gly) domain, which is evolutionarily conserved and generally considered to bind to α-tubulin to regulate the function of microtubules. However, there has been a dearth of research on CAP-Gly proteins in fungal pathogens, including Cryptococcus neoformans, which is a global cause of fatal meningoencephalitis in immunocompromised patients. In this study, we identified five CAP-Gly protein-encoding genes in C. neoformans. Among these, Cgp1 encoded by CNAG_06352 has a unique domain structure containing CAP-Gly, SPEC, and Spc7 domains that is not orthologous to CAPs in other eukaryotes. Supporting the role of Cgp1 in microtubule-related function, we demonstrate that deletion or overexpression of CGP1 alters cellular susceptibility to thiabendazole, a microtubule destabilizer and that Cgp1 is co-localized with cytoplasmic microtubules. Related to the cellular function of microtubules, Cgp1 governs the maintenance of membrane stability and genotoxic stress responses. Deletion of CGP1 also reduces production of melanin pigment and attenuates the virulence of C. neoformans. Furthermore, we demonstrate that Cgp1 uniquely regulates the sexual differentiation of C. neoformans with distinct roles in the early and late stage of mating. Domain analysis revealed that the CAP-Gly domain plays a major role in all Cgp1 functions examined. In conclusion, this novel CAP-Gly protein, Cgp1, has pleotropic roles in regulating growth, stress responses, differentiation, and virulence in C. neoformans.
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container_issue	1
title_short	The novel microtubule-associated CAP-glycine protein Cgp1 governs growth, differentiation, and virulence of Cryptococcus neoformans
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