Env7p Associates with the Golgin Protein Imh1 at the <italic toggle="yes">trans</italic>-Golgi Network in <named-content content-type="genus-species">Candida albicans</named-content>

ABSTRACT Vesicular dynamics is one of the very important aspects of cellular physiology, an imbalance of which leads to the disorders or diseases in higher eukaryotes. We report the functional characterization of a palmitoylated protein kinase from Candida albicans whose homologue in Saccharomyces c...

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Autores principales:	Kongara Hanumantha Rao, Swagata Ghosh, Asis Datta
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2016
Materias:	Candida albicans Env7 Imh1 trans-Golgi network palmitoylation virulence Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/12faa2e2c8264a28917afb559eea4682
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spelling	oai:doaj.org-article:12faa2e2c8264a28917afb559eea46822021-11-15T15:21:14ZEnv7p Associates with the Golgin Protein Imh1 at the <italic toggle="yes">trans</italic>-Golgi Network in <named-content content-type="genus-species">Candida albicans</named-content>10.1128/mSphere.00080-162379-5042https://doaj.org/article/12faa2e2c8264a28917afb559eea46822016-08-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mSphere.00080-16https://doaj.org/toc/2379-5042ABSTRACT Vesicular dynamics is one of the very important aspects of cellular physiology, an imbalance of which leads to the disorders or diseases in higher eukaryotes. We report the functional characterization of a palmitoylated protein kinase from Candida albicans whose homologue in Saccharomyces cerevisiae has been reported to be involved in negative regulation of membrane fusion and was named Env7. However, the downstream target of this protein remains to be identified. Env7 in C. albicans (CaEnv7) could be isolated from the membrane fraction and localized to vesicular structures associated with the Golgi apparatus. Our work reports Env7 in C. albicans as a new player involved in maintaining the functional dynamics at the trans-Golgi network (TGN) by interacting with two other TGN-resident proteins, namely, Imh1p and Arl1p. Direct interaction could be detected between Env7p and the golgin protein Imh1p. Env7 is itself phosphorylated (Env7p) and phosphorylates Imh1 in vivo. An interaction between Env7 and Imh1 is required for the targeted localization of Imh1. CaEnv7 has a putative palmitoylation site toward both N and C termini. An N-terminal palmitoylation-defective strain retains its ability to phosphorylate Imh1 in vitro. An ENV7 homozygous mutant showed compromised filamentation in solid media and attenuated virulence, whereas an overexpressed strain affected cell wall integrity. Thus, Env7 plays a subtle but important role at the level of multitier regulation that exists at the TGN. IMPORTANCE A multitier regulation exists at the trans-Golgi network in all higher organisms. We report a palmitoylated protein kinase, Env7, that functions at the TGN interface by interacting with two more TGN-resident proteins, namely, Imh1 and Arl1. Palmitoylation seems to be important for the specific localization. This study focuses on the involvement of a ubiquitous protein kinase, whose substrates had not yet been reported from any organism, as an upstream signaling component that modulates the activity of the Imh1-Arl1 complex crucial for maintaining membrane asymmetry. Virulence is significantly diminished in an Env7 mutant. The functioning of this protein in C. albicans seems to be quite different from its nearest homologue in S. cerervisiae, which reflects the evolutionary divergence between these two organisms.Kongara Hanumantha RaoSwagata GhoshAsis DattaAmerican Society for MicrobiologyarticleCandida albicansEnv7Imh1trans-Golgi networkpalmitoylationvirulenceMicrobiologyQR1-502ENmSphere, Vol 1, Iss 4 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Candida albicans Env7 Imh1 trans-Golgi network palmitoylation virulence Microbiology QR1-502
spellingShingle	Candida albicans Env7 Imh1 trans-Golgi network palmitoylation virulence Microbiology QR1-502 Kongara Hanumantha Rao Swagata Ghosh Asis Datta Env7p Associates with the Golgin Protein Imh1 at the <italic toggle="yes">trans</italic>-Golgi Network in <named-content content-type="genus-species">Candida albicans</named-content>
description	ABSTRACT Vesicular dynamics is one of the very important aspects of cellular physiology, an imbalance of which leads to the disorders or diseases in higher eukaryotes. We report the functional characterization of a palmitoylated protein kinase from Candida albicans whose homologue in Saccharomyces cerevisiae has been reported to be involved in negative regulation of membrane fusion and was named Env7. However, the downstream target of this protein remains to be identified. Env7 in C. albicans (CaEnv7) could be isolated from the membrane fraction and localized to vesicular structures associated with the Golgi apparatus. Our work reports Env7 in C. albicans as a new player involved in maintaining the functional dynamics at the trans-Golgi network (TGN) by interacting with two other TGN-resident proteins, namely, Imh1p and Arl1p. Direct interaction could be detected between Env7p and the golgin protein Imh1p. Env7 is itself phosphorylated (Env7p) and phosphorylates Imh1 in vivo. An interaction between Env7 and Imh1 is required for the targeted localization of Imh1. CaEnv7 has a putative palmitoylation site toward both N and C termini. An N-terminal palmitoylation-defective strain retains its ability to phosphorylate Imh1 in vitro. An ENV7 homozygous mutant showed compromised filamentation in solid media and attenuated virulence, whereas an overexpressed strain affected cell wall integrity. Thus, Env7 plays a subtle but important role at the level of multitier regulation that exists at the TGN. IMPORTANCE A multitier regulation exists at the trans-Golgi network in all higher organisms. We report a palmitoylated protein kinase, Env7, that functions at the TGN interface by interacting with two more TGN-resident proteins, namely, Imh1 and Arl1. Palmitoylation seems to be important for the specific localization. This study focuses on the involvement of a ubiquitous protein kinase, whose substrates had not yet been reported from any organism, as an upstream signaling component that modulates the activity of the Imh1-Arl1 complex crucial for maintaining membrane asymmetry. Virulence is significantly diminished in an Env7 mutant. The functioning of this protein in C. albicans seems to be quite different from its nearest homologue in S. cerervisiae, which reflects the evolutionary divergence between these two organisms.
format	article
author	Kongara Hanumantha Rao Swagata Ghosh Asis Datta
author_facet	Kongara Hanumantha Rao Swagata Ghosh Asis Datta
author_sort	Kongara Hanumantha Rao
title	Env7p Associates with the Golgin Protein Imh1 at the <italic toggle="yes">trans</italic>-Golgi Network in <named-content content-type="genus-species">Candida albicans</named-content>
title_short	Env7p Associates with the Golgin Protein Imh1 at the <italic toggle="yes">trans</italic>-Golgi Network in <named-content content-type="genus-species">Candida albicans</named-content>
title_full	Env7p Associates with the Golgin Protein Imh1 at the <italic toggle="yes">trans</italic>-Golgi Network in <named-content content-type="genus-species">Candida albicans</named-content>
title_fullStr	Env7p Associates with the Golgin Protein Imh1 at the <italic toggle="yes">trans</italic>-Golgi Network in <named-content content-type="genus-species">Candida albicans</named-content>
title_full_unstemmed	Env7p Associates with the Golgin Protein Imh1 at the <italic toggle="yes">trans</italic>-Golgi Network in <named-content content-type="genus-species">Candida albicans</named-content>
title_sort	env7p associates with the golgin protein imh1 at the <italic toggle="yes">trans</italic>-golgi network in <named-content content-type="genus-species">candida albicans</named-content>
publisher	American Society for Microbiology
publishDate	2016
url	https://doaj.org/article/12faa2e2c8264a28917afb559eea4682
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Env7p Associates with the Golgin Protein Imh1 at the <italic toggle="yes">trans</italic>-Golgi Network in <named-content content-type="genus-species">Candida albicans</named-content>

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