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Env7p associates with the golgin protein Imh1 at the trans-Golgi network in Candida albicans

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Title Env7p associates with the golgin protein Imh1 at the trans-Golgi network in Candida albicans
 
Creator Rao, Kongara Hanumantha
Ghosh, Swagata
Datta, Asis
 
Subject Candida albicans
Golgin Protein
trans-Golgi Network
 
Description Accepted date: June 29, 2016
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.
We are grateful to Judith Berman, A. J. P. Brown, Masakazu Niimi, W. A. Fonzi, Jim Dover, and A. D. Johnson for their generous gifts of Candida albicans strains and plasmids used in this study. We also thank Sunita Prakash, Proteomics Facility, Molecular Biophysics Unit, Indian Institute of Science, Bangalore, for identification of proteins and Prabhat Kumar, AIRF, JNU, for help in capturing confocal images. S.G. acknowledges a Personal Research Grant from Kalyani University and the grant received from the DST-PURSE scheme. K.H.R. is a recipient of a Senior Research Associate Fellowship from the Council of Scientific Industrial Research, India.
 
Date 2016-08-11T11:10:11Z
2016-08-11T11:10:11Z
2016
 
Type Article
 
Identifier mSphere, 1(4): e00080-16
2379-5042
http://172.16.0.77:8080/jspui/handle/123456789/675
http://msphere.asm.org/content/1/4/e00080-16
10.1128/mSphere.00080-16
 
Language en_US
 
Publisher American Society for Microbiology