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Updated: Feb 15, 2026

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
Published on: May 3, 2018
A novel encystation specific protein kinase regulates chitin synthesis in Entamoeba invadens
Sintu Kumar Samanta1, Sneha Susan Varghese1, Deepak Krishnan1
1Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur 721302, India.
Abstract:
Phosphorylation is an important post-translational modification of proteins and is involved in the regulation of a variety of cellular events. The proteome of Entamoeba invadens, the reptilian counterpart of Entamoeba histolytica consists of an overwhelming number of putative protein kinases, and some may have a role to play in Entamoeba encystation. In this study, we have identified a novel protein kinase named as EiCSpk (Entamoeba invadenscyst specific protein kinase) which expressed almost exclusively during encystation. It is an active Protein kinase C with a characteristic substrate phosphorylation and auto-phosphorylation property. Gene silencing study has unveiled its role as a regulator of chitin synthesis through transcriptional activation of the chitin synthesis pathway genes along with glycogen phosphorylases that are involved in the influx of glucose from glycogen breakdown for chitin synthesis.
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