drosophila protein kinase ck2: genetics, regulatory complexity and emerging roles during development
Clicks: 163
ID: 128493
2016
Article Quality & Performance Metrics
Overall Quality
Improving Quality
0.0
/100
Combines engagement data with AI-assessed academic quality
Reader Engagement
Emerging Content
0.3
/100
1 views
1 readers
Trending
AI Quality Assessment
Not analyzed
Abstract
CK2 is a Ser/Thr protein kinase that is highly conserved amongst all eukaryotes. It is a well-known oncogenic kinase that regulates vital cell autonomous functions and animal development. Genetic studies in the fruit fly Drosophila are providing unique insights into the roles of CK2 in cell signaling, embryogenesis, organogenesis, neurogenesis, and the circadian clock, and are revealing hitherto unknown complexities in CK2 functions and regulation. Here, we review Drosophila CK2 with respect to its structure, subunit diversity, potential mechanisms of regulation, developmental abnormalities linked to mutations in the gene encoding CK2 subunits, and emerging roles in multiple aspects of eye development. We examine the Drosophila CK2 “interaction map” and the eye-specific “transcriptome” databases, which raise the prospect that this protein kinase has many additional targets in the developing eye. We discuss the possibility that CK2 functions during early retinal neurogenesis in Drosophila and mammals bear greater similarity than has been recognized, and that this conservation may extend to other developmental programs. Together, these studies underscore the immense power of the Drosophila model organism to provide new insights and avenues to further investigate developmentally relevant targets of this protein kinase.Reference Key |
bandyopadhyay2016pharmaceuticalsdrosophila
Use this key to autocite in the manuscript while using
SciMatic Manuscript Manager or Thesis Manager
|
---|---|
Authors | ;Mohna Bandyopadhyay;Scott Arbet;Clifton P. Bishop;Ashok P. Bidwai |
Journal | journal of cerebral blood flow and metabolism |
Year | 2016 |
DOI | 10.3390/ph10010004 |
URL | |
Keywords |
Citations
No citations found. To add a citation, contact the admin at info@scimatic.org
Comments
No comments yet. Be the first to comment on this article.