Abstract
Regarded as constitutively active enzymes, known to participate in many, diverse biological processes, the intracellular regulation bestowed on the CK1 family of serine/threonine protein kinases is critically important, yet poorly understood. Here, we provide an overview of the known CK1-dependent cellular functions and review the emerging roles of CK1-regulating proteins in these processes. We go on to discuss the advances, limitations and pitfalls that CK1 researchers encounter when attempting to define relationships between CK1 isoforms and their substrates, and the challenges associated with ascertaining the correct physiological CK1 isoform for the substrate of interest. With increasing interest in CK1 isoforms as therapeutic targets, methods of selectively inhibiting CK1 isoform-specific processes is warranted, yet challenging to achieve given their participation in such a vast plethora of signalling pathways. Here, we discuss how one might shut down CK1-specific processes, without impacting other aspects of CK1 biology.
Highlights
The post-translational modification of proteins offers multiple and diverse ways of controlling protein function
Of the post-translational modifications that proteins can undergo in cells, phosphorylation is perhaps one of the best studied to date
Many studies use casein kinase 2 (CK2) as a control in experiments seeking to prove that the phosphorylation of the substrate of interest is specific to casein kinase 1 (CK1), whereas they are unrelated enzymes
Summary
The post-translational modification of proteins offers multiple and diverse ways of controlling protein function.
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