Abstract
The role of CK2beta has been defined as the regulatory subunit of protein kinase CK2, which is a heterotetrameric complex composed of two CK2beta and two catalytic active CK2alpha subunits. The identification of other serine/threonine kinases such as A-Raf, Chk1, and c-Mos that interact with and are regulated by CK2beta has challenged this view and provided evidence for functions of CK2beta outside the CK2 holoenzyme. In this report we describe the first interaction of Drosophila CK2beta outside the CK2 holoenzyme with p21-activated kinase (PAK) proteins. This interaction is seen for distinct PAK and CK2beta isoforms. In contrast to the CK2alpha-CK2beta interaction, dimer formation of the CK2beta subunits is not a prerequisite for binding of PAK proteins. Our results support the idea that CK2beta can bind to PAK proteins in a CK2alpha independent manner and negatively regulates PAK kinase activity.
