Document Type
Article
Language
eng
Format of Original
13 p.
Publication Date
2012
Publisher
Rockefeller University Press
Source Publication
Journal of Cell Biology
Source ISSN
0021-9525
Original Item ID
doi: 10.1083/jcb.201111042
Abstract
A-kinase anchoring proteins (AKAPs) contain an amphipathic helix (AH) that binds the dimerization and docking (D/D) domain, RIIa, in cAMP-dependent protein kinase A (PKA). Many AKAPs were discovered solely based on the AH–RIIa interaction in vitro. An RIIa or a similar Dpy-30 domain is also present in numerous diverged molecules that are implicated in critical processes as diverse as flagellar beating, membrane trafficking, histone methylation, and stem cell differentiation, yet these molecules remain poorly characterized. Here we demonstrate that an AKAP, RSP3, forms a dimeric structural scaffold in the flagellar radial spoke complex, anchoring through two distinct AHs, the RIIa and Dpy-30 domains, in four non-PKA spoke proteins involved in the assembly and modulation of the complex. Interestingly, one AH can bind both RIIa and Dpy-30 domains in vitro. Thus, AHs and D/D domains constitute a versatile yet potentially promiscuous system for localizing various effector mechanisms. These results greatly expand the current concept about anchoring mechanisms and AKAPs.
Recommended Citation
Sivadas, Priyanka; Dienes, Jennifer M.; Maurice, Martin St.; Meek, William D.; and Yang, Pinfen, "A Flagellar A-Kinase Anchoring Protein with Two Amphipathic Helices Forms a Structural Scaffold in the Radial Spoke Complex" (2012). Biological Sciences Faculty Research and Publications. 121.
https://epublications.marquette.edu/bio_fac/121
Comments
Published version. Journal of Cell Biology, Vol. 199, No. 4 (2012): 639-651. Permalink. © 2012 Rockefeller University Press. Used with permission.