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Signaling of the direction-sensing FAK/RACK1/PDE4D5 complex to the small GTPase Rap1

Content Provider	PubMed Central
Author	Bryan, Serrels Sandilands, Emma Frame, Margaret C.
Copyright Year	2011
Abstract	We recently reported that a complex between focal adhesion kianse (FAK) and the molecular scaffold RACK1 controlled nascent integrin adhesion formation and cell polarization, via peripheral recruitment of the cAMP - degrading PDE4D5 isoform. Here we review and extend these studies by demonstrating that the FAK/RACK1/PDE4D5 ‘direction-sensing’ complex likely functions by signaling, via the guanine nucleotide exchange factor EPAC , to its small GTPase target Rap1. Specifically, activating EPAC suppresses polarization of squamous cancer cells, while, in contrast, modulating PKA, the other major cAMP effector, has no effect. Moreover, FAK-deficient malignant keratinocytes re-expressing a FAK mutant that cannot bind to RACK1, namely FAK-E139A,D140A, display elevated Rap1 that is linked to impaired polarization. Thus, it is likely that the FAK/RACK1/PDE4D5 complex signals to keep Rap1 low at appropriate times and in a spatially-regulated manner as cells first sense their environment and make decisions about nascent adhesion stabilization and polarization. RACK1 is abundantly expressed in both normal and malignant keratinocytes, while FAK and PDE4D5 are both elevated in the cancer cells, suggesting that the FAK/RACK1/PDE4D5/Rap1 signaling axis may contribute to FAK's well documented role in tumor progression.
Related Links	http://dx.doi.org/10.4161/sgtp.2.1.15137
Ending Page	61
Page Count	8
Starting Page	54
File Format	PDF
ISSN	21541248
e-ISSN	21541256
Journal	Small GTPases
Issue Number	1
Volume Number	2
Language	English
Publisher	Landes Bioscience
Publisher Date	2011-01-01
Access Restriction	Open
Rights Holder	Landes Bioscience
Subject Keyword	Biomaterials Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry

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