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HIKE, a candidate protein binding site for PH domains, is a major regulatory region of Gβ proteins

✍ Scribed by Saverio Alberti

Publisher
John Wiley and Sons
Year
1999
Tongue
English
Weight
88 KB
Volume
35
Category
Article
ISSN
0887-3585

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✦ Synopsis

HIKE is a highly conserved sequence motif that selectively occurs in proteins candidate to bind PH domains, e.g., the ␤ subunit of heterotrimeric G proteins, kinases, ankyrin and kinesin. Thus, the HIKE region has been predicted to be a protein docking site for PH domains. This work evidentiates recent experimental evidence that unambiguously defines the functional role of HIKE in G ␤ as a multiple effector docking site and as a major regulatory region of G protein's function. Indeed, the G ␤ HIKE interacts with the ␤-adrenergic receptor kinase, G ␣ , G ␥ , adenylyl cyclase 2, phospholipase C ␤2, inward rectifier K channels, calcium channel ␣1B, calmodulin, phosducin, ste20. Quite interestingly, HIKE is located in the G ␤ region that faces the cell membrane. Thus, HIKE also interacts with the cell membrane and may dynamically regulate membrane vs effector binding of the G ␣␤␥ trimer. These findings fulfill a major prediction of the HIKE model, i.e., that HIKE is a regulatory region for protein-protein interactions. A role of HIKE as a proteic binding site for PH domains is supported by the profound influence of HIKE mutations on the largely PH-mediated binding of ␤-ARK to G ␤ . Pro-

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