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J. Biol. Chem., Vol. 282, Issue 45, 33155-33167, November 9, 2007

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MyRIP Anchors Protein Kinase A to the Exocyst Complex^*

From the Howard Hughes Medical Institute, Vollum Institute, Oregon Health & Science University, Portland, Oregon 97239

The movement of signal transduction enzymes in and out of multi-protein complexes coordinates the spatial and temporal resolution of cellular events. Anchoring and scaffolding proteins are key to this process because they sequester protein kinases and phosphatases with a subset of their preferred substrates. The protein kinase A-anchoring family of proteins (AKAPs), which target the cAMP-dependent protein kinase (PKA) and other enzymes to defined subcellular microenvironments, represent a well studied group of these signal-organizing molecules. In this report we demonstrate that the Rab27a GTPase effector protein MyRIP is a member of the AKAP family. The zebrafish homolog of MyRIP (Ze-AKAP2) was initially detected in a two-hybrid screen for AKAPs. A combination of biochemical, cell-based, and immunofluorescence approaches demonstrate that the mouse MyRIP ortholog targets the type II PKA holoenzyme via an atypical mechanism to a specific perinuclear region of insulin-secreting cells. Similar approaches show that MyRIP interacts with the Sec6 and Sec8 components of the exocyst complex, an evolutionarily conserved protein unit that controls protein trafficking and exocytosis. These data indicate that MyRIP functions as a scaffolding protein that links PKA to components of the exocytosis machinery.

Received for publication, June 22, 2007 , and in revised form, August 28, 2007.

^* This work was supported by National Institutes of Health Grants 5 F32HL074647 (to A. S. G.) and GM48231 (to J. D. S.) and by a postdoctoral fellowship from the Canadian Institutes of Health Research (to S. A. H.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Howard Hughes Medical Institute, Vollum Institute, Oregon Health & Science University, 3181 S.W. Sam Jackson Park Rd., Portland, OR 97239. Tel.: 503-494-4652; Fax: 503-494-0519; E-mail: scott{at}ohsu.edu.

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