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Am J Physiol Cell Physiol 282: C205-C212, 2002;
0363-6143/02 $5.00
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Vol. 282, Issue 1, C205-C212, January 2002

Characterization of RIIbeta and D-AKAP1 in differentiated adipocytes

Archana Chaudhry, Chen Zhang, and James G. Granneman

CNS Molecular Sciences, Pfizer Global Research and Development, Ann Arbor 48105; and Department of Psychiatry and Behavioral Neurosciences, Wayne State University School of Medicine, Detroit, Michigan 48201

A-kinase anchoring proteins (AKAPs) have been proposed to regulate cAMP-dependent signaling in the cell by targeting RII subunits of protein kinase A (PKA) to specific subcellular compartments. RIIbeta is the predominant PKA subtype in adipose tissue. In gel overlay assays of C3H/10T1/2 adipocytes and adipose tissue, RIIbeta bound to several proteins including a prominent 132-kDa band, which was strongly induced upon differentiation of C3H/10T1/2 cells into adipocytes. Immunoblotting and nuclease protection analysis of C3H/10T1/2 cellular extracts identified this band as D-AKAP1/S-AKAP84, a putative AKAP. Immunocytochemical analysis of C3H/10T1/2 adipocytes revealed that most of D-AKAP1/S-AKAP84, but not RIIbeta , was colocalized with a mitochondrial-selective dye, MitoTracker red. These findings were further confirmed in studies where D-AKAP1/ S-AKAP84, but not RIIbeta , were localized in purified mitochondria made from C3H/10T1/2 adipocytes. Moreover, D-AKAP1, which is upregulated after differentiation, did not recruit RIIbeta to membrane fractions enriched in mitochondria. These results demonstrate that D-AKAP1/S-AKAP84 does not interact with PKA in differentiated C3H/10T1/2 adipocytes under the conditions tested.

anchoring proteins; adipose tissue; protein kinase A; adenosine 3',5'-cyclic monophosphate


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