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© The Rockefeller University Press, 0021-9525/2002/8/659 $5.00
The Journal of Cell Biology, Volume 158, Number 4, August 19, 2002 659-668

Rab32 is an A-kinase anchoring protein and participates in mitochondrial dynamics

¹ Howard Hughes Medical Institute, Vollum Institute
² Department of Cellular and Developmental Biology, Oregon Health and Sciences University, Portland, OR 97201

Address correspondence to John D. Scott, Howard Hughes Medical Institute, Vollum Institute, Oregon Health and Sciences University, 3181 S.W. Sam Jackson Park Road, Portland, OR 97201. Tel.: (503) 494-4652. Fax: (503) 494-0519. E-mail: scott{at}ohsu.edu

A-kinase anchoring proteins (AKAPs) tether the cAMP-dependent protein kinase (PKA) and other signaling enzymes to distinct subcellular organelles. Using the yeast two-hybrid approach, we demonstrate that Rab32, a member of the Ras superfamily of small molecular weight G-proteins, interacts directly with the type II regulatory subunit of PKA. Cellular and biochemical studies confirm that Rab32 functions as an AKAP inside cells. Anchoring determinants for PKA have been mapped to sites within the conserved 5 helix that is common to all Rab family members. Subcellular fractionation and immunofluorescent approaches indicate that Rab32 and a proportion of the cellular PKA pool are associated with mitochondria. Transient transfection of a GTP binding–deficient mutant of Rab32 promotes aberrant accumulation of mitochondria at the microtubule organizing center. Further analysis of this mutant indicates that disruption of the microtubule cytoskeleton results in aberrantly elongated mitochondria. This implicates Rab32 as a participant in synchronization of mitochondrial fission. Thus, Rab32 is a dual function protein that participates in both mitochondrial anchoring of PKA and mitochondrial dynamics.

Key Words: protein kinase; cAMP; anchoring protein; Rab protein; mitochondria

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