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J Biol Chem, Vol. 274, Issue 17, 12124-12128, April 23, 1999

Phosphorylation of F-actin-Associating G Protein ₁₂ Subunit Enhances Fibroblast Motility

Hiroshi Ueda, Junji Yamauchi^§, Hiroshi Itoh^§, Rika Morishita, Yoshito Kaziro^§, Kanefusa Kato, and Tomiko Asano

From the  Department of Biochemistry, Institute for Developmental Research, Aichi Human Service Center, Kasugai, Aichi 480-0392 and the ^§ Department of Biological Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Midori-ku, Yokohama 226-8501, Japan

Eleven isoforms of G protein  subunit have been found thus far, but the precise roles of individual  subunits are not known. The ₁₂ subunit has two unique properties: phosphorylation by protein kinase C and association with F-actin. To elucidate the role of ₁₂, we overexpressed ₁₂ and other  subunits in NIH 3T3 cells together with the ₁ subunit. The overexpressed ₁₂ as well as endogenous ₁₂, but not ₂, ₅, and ₇ subunits, associated with cytoskeletal components. Expression of ₁₂ induced remarkable changes including cell rounding, disruption of stress fibers, and enhancement of cell migration, but expression of other  subunits did not induce significant changes. Deletion of the N-terminal region of ₁₂ decreased the abilities of ₁₂ to associate with cytoskeletal fractions, to induce cell rounding, and to increase cell motility. Replacement by alanine of Ser² of ₁₂ (Ser¹ of a mature ₁₂ protein), a phosphorylation site for protein kinase C, eliminated these effects of ₁₂, whereas a mutant in which Ser² was replaced with glutamic acid showed effects equivalent to wild-type ₁₂. These results indicate that phosphorylation of ₁₂ at Ser² enhances the motility of cells.

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