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Volume 271, Number 42, Issue of October 18, 1996 pp. 26200-26208
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

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Evidence for Endogenous ADP-ribosylation of GTP-binding Proteins in Neuronal Cell Nucleus
POSSIBLE INDUCTION BY MEMBRANE DEPOLARIZATION

(Received for publication, September 6, 1995, and in revised form, July 31, 1996)

Malca Cohen-Armon , Ilan Hammel ^¶ , Yosef Anis , Shirley Homburg and Noya Dekel

From the  Department of Physiology and Pharmacology, Neufeld Cardiac Research Institute and ^¶ Department of Pathology, Sackler School of Medicine, Tel-Aviv University, 69978 Tel-Aviv, Israel

GTP-binding protein(s) recognized by antibodies against the -subunits of G_i- and G_o-proteins were detected in crude nuclei isolated from rat brain stem and cortex. Immunohistochemical staining indicated that in the cortex these proteins are perinuclear, or are embedded in the nuclear membrane. Evidence is presented for an endogenous ADP-ribosylation of these proteins, which competes with their PTX-catalyzed ADP-ribosylation. The endogenous reaction has the characteristics of nonenzymatic ADP-ribosylation of cysteine residues, known to involve NAD-glycohydrolase activity. In vitro experiments showed that the -subunit of G_o-proteins in the cell membrane also acts as a substrate of this endogenous ADP-ribosylation. The in situ effect of membrane depolarization on the nuclear GTP-binding proteins may be attributable to their depolarization-induced endogenous ADP-ribosylation, suggesting a novel signaling mechanism in neuronal cells in the central nervous system.

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