Abstract
Rab proteins are small Ras-like GTPases that regulate vesicular trafficking events in the cell. More than 50 Rabs have been described in mammalian cells (1), each with a specific subcellular localization reflecting the functional specificity of Rabs to specific trafficking steps (2–5). Rabs contain two cysteine residues at or near the carboxyl terminus, arranged in a variety of motifs. Both cysteine residues are modified by the attachment of geranylgeranyl groups via thioether bonds, in a reaction catalyzed by Rab geranylgeranyl transferase (also known as GGTase type II, RGGT) (6). This enzyme is a tightly bound heterodimer, composed of a 60-kDa α-subunit and a 38-kDa β-subunit, both related to the α- and β-subunits of the other known protein prenyltransferases, farnesyl transferase and caax geranylgeranyl transferase (also known as GGTase type I).
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References
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Pereira-Leal, J.B., Gomes, A.Q., Seabra, M.C. (2002). Analysis and Preparation of Stable Complexes between Rab GTPases, Rab Escort Protein, and Rab Geranylgeranyl Transferase. In: Manser, E., Leung, T. (eds) GTPase Protocols. Methods in Molecular Biology™, vol 189. Springer, Totowa, NJ. https://doi.org/10.1385/1-59259-281-3:157
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DOI: https://doi.org/10.1385/1-59259-281-3:157
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