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Titlebook: Cytoskeleton and Small G Proteins; Philippe Jeanteur Book 1999 Springer-Verlag Berlin Heidelberg 1999 Cytoskeleton.Cytoskelett.GTPases.GTP

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The DH Protein Family, Exchange Factors for Rho-Like GTPases,ious forms of vesicle transport, nuclear transport and actin cytoskeleton regulation (Bourne et al. 1990). These small GTPases (about 21 kDa) act as molecular switches that are active when they are GTP-bound, and inactive when GTP is converted to GDP, due to their intrinsic GTPase activity (Boguski
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Rac and Cdc42 Effectors,state. Until recently, members of the Rho-subfamily were believed to be primarily involved in the regulation of cytoskeletal organization in response to extracellular growth factors. However, studies from numerous groups over the past few years have revealed that the Rho-GTPases play crucial roles i
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Georg Petroianu,Peter Michael Osswaldly, intrinsic signals during the cell cycle lead to reorganization of actin filaments during mitosis followed by formation and contraction of the actin-based contractile ring at cytokinesis (Ridley 1995).
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Georg Petroianu,Peter Michael Osswalde GTP/ GDP in vivo. GEFs, which are also termed guanine nucleotide dissociation stimulators (GDSs) or guanine nucleotide release factors (GRFs), induce the active conformation. Guanine nucleotide dissociation inhibitors (GDIs) bind GTPases and stabilize their conformation, either in the GDP-bound-or
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Georg Petroianu,Peter Michael Osswaldc Ras proteins (e.g. G12V or Q61L) leads to constitutively active Rho proteins, due to a reduced GTP hydrolysis. Once loaded with GTP, the GTPase gains the ability to bind cognate effector downstream targets, which converts the input signal into a specific set of activations.
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