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Example sentences for: gtpases
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In all of the known Ras-related GTPases the guanine nucleotide binding site is surrounded by a set of highly conserved sequence elements [ 33 34 ] . One of these elements, termed the G2 motif, consists of NKxD (with the asparagine located at position 116 in H-Ras).
ADP-ribosylation of Rho proteins by C3 exoenzyme prevents neurite retraction in the specialized growth cone of developing neurons, and in fact promotes neurite outgrowth in the same fashion as microinjection of purified dominant negative RhoA T19N [ 39 ] . In these instances, neuronal N1E-115 cell outgrowth induced by inactivation of RhoA was mimicked by microinjection of Rac1- or Cdc42-GST fusion proteins, and could be abolished by coinjection of dominant negative Cdc42 T17Nor Rac1 T17N [ 39 ] . From these results, the authors concluded that inactivation of RhoA by C3 exoenzyme treatment resulted in the activation of Rac1 and Cdc42 GTPases, suggesting the mutually exclusive function of RhoA and Rac1/Cdc42.
PLD1 is an extracellular signal-activated phospholipase; its activity rises when receptors for certain hormones, growth factors, neurotransmitters, cytokines, and other mediators are activated, and upon treatment of cells with phorbol esters (reviewed in [ 7 8 ] ). Studies using recombinant PLD1 tagged with green fluorescent protein or Flu-epitopes indicate that it is localized in the endoplasmic reticulum, Golgi apparatus, late endosomes, and plasma membrane ( [ 6 ] , reviewed in [ 7 ] ). In vitro, basal PLD1 activity is usually low and can be stimulated by a variety of factors, including phosphatidylinositol 4, 5-bisphosphate (PIP 2 ), protein kinase C (PKC), and several small GTPases, e.g.
Hence, considerable diversity of protein domains appears to have emerged prior to the "crystallization" [ 95 ] of a transcription machinery similar to the one that operates in modern cells and probably had been already in place in LUCA [ 96 ] . Similar conclusions regarding the early stages of protein domain evolution have been reached previously as a result of evolutionary analysis of proteins involved in translation, such as aminoacyl-tRNA synthetases and GTPases: substantial diversification of protein domains had occurred prior to the "crystallization" of elaborate, modern-type translation machinery [ 66 97 ] .
Interestingly, inhibition of Rho-p160ROCK has recently been shown to give similar lymphocyte morphology as inhibition of Rho with C3 [ 50 ] . Another interesting candidate may be p120 PKN, as recent studies have established that PKN phosphorylates cytoskeletal intermediate filaments [ 47 ] and is directly linked to the cytoskeletal network through associations with α-actinin [ 48 ] . Also, PKN may be involved in relating cytoplasmic signals to the nucleus, for in response to stress, nuclear translocation of PKN occurs [ 49 ] . This is particularly important in light of previous work demonstrating that inactivation of Rho in peripheral blood T lymphocytes inhibits costimulatory signals up-regulating IL-2 production [ 25 ] . Future experiments will focus on determining the relationship of Rho GTPases and the regulation of T cell morphology [ 25 51 52 ] .
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