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      Rho GTPases as regulators of morphological neuroplasticity

      research-article
      Author(s): , , *
      Publication date PMC-release:
      Journal: Annals of Anatomy
      Publisher: G. Fischer
      Keywords: C3, Clostridium botulinum ribosyltransferase, cAMP, cyclic adenosine monophosphate, Cdc42, cell division control protein 42 homolog, CRIB, Cdc42/Rac interactive binding, DRG, dorsal root ganglia, ERK, extracellular signal-regulated kinase, FAK, focal adhesion kinase, FGF-2, fibroblast growth factor 2, GAP, GTPase-activating protein, GDI, guanine nucleotide dissociation inhibitor, GEF, guanine nucleotide exchange factor, GSK-3β, glycogen synthase kinase-3β, JNK, Jun N-terminal kinase, LPA, lysophosphatidic acid, m-Dia, formin mammalian diaphanous, MAP, mitogen-activated protein, MLC, myosin light chain, N-WASP, neural Wiskott–Aldrich syndrome protein, NGF, nerve growth factor, NT3, neurotrophin-3, PAK, partitioning defective-6, PAR6, p21-activated kinase, PI3K, phosphatidylinositol-3 kinase, PIP, phosphatidylinositol 4,5-bisphosphate, PIP-5kinase, phosphatidylinositol-4 phosphate-5 kinase, PKN, protein kinase N, Rac, Ras-related C3 botulinum toxin substrate, Ras, Rat sarcoma, Rho, Ras homologous, ROCK, Rho-associated coiled-coil-containing protein kinase, SAPK, stress-activated protein kinase, Smurf, Smad ubiquitination regulatory factor, Rac, Cdc42, GEF, GAP, Axon, Dendrite, Growth cone, Branching, Sprouting, Elongation

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          Summary

          GTPases function as intracellular, bimolecular switches by adopting different conformational states in response to binding GDP or GTP. Their activation is mediated through cell-surface receptors. Rho GTPases act on several downstream effectors involved in cellular morphogenesis, cell polarity, migration and cell division. In neurons, Rho GTPases regulate various features of dendritic and axonal outgrowth during development and regeneration mainly through their effects on the cytoskeleton. This review summarizes the main functions of Rho, Rac and Cdc42 GTPases as key regulators of morphological neuroplasticity under normal and pathological conditions.

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          Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B.

          D. Cross, D Alessi, P. Cohen … (1995)
          Glycogen synthase kinase-3 (GSK3) is implicated in the regulation of several physiological processes, including the control of glycogen and protein synthesis by insulin, modulation of the transcription factors AP-1 and CREB, the specification of cell fate in Drosophila and dorsoventral patterning in Xenopus embryos. GSK3 is inhibited by serine phosphorylation in response to insulin or growth factors and in vitro by either MAP kinase-activated protein (MAPKAP) kinase-1 (also known as p90rsk) or p70 ribosomal S6 kinase (p70S6k). Here we show, however, that agents which prevent the activation of both MAPKAP kinase-1 and p70S6k by insulin in vivo do not block the phosphorylation and inhibition of GSK3. Another insulin-stimulated protein kinase inactivates GSK3 under these conditions, and we demonstrate that it is the product of the proto-oncogene protein kinase B (PKB, also known as Akt/RAC). Like the inhibition of GSK3 (refs 10, 14), the activation of PKB is prevented by inhibitors of phosphatidylinositol (PI) 3-kinase.
          Article 0 comments Cited 1034 times – based on 0 reviews     Review now
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            Phosphorylation and activation of myosin by Rho-associated kinase (Rho-kinase).

            Megumi K. Kimura, K Chihara, Kori Matsuura … (1996)
            The small GTPase Rho is implicated in physiological functions associated with actin-myosin filaments such as cytokinesis, cell motility, and smooth muscle contraction. We have recently identified and molecularly cloned Rho-associated serine/threonine kinase (Rho-kinase), which is activated by GTP Rho (Matsui, T., Amano, M., Yamamoto, T., Chihara, K., Nakafuku, M., Ito, M., Nakano, T., Okawa, K., Iwamatsu, A., and Kaibuchi, K. (1996) EMBO J. 15, 2208-2216). Here we found that Rho-kinase stoichiometrically phosphorylated myosin light chain (MLC). Peptide mapping and phosphoamino acid analyses revealed that the primary phosphorylation site of MLC by Rho-kinase was Ser-19, which is the site phosphorylated by MLC kinase. Rho-kinase phosphorylated recombinant MLC, whereas it failed to phosphorylate recombinant MLC, which contained Ala substituted for both Thr-18 and Ser-19. We also found that the phosphorylation of MLC by Rho-kinase resulted in the facilitation of the actin activation of myosin ATPase. Thus, it is likely that once Rho is activated, then it can interact with Rho-kinase and activate it. The activated Rho-kinase subsequently phosphorylates MLC. This may partly account for the mechanism by which Rho regulates cytokinesis, cell motility, or smooth muscle contraction.
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              Spatiotemporal dynamics of RhoA activity in migrating cells.

              Olivier Pertz, Louis Hodgson, Richard Klemke … (2006)
              Rho family GTPases regulate the actin and adhesion dynamics that control cell migration. Current models postulate that Rac promotes membrane protrusion at the leading edge and that RhoA regulates contractility in the cell body. However, there is evidence that RhoA also regulates membrane protrusion. Here we use a fluorescent biosensor, based on a novel design preserving reversible membrane interactions, to visualize the spatiotemporal dynamics of RhoA activity during cell migration. In randomly migrating cells, RhoA activity is concentrated in a sharp band directly at the edge of protrusions. It is observed sporadically in retracting tails, and is low in the cell body. RhoA activity is also associated with peripheral ruffles and pinocytic vesicles, but not with dorsal ruffles induced by platelet-derived growth factor (PDGF). In contrast to randomly migrating cells, PDGF-induced membrane protrusions have low RhoA activity, potentially because PDGF strongly activates Rac, which has previously been shown to antagonize RhoA activity. Our data therefore show that different extracellular cues induce distinct patterns of RhoA signalling during membrane protrusion.
              Article 0 comments Cited 244 times – based on 0 reviews     Review now
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                Author and article information

                Journal
                Journal ID (nlm-ta): Ann Anat
                Journal ID (iso-abbrev): Ann. Anat
                Title: Annals of Anatomy
                Publisher: G. Fischer
                ISSN (Print): 0940-9602
                ISSN (Electronic): 1618-0402
                Publication date PMC-release: July 2011
                Publication date (Print): July 2011
                Volume: 193
                Issue: 4
                Pages: 259-266
                Affiliations
                Division of Neuroanatomy, Medical University of Innsbruck, Muellerstrasse 59, A-6020 Innsbruck, Austria
                Author notes
                [* ]Corresponding author. Tel.: +43 512 9003 71160. lars.klimaschewski@ 123456i-med.ac.at Lars.Klimaschewski@ 123456uibk.ac.at
                Article
                Publisher ID: AANAT50551
                DOI: 10.1016/j.aanat.2011.02.015
                PMC ID: 3143277
                PubMed ID: 21459565
                SO-VID: 4a998a1a-cc90-45e1-a571-62c6fc8379e8
                Copyright © © 2011 Elsevier GmbH.
                License:

                This document may be redistributed and reused, subject to certain conditions.

                History
                Date received : 19 February 2011
                Date accepted : 28 February 2011
                Categories
                Subject: Article

                ScienceOpen disciplines: Anatomy & Physiology
                Keywords: rho, ras homologous,crib, cdc42/rac interactive binding,gsk-3β, glycogen synthase kinase-3β,dendrite,rock, rho-associated coiled-coil-containing protein kinase,gap, gtpase-activating protein,gef,camp, cyclic adenosine monophosphate,pip-5kinase, phosphatidylinositol-4 phosphate-5 kinase,pak, partitioning defective-6,gap,par6, p21-activated kinase,n-wasp, neural wiskott–aldrich syndrome protein,map, mitogen-activated protein,fak, focal adhesion kinase,m-dia, formin mammalian diaphanous,pkn, protein kinase n,erk, extracellular signal-regulated kinase,ras, rat sarcoma,pip, phosphatidylinositol 4,5-bisphosphate,drg, dorsal root ganglia,sprouting,ngf, nerve growth factor,smurf, smad ubiquitination regulatory factor,rac, ras-related c3 botulinum toxin substrate,axon,growth cone,c3, clostridium botulinum ribosyltransferase,sapk, stress-activated protein kinase,pi3k, phosphatidylinositol-3 kinase,branching,fgf-2, fibroblast growth factor 2,cdc42, cell division control protein 42 homolog,cdc42,mlc, myosin light chain,gdi, guanine nucleotide dissociation inhibitor,jnk, jun n-terminal kinase,elongation,nt3, neurotrophin-3,lpa, lysophosphatidic acid,gef, guanine nucleotide exchange factor,rac
                Data availability:
                ScienceOpen disciplines: Anatomy & Physiology
                Keywords: rho, ras homologous, crib, cdc42/rac interactive binding, gsk-3β, glycogen synthase kinase-3β, dendrite, rock, rho-associated coiled-coil-containing protein kinase, gap, gtpase-activating protein, gef, camp, cyclic adenosine monophosphate, pip-5kinase, phosphatidylinositol-4 phosphate-5 kinase, pak, partitioning defective-6, gap, par6, p21-activated kinase, n-wasp, neural wiskott–aldrich syndrome protein, map, mitogen-activated protein, fak, focal adhesion kinase, m-dia, formin mammalian diaphanous, pkn, protein kinase n, erk, extracellular signal-regulated kinase, ras, rat sarcoma, pip, phosphatidylinositol 4,5-bisphosphate, drg, dorsal root ganglia, sprouting, ngf, nerve growth factor, smurf, smad ubiquitination regulatory factor, rac, ras-related c3 botulinum toxin substrate, axon, growth cone, c3, clostridium botulinum ribosyltransferase, sapk, stress-activated protein kinase, pi3k, phosphatidylinositol-3 kinase, branching, fgf-2, fibroblast growth factor 2, cdc42, cell division control protein 42 homolog, cdc42, mlc, myosin light chain, gdi, guanine nucleotide dissociation inhibitor, jnk, jun n-terminal kinase, elongation, nt3, neurotrophin-3, lpa, lysophosphatidic acid, gef, guanine nucleotide exchange factor, rac

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