title: Concentric zones of active RhoA and Cdc42 around single cell wounds.
abstract: Rho GTPases control many cytoskeleton-dependent processes, but how they regulate spatially distinct features of cytoskeletal function within a single cell is poorly understood. Here, we studied active RhoA and Cdc42 in wounded Xenopus oocytes, which assemble and close a dynamic ring of actin filaments (F-actin) and myosin-2 around wound sites. RhoA and Cdc42 are rapidly activated around wound sites in a calcium-dependent manner and segregate into distinct, concentric zones around the wound, with active Cdc42 in the approximate middle of the F-actin array and active RhoA on the interior of the array. These zones form before F-actin accumulation, and then move in concert with the closing array. Microtubules and F-actin are required for normal zone organization and dynamics, as is crosstalk between RhoA and Cdc42. Each of the zones makes distinct contributions to the organization and function of the actomyosin wound array. We propose that similar rho activity zones control related processes such as cytokinesis.
authors.affiliation: Department of Zoology, University of Wisconsin-Madison, Madison, WI 53706, USA.
authors.forename: Hélène A
authors.initials: HA
authors.lastname: Benink
authors.forename: William M
authors.initials: WM
authors.lastname: Bement
mesh_terms: D000199:Actins / Q000187:drug effects / Q000378:metabolism; D000818:Animals; D019086:Bridged Bicyclo Compounds, Heterocyclic / Q000494:pharmacology; D002118:Calcium / Q000172:deficiency / Q000502:physiology; D024722:Cardiac Myosins / Q000378:metabolism; D015638:Cytochalasin D / Q000494:pharmacology; D003599:Cytoskeleton / Q000187:drug effects / Q000378:metabolism; D005260:Female; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry / Q000378:metabolism; D007700:Kinetics; D007834:Lasers; D008164:Luminescent Proteins / Q000737:chemistry; D008845:Microinjections; D008856:Microscopy, Fluorescence; D008870:Microtubules / Q000187:drug effects / Q000378:metabolism; D008954:Models, Biological; D018994:Myosin Light Chains / Q000378:metabolism; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000378:metabolism; D015739:Nocodazole / Q000494:pharmacology; D009865:Oocytes / Q000166:cytology / Q000378:metabolism*; D017239:Paclitaxel / Q000494:pharmacology; D010766:Phosphorylation; D012333:RNA, Messenger / Q000008:administration & dosage / Q000235:genetics; D013844:Thiazoles / Q000494:pharmacology; D053778:Thiazolidines; D014118:Toxins, Biological / Q000494:pharmacology; D051317:Wiskott-Aldrich Syndrome Protein, Neuronal; D014981:Xenopus; D020764:cdc42 GTP-Binding Protein / Q000235:genetics / Q000378:metabolism*; D020742:rhoA GTP-Binding Protein / Q000235:genetics / Q000378:metabolism*
chemical_list: D000199:Actins; D019086:Bridged Bicyclo Compounds, Heterocyclic; D047908:Intracellular Signaling Peptides and Proteins; D008164:Luminescent Proteins; D018994:Myosin Light Chains; D009419:Nerve Tissue Proteins; D012333:RNA, Messenger; D013844:Thiazoles; D053778:Thiazolidines; D014118:Toxins, Biological; D051317:Wiskott-Aldrich Syndrome Protein, Neuronal; C107184:myosin light chain 2; D015638:Cytochalasin D; D024722:Cardiac Myosins; D020764:cdc42 GTP-Binding Protein; D020742:rhoA GTP-Binding Protein; C037068:latrunculin B; D017239:Paclitaxel; D015739:Nocodazole; D002118:Calcium