title: Actin, RhoA, and Rab11 participation during encystment in Entamoeba invadens.
abstract: In the genus Entamoeba, actin reorganization is necessary for cyst differentiation; however, its role is still unknown. The aim of this work was to investigate the role of actin and encystation-related proteins during Entamoeba invadens encystation. Studied proteins were actin, RhoA, a small GTPase involved through its effectors in the rearrangement of the actin cytoskeleton; Rab11, a protein involved in the transport of encystation vesicles; and enolase, as an encystment vesicles marker. Results showed a high level of polymerized actin accompanied by increased levels of RhoA-GTP during cell rounding and loss of vacuoles. Cytochalasin D, an actin polymerization inhibitor, and Y27632, an inhibitor of RhoA activity, reduced encystment in 80%. These inhibitors also blocked cell rounding, disposal of vacuoles, and the proper formation of the cysts wall. At later times, F-actin and Rab11 colocalized with enolase, suggesting that Rab11 could participate in the transport of the cyst wall components through the F-actin cytoskeleton. These results suggest that actin cytoskeleton rearrangement is playing a decisive role in determining cell morphology changes and helping with the transport of cell wall components to the cell surface during encystment of E. invadens.
authors.affiliation: Departamento de Infectómica y Patogénesis Molecular, Centro de Investigación y de Estudios Avanzados del I.P.N., Avenida Instituto Politécnico Nacional No. 2508, Colonia San Pedro Zacatenco, Delegación Gustavo A. Madero, 07360 México City, DF, Mexico.
authors.forename: M
authors.initials: M
authors.lastname: Herrera-Martínez
authors.forename: V I
authors.initials: VI
authors.lastname: Hernández-Ramírez
authors.forename: A E
authors.initials: AE
authors.lastname: Lagunes-Guillén
authors.forename: B
authors.initials: B
authors.lastname: Chávez-Munguía
authors.forename: P
authors.initials: P
authors.lastname: Talamás-Rohana
mesh_terms: D000199:Actins / Q000235:genetics / Q000378:metabolism*; D000595:Amino Acid Sequence; D000818:Animals; D003599:Cytoskeleton / Q000378:metabolism / Q000648:ultrastructure; D004747:Entamoeba / Q000235:genetics / Q000254:growth & development* / Q000378:metabolism*; D006801:Humans; D008969:Molecular Sequence Data; D015800:Protozoan Proteins / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D014617:Vacuoles / Q000378:metabolism / Q000648:ultrastructure; D020691:rab GTP-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D020742:rhoA GTP-Binding Protein / Q000235:genetics / Q000378:metabolism*; D000099193:rab11 GTP-Binding Proteins
chemical_list: D000199:Actins; D015800:Protozoan Proteins; D020691:rab GTP-Binding Proteins; D020742:rhoA GTP-Binding Protein; D000099193:rab11 GTP-Binding Proteins