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Microbiology (Reading). 2017 Aug;163(8):1156-1166. doi: 10.1099/mic.0.000503.

Cdc42 activation state affects its localization and protein levels in fission yeast.

Microbiology (Reading, England)

Miguel Estravís, Sergio Antonio Rincón, Elvira Portales, Pilar Pérez, Beatriz Santos

Affiliations

  1. Instituto de Biología Funcional y Genómica (IBFG), Consejo Superior de Investigaciones Científicas, University of Salamanca, 37007 Salamanca, Spain.
  2. Present address: Institut Curie, Centre de Recherche, PSL Research University, CNRS UMR144, F-75248 Paris, France.
  3. Departamento de Microbiología y Genética, University of Salamanca, 37007 Salamanca, Spain.

PMID: 28742002 DOI: 10.1099/mic.0.000503

Abstract

Rho GTPases control polarized cell growth and are well-known regulators of exocytic and endocytic processes. Cdc42 is an essential GTPase, conserved from yeast to humans, that is critical for cell polarization. Cdc42 is negatively regulated by the GTPase-activating proteins (GAPs) and the GDP dissociation inhibitors (GDIs), and positively regulated by guanine nucleotide exchange factors (GEFs). Cdc42 GTPase can be found in a GTP- or GDP-bound state, which determines the ability to bind downstream effector proteins and activate signalling pathways. Only GTP-bound Cdc42 is active. In this study we have analysed the localization of the different nucleotide-bound states of Cdc42 in

Keywords: Cdc42; GTPase; fission yeast; polarity

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