Atlas préhistorique de la Tunisie. 11. Kairouan

Zoughlami Jamel, Chenorkian Robert, Harbi-Riahi Mounira. Atlas préhistorique de la Tunisie. 11. Kairouan. Rome : École Française de Rome, 1998. 166 p. (Publications de l'École française de Rome, 81-11

Atlas préhistorique de la Tunisie. 1. Tabarka

Camps Gabriel, Gragueb Abderrazak, Harbi-Riahi Mounira et al. Atlas préhistorique de la Tunisie. 1. Tabarka. Rome : École Française de Rome, 1985. 34 p. (Publications de l'École française de Rome, 81-1

Atlas préhistorique de la Tunisie. 2. Bizerte

Gragueb Abderrazak, Camps Gabriel, Harbi-Riahi Mounira et al. Atlas préhistorique de la Tunisie. 2. Bizerte. Rome : École Française de Rome, 1985. 46 p. (Publications de l'École française de Rome, 81-2

Atlas préhistorique de la Tunisie. 1. Tabarka

Camps Gabriel, Gragueb Abderrazak, Harbi-Riahi Mounira et al. Atlas préhistorique de la Tunisie. 1. Tabarka. Rome : École Française de Rome, 1985. 34 p. (Publications de l'École française de Rome, 81-1

Atlas préhistorique de la Tunisie. 12. El Djem

Camps Gabriel, Gragueb Abderrazak, Harbi-Riahi Mounira et al. Atlas préhistorique de la Tunisie. 12. El Djem. Rome : École Française de Rome, 1995. 34 p. (Publications de l'École française de Rome, 81-12

Atlas préhistorique de la Tunisie. 2. Bizerte

Gragueb Abderrazak, Camps Gabriel, Harbi-Riahi Mounira et al. Atlas préhistorique de la Tunisie. 2. Bizerte. Rome : École Française de Rome, 1985. 46 p. (Publications de l'École française de Rome, 81-2

The emergence of domestication in eastern Maghreb: a new model for Tunisia

International audienc

Rac1 interacts through its C-terminus with NPM1.

<p>(A) Schematic representation of the Rho-like GTPase C-terminal peptides fused to a protein transduction domain as used in this study. (B) Pull-down (PD) experiments were performed using lysates from HeLa cells (upper panel) or Jurkat T-cells (lower panel) with a control peptide, wild-type and mutant Rac1 C-terminal peptides, Rac2, RhoA and RhoG C-terminal peptides. Association of endogenous NPM1 was detected by immunoblotting (IB) with an NPM1 specific monoclonal antibody (representative example out of three independent experiments is shown). (C) Pull-down (PD) experiment was performed using lysates from HeLa cells with a control peptide, wild-type and mutant Rac1 C-terminal peptides. Association of phosphorylated NPM1 (pNPM1) was detected by immunoblotting (IB) with a phospho-specific NPM1 antibody. (representative example out of two independent experiments is shown). (D) Pull-down (PD) experiment using full-length Rac1 and Rac1 lacking the C-terminus (ΔC) both fused to GST or GST alone was performed with lysates from HeLa cells exogenously expressing GFP-NPM1. Association of NPM1 was detected by immunoblotting (IB) with a GFP specific monoclonal antibody. The ponceau staining shows the presence of the different GST constructs. ED: effector domain of Rac1, HV: hypervariable domain of Rac1, PTD: protein transduction domain, Rac1 PPP→AAA, Rac1 RKR→AAA: Rac1 C-terminal peptide mutants where the three prolines, or RKR sequence were replaced by alanine residues, respectively, TCL: total cell lysates, PD: pull-down, IB: immunoblotting.</p

NPM1 is a negative regulator of Rac1.

<p>(A) Rac1 GTP loading was measured by biotinylated Pak-CRIB peptide-based pull-down (PD) with lysates of GFP control-transfected HeLa cells or HeLa cells transfected with GFP-NPM1. Rac1, Rac1 GTP and GFP-NPM1 were detected by immunoblotting with Rac1 and GFP specific monoclonal antibodies respectively. The bar graph shows the relative levels of Rac1 GTP levels compared to that in control as determined by quantification of Western blots (representative example out of three independent experiments is shown). TCL: total cell lysates, PD: pull-down. (B) Cell spreading on fibronectin coated ECIS-electrodes was determined for mock-transfected HeLa cells or HeLa cells expressing GFP-tagged NPM1. The results are depicted as normalized mean resistance of three independent experiments. (n = 3) *p<0.05, **p<0.01. (C) Rac1 GTP loading was measured by biotinylated Pak-CRIB peptide-based pull-down (PD) with lysates of GFP control-transfected HeLa cells or HeLa cells transfected with GFP-NPM1 in the absence or presence of the GEF protein Tiam-C-1199 tagged with HA. Rac1 and Rac1 GTP were detected by immunoblotting with Rac1 specific monoclonal antibody. GFP-NPM1 and Tiam-C-1199-HA were detected by immunoblotting with GFP and HA specific monoclonal antibodies, respectively.</p