von Dr. Diana Sandulache
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| [1.] Dsa/Fragment 034 00 - Diskussion Zuletzt bearbeitet: 2016-08-18 20:44:23 WiseWoman | Debonneville et al 2001, Dsa, Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop |
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| Untersuchte Arbeit: Seite: 34, Zeilen: figure |
Quelle: Debonneville et al 2001 Seite(n): 7053, Zeilen: figure |
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Figure nr. 7 - Schematic view of Nedd4-2 and Sgk1. (A) Scheme of Xenopus Nedd4-2 with the consensus phosphorylation sites and Xenopus Sgk1 with the indication of the catalytic domain, the catalytically essential Lys130 and the PY motif. (B) Conserved consensus phosphorylation sites in mouse, human and Xenopus Nedd4-2. |
Fig. 1. Schematic view of Nedd4-2 and Sgk1. (A) Scheme of Xenopus Nedd4-2 with the consensus phosphorylation sites and Xenopus Sgk1 with the indication of the catalytic domain, the catalytically essential Lys130 and the PY motif. (B) Conserved consensus phosphorylation sites in mouse, human and Xenopus Nedd4-2. |
The source is mentioned on the previous page, but without indication that the figure is taken from it. |
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| [2.] Dsa/Fragment 034 01 - Diskussion Zuletzt bearbeitet: 2016-08-04 22:00:34 WiseWoman | Boini 2006, Dsa, Fragment, Gesichtet, KomplettPlagiat, SMWFragment, Schutzlevel sysop |
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| Untersuchte Arbeit: Seite: 34, Zeilen: 1-20 |
Quelle: Boini 2006 Seite(n): 16, Zeilen: 1ff |
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| This inhibitory effect of SGK1 on Nedd4-2 likely involves 14-3-3 proteins as phosphorylation of Ser444 in Nedd4-2 creates a possible binding site for such proteins, an inherited form of salt-sensitive hypertension are caused by mutations in the genes encoding β- and γ -ENaC (Hansson JH. et al., (1995) Proc Natl Acad Sci USA; Shimkets RA. et al., (1994) Cell). These mutations invariably cause either the deletion or the mutation of the PY-motifs on these subunits. When such Liddle channels are expressed in heterologous systems, increases in both the density at the cell surface and the open probability of ENaC are observed (Firsov et al., (1996) Proc Natl Acad Sci USA; Snyder PM. et al., (1994) Cell; Schild et al., (1995) Proc Natl Acad Sci USA; Schild et al., (1996) EMBO J). Loffing and his coworkers, has demonstrated that these PY-motifs are the binding sites for ubiquitin-protein ligases of the Nedd4/Nedd4-like family (Kamynina E. et al., (2001) EMBO J) and particularly of Nedd4-2 (Kamynina E. et al., (2001) EMBO J; Snyder PM. et al., (2004) J Biol Chem).
It is thought that Nedd4-2 binds via its WW domains with the PY-motifs of ENaC and ubiquitylates ENaC on its own α and γ subunits, consequently leading to the internalization and degradation of ENaC in the endosomal/lysosomal system (Snyder PM. et al., (2004) J Biol Chem). In Liddle’s syndrome, this mechanism is impaired owing to the inactivation of a PY-motif, causing the accumulation of ENaC at the plasma membrane (Kamynina E. and Staub O., (2002) Am J Physiol Renal Physiol). The activity of ENaC and the Na+, K+-ATPase is tightly regulated by aldosterone and by SGK1 (Vallon V. et al., (2005) Am J Physiol Regul Integr Comp Physiol; Bhargava A. et al., (2004) Trends Endocrinol Metab). |
[...], an inherited form of salt-sensitive hypertension are caused by mutations in the genes encoding β- and γ -ENaC (Hansson et al., 1995; Shimkets et al., 1994). These mutations invariably cause either the deletion or the mutation of the PY-motifs on these subunits. When such Liddle channels are expressed in heterologous systems, increases in both the density at the cell surface and the open probability of ENaC are observed (Firsov et al., 1996; Snyder et al., 1995; Schild et al., 1995; Schild et al., 1996). Loffing and his coworkers, has demonstrated that these PY-motifs are the binding sites for ubiquitin-protein ligases of the Nedd4/Nedd4-like family (Kamynina et al., 2001; Kamynina et al., 2001a ) and particularly of Nedd4-2 (Kamynina et al., 2001; Kamynina et al., 2001a; Snyder et al., 2004). It is thought that Nedd4-2 binds via its WW domains with the PY-motifs of ENaC and ubiquitylates ENaC on its α and γ subunits, consequently leading to the internalization and degradation of ENaC in the endosomal/lysosomal system (Snyder et al., 2004). In Liddle’s syndrome, this mechanism is impaired owing to the inactivation of a PY-motif, causing the accumulation of ENaC at the plasma membrane (Kamynina and Staub 2002). The activity of ENaC and the Na+, K+-ATPase is tightly regulated by aldosterone and by SGK1 (Kellenberger and Schild 2002; Vallon et al., 2005; Bhargava et al., 2004). [...] This inhibitory effect of SGK1 on Nedd4-2 likely involves 14-3-3 proteins as phosphorylation of Ser444 in Nedd4-2 creates a possible binding site for such proteins |
The source is not given. Note that the first sentence makes little sense, as it is a combination of two unrelated half-sentences of the source. Apparently the last line of the source on page 16 has not been continued with the first line on page 17, but with the first line on page 16 again, leading to this result. Also, the source writes Ser444, Dsa writes Ser444 constistently. |
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