Notch receptor proteins

Nonsteroidal antiinflammatory drugs, interaction with lithium, 36 66 No-phonon transition, 35 324 Norbomadiene complexes with cobalt, 12 286 with copper, 12 328, 330, 331 with gold, 12 348, 349 with group VIB metals, 12 231 with group VnB metals, 12 241 with iron, 12 265 with palladium, 12 314 with platinum, 12 319 with rhodium, 12 300-302 with ruthenium, 12 278, 279 with silver, 12 340-342, 344, 346 Norbomylsiloxane, 42 226, 228 Notch receptor proteins, 46 473, 475 h (N)" oxime complexes, osmium, 37 260 h (N,0) oxime complexes, osmium, 37 260 (NPr ljiFeCfrdto),], magnetization versus temperature, 43 230... 

Transmembrane Signaling. Figure 2 Membrane topology of receptors that are associated with effector proteins. Upon binding to their cognate ligands (cyan), receptor proteins without intramolecularly linked effector domain couple via transducer proteins (yellow) to or directly recruit and activate effector proteins (red). Notch receptors release their transducer domains upon proteolytic cleavage, a, p and y stand for G-protein a-, p- and y-subunits, respectively. 

Figure 5 Proteolytic processing and signaling of the Notch receptor. In the ER, Notch is cleaved at SI by a furin-like protease to produce a stable heterodimeric receptor that is trafficked to the cell surface. Interaction with ligands such as the proteins Delta and Jagged triggers a shedding of the ectodomain by membrane-tethered metalloprotease-mediated cleavage at S2. The remnant then is cleaved at least twice, at the S3 and S4 sites, to release the Notch counterpart of Ap (Np) and the intracellular domain (NICD). The latter translocates to the nucleus where it interacts with transcription factors to influence gene expression relevant to cell differentiation.

Okajima T, Xu A, Lei L, Irvine KD. Chaperone activity of protein O-fucosyltransferase 1 promotes notch receptor folding. Science 2005 307 1599-1603. 

NOTCH proteins participate in conserved pathways that regulate cellular differentiation, proliferation, and cell death. Mammalian NOTCH receptors are single-pass transmembrane proteins that transmit juxtacrine signals initiated by ligands of the Delta, Serrate, or Lag-2 family [122, 123], When ligands bind to the extracellular domain of NOTCH1, sequential proteolytic processing events lead to the... 

Neu protein, which takes part in embryonic differentiation and Notch protein, a receptor protein in the plasma membrane that functions in developmentally important signaling (Chapter 14). Besides the EGF domain, these proteins contain domains found in other proteins. For example, TPA possesses a trypsin domain, a common feature in enzymes that degrade proteins. 

Fig. 12.2. Model of Notch signalling. The Notch protein is a ligand activated transmembrane receptor which is subject to proteolysis of the intracellular domain upon ligand binding. The nature of the protease involved is still a matter of debate. The proteolytically released intranceUu-lar domain of Notch (NICD) translocates into the nucleus where it interacts with a family of transcription factors, the CSL proteins, resulting in a change in transcription of target genes.

---