Intracellular domain

Domain (or cytoplasm) cells of the receptor interacts with the interior of the laying organelle or cell, of the signal. There are two fundamentally different for this interaction.
Then sends a signal to the signal circuit to the destination, specific proteins and effector proteins – I intracellular domain communication through protein interactions.
The enzyme-linked receptors having an enzymatic activity in the intracellular domain. In many cases, is a tyrosine kinase. Enzyme activity, may be present in an enzyme associated with the intracellular domain.

Intracellulardomain1

 

Notch signaling pathway is important in cell differentiation. Current Opinion is that it is cleaved within the cell ligand activation Notch receptor. Then, Notch intracellular domain to translocate to the nucleus, bind to (the RBP-Jk in mammals) suppressor of hair, it functions as (HES mammals) gene expression of trans enhancer of split. In this report, three Notch intracellular domain (IC), an activator weak contrast to the IP level analysis all other, as a repressor by blocking the ability of 1 IC notch physical act of -5 promoter to activate expression of HES and HES-1 has been shown. We, Notch 3 IC presents a model of preventing notch 1 IC-mediated activation of two levels. First, Notch 3 IC activates transcription when it is located near the promoter and competes with RBP the Notch 1 IC access Jk. Second, in order to limit the amount, Notch 3 IC is likely to compete with 1 IC notch for coactivator of this common. In conclusion, this is the first example of a notch circuit that acts as a repressor in the enhancer of split / HES regulations, Notch receptor of the mammalian indicates that it was a variety of functions in the course of evolution.

NAChR subunits each have adopted a composite membrane topology, including the (M1-M4) large extracellular N-terminal agonist binding domain four α-helical transmembrane domain. In previous studies, it is the interaction with intracellular proteins; shows (between the M4 and M3) intracellular domain of the large amount that the nAChR is important for (Jeanclos et al, 2001, 2003 Maimone and Huebsch.) are. Receptor targeting (Williams et al, 1998) and ion channel characteristics (.; Hales et al, 2006; Kelly et al, 2003 .. Gee et al, 2007). The purpose of this study is to do a detailed comparison of the intracellular domain of the nAChR of different subunits. This, and (from α7 subunit of nAChR) extracellular domain of a common transmembrane domain – accomplished by establishing a series of chimeric subunits and a cytoplasmic domain lines nAChR (5 from HT3A subunits) are different are.

It does not have a significant effect on the level of the subunit common proteins were detected in cells transfected M3-M4 intracellular loop domain in the form of nAChR, and the assembly level of the intracellular receptor and cell surface I have a major impact. Comparison of functional properties reveals a significant effect of the intracellular domain of the receptor desensitization and two-stroke single-channel conductance. Further, as a result of nAChR polarization line, testing was performed using a polarized epithelial cells showed that it is possible to influence the non-polarization distribution targeting or receptor.

NAChR subunits each have adopted a composite membrane topology, including the (M1-M4) large extracellular N-terminal agonist binding domain four α-helical transmembrane domain. In previous studies, (between the M4 and M3) intracellular domain of the large number that has been shown, it is important for interaction targeting receptors and intracellular proteins, and ion channel properties nAChR some. The purpose of this study is to do a detailed comparison of the intracellular domain of the nAChR of different subunits. This, and (from α7 subunit of nAChR) extracellular domain of a common transmembrane domain – accomplished by establishing a series of chimeric subunits and a cytoplasmic domain lines nAChR (5 from HT3A subunits) are different are.

Construction of chimeras (α7V201-5HT3A), and related chimeras (Cooper, Miller, 1997), such as including an intracellular domain and 5-HT3A transmembrane subunit and mouse extracellular domain nAChRα7 subunit of the rat has been described previously Here, 5 HT3A intracellular domain cycle will be replaced by equivalent area α7 subunit (such as Gee, 2007) to the described in (α74TM-5HT3A). Was introduced in (BstZ17I is in NotI) Unique restriction sites, M3-M4 cell large-scale use (Stratagene, Amsterdam, Netherlands) quick-change site-directed mutagenesis system N-and C-termini is for I’ll make α74TM-5HT3A was both ends of the line in the domain α74TM-5HT3A the (the I / Bst). In α74TM-5HT3A the original structure, the α7 sequence (the first is a QDLQRP / MPKWTR,. Introduce NotI site corresponding to Met 327 in α7 sequence in rats, the first of α7 amino acid sequence of the M3 end of the M3-M4 loop I met Ray in α74TM-5HT3A which changes the amino acid sequence.

Inactivating mutation KISS-1 receptor (KISS1R) has been described as a rare cause of transmission solitary hypogonadotropic hypogonadism as a recessive trait recently. Several mutations have been described, the structure of KISS1R – it is still being fully understand the function relationship. In this case, proline three in the intracellular domain – it has benefited from the opening of the new mutation KISS1R to characterize the structure and function of unusual motif protein consisting arginine (PRR) repeat – arginine. One iteration of the frame within the heterozygous insertion PRR PRR triple leading to the synthesis of the receptor PRR repeat four times that found in the case of each of (PRR-KISS1R),. Without having to change the whole expression, functional analysis of PRR-KISS1R, shows a decrease in the maximum response of kisspeptin stimulation associated with low expression of cell surface. PRR-KISS1R exert a dominant negative effect of synthesis of wild-type (WT)-KISS1R. Instead This effect is due to the nature of the inserted residues to the difference in length between the intracellular domain of WT-KISS1R and PRR-KISS1R. The poly-proline type II helix, molecular dynamics analysis showed PRR limited arginine-rich region that this additional. Overall, in this study, it indicates that there is a possibility that be included in the heterojunction KISS1R cause hypogonadotropic hypogonadism in a dominant negative effect on the WT receptor. Proline – Add PRR repeat of the motif rich in arginine, you can not change the three-dimensional structure of the intracellular domain of dramatic KISS1R, react with the partner protein probably.