Signaling Through G Protein-Coupled Receptors

Iismaa, Tiina P.; Biden, Trevor J.; Shine, John

doi:10.1007/978-3-662-21930-0_2

Cited by 14 publications

(17 citation statements)

References 188 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The similarity between the B. microplus receptor and the lymnokinin receptor is greater than that found among the subtypes of the mammalian NPY receptor, Y1, Y2 and Y4, which are activated by the same ligand (Larhammar, 1996). Thus, the ligand for the B. microplus receptor is most likely closely related to lymnokinin, PSFHSWS-NH 2 , because GPCRs which interact with closely related ligands have the greatest sequence homology and structural conservation (Iismaa et al , 1995;Cox et al , 1997). However, leucokinins have not been identified in the Acari, but they have been isolated from insects (Nässel, 1996) and the pond snail (Cox et al , 1997).…”

Section: Discussionmentioning

confidence: 92%

“…There is also a third glycosylation site, Asp 204, in the predicted second extracellular loop. Two cysteine residues in the intracellular C terminus (Cys 348, Cys 350) represent likely sites for palmitoylation (Iismaa et al , 1995).…”

Section: Resultsmentioning

confidence: 99%

“…Multiple glycosylation sites are found in the N termini of several neuropeptide receptors (Li et al, 1992;Monnier et al, 1992;Watson & Arkinstall, 1994;Cox et al, 1997;Tensen et al, 1998a,b). Two cysteines, Cys 348 and Cys 350 in the C-terminal region of the B. microplus receptor are potential sites for palmitoylation, which may be important for receptor function (Watson & Arkinstall, 1994;Iismaa et al, 1995). Receptor binding sites for peptides and protein agonists of GPCRs include the N terminus and extracellular loops (Gether & Kobilka, 1998).…”

Section: Discussionmentioning

confidence: 99%

See 2 more Smart Citations

Cloning and transcriptional expression of a leucokinin‐like peptide receptor from the Southern cattle tick, Boophilus microplus (Acari: Ixodidae)

Holmes

Chen

et al. 2000

Insect Molecular Biology

View full text Add to dashboard Cite

Leucokinins are invertebrate neuropeptides that exhibit myotropic and diuretic activity. Only one leucokinin-like peptide receptor is known, the lymnokinin receptor from the mollusc Lymnaea stagnalis. A cDNA encoding a leucokinin-like peptide receptor was cloned from the Southern cattle tick, Boophilus microplus, a pest of cattle world-wide. This is the first neuropeptide receptor known from the Acari and the second known in the subfamily of leucokinin-like peptide G-protein-coupled receptors. The deduced amino acid sequence exhibits 40% identity to the lymnokinin receptor. The receptor transcript is present in all tick life stages as determined by semiquantitative reverse transcription polymerase chain reaction. We also propose that the sequence AAF50775.1 from the Drosophila melanogaster genome (CG10626) encodes the first identified insect leucokinin receptor.

show abstract

Section: Discussionmentioning

confidence: 92%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

See 1 more Smart Citation

Cloning and transcriptional expression of a leucokinin‐like peptide receptor from the Southern cattle tick, Boophilus microplus (Acari: Ixodidae)

Holmes

Chen

et al. 2000

Insect Molecular Biology

View full text Add to dashboard Cite

show abstract

“…Generally, the signal transduction mechanism of GPCRs involves ligandinduced changes that affect the conformation of the intracellular surface of the receptors and hence promote the coupling to G proteins (2)(3)(4)(5)(6). In the case of the secretin/VIP receptor subfamily, this stimulation process activates adenylate cyclase and eventually leads to the elevation of intracellular cAMP (7)(8)(9)(10)(11). Besides cAMP, other intracellular second messengers, such as Ca 2ϩ and inositol phosphates have also been reported (12)(13)(14).…”

mentioning

confidence: 98%

Functional Segregation of the Highly Conserved Basic Motifs within the Third Endoloop of the Human Secretin Receptor

2001

View full text Add to dashboard Cite

In this study, a mutagenesis-based strategy was employed to assess the roles of two highly conserved motifs (KLR and RLAR) within the third endoloop of the human secretin receptor. Block deletion of KLRT and mutation of Lys323 (K 323 I) significantly reduced cAMP accumulation, and these mutations did not affect ligand interaction and receptor number expressed on the cell surface. Thus, the KLRT region at the N terminus of the third endoloop, particularly Lys323, is important for G protein coupling. For the RLAR motif, receptors with substitutions at positions 339 and 342 from Arg to Ala (R 339, 342 A), Glu (R 339, 342 E), or Ile (R 339, 342 I) as well as block deletion of the RLAR motif were all found to be defective in both secretin-binding and cAMP production. Interestingly, a single mutation at the corresponding positions of Arg339 or Arg342 responded as the wild-type human secretin receptor in all functional assays, indicating that the presence of one Arg at either position within the RLAR motif is sufficient for a normal receptor function. Immunofluorescent staining of these mutant receptors showed that these Arg residues are responsible for surface presentation and/or receptor stability. (Endocrinology 142: 3926 -3934, 2001)T HE SECRETIN RECEPTOR has a high affinity for secretin and a relatively low affinity for VIP (1) and belongs to the class II G protein-coupled receptor (GPCR) subfamily. This secretin/VIP receptor subfamily also includes receptors for glucagon, glucagon-like peptide-1 (GLP-1), gastric inhibitory peptide, PTH, pituitary adenylate cyclase activating polypeptide, and GHRH. Generally, the signal transduction mechanism of GPCRs involves ligandinduced changes that affect the conformation of the intracellular surface of the receptors and hence promote the coupling to G proteins (2-6). In the case of the secretin/VIP receptor subfamily, this stimulation process activates adenylate cyclase and eventually leads to the elevation of intracellular cAMP (7-11). Besides cAMP, other intracellular second messengers, such as Ca 2ϩ and inositol phosphates have also been reported (12)(13)(14).Like other GPCRs, the secretin receptor displays a common structural profile in which seven transmembrane domains are linked by alternative exo-and endoloops. Within the same class, there are many conserved amino acid residues, including six well-conserved cysteine residues in the N-terminal extracellular domain and multiple consensus N-glycosylation sites. Nevertheless, these receptors share only 25-50% of amino acid identity among themselves. When compared with other classes of receptors, such as the rhodopsin/␤-adrenergic receptor family, the secretin receptor family is distinct with respect to the primary sequence. Even with this minimal level of sequence homology, comparisons of receptor properties within the family can provide insight into the importance of specific structural domains or motifs. For example, the diversity of the N termini of these receptors in amino acid composition suggests that the N-terminal ...

show abstract

“…Fos/jun interactions are regulated by activation of PKC, CaMK-II, or CaMK-IV. tional activators, and transcriptional regulators [94]. It is important to note that increased cAMP signaling from activated glial cells can inhibit toxic activities [95].…”

Section: Mp Mediators and Signal Transductionmentioning

confidence: 99%

Insights into the neurodegenerative process of Alzheimer's disease: a role for mononuclear phagocyte-associated inflammation and neurotoxicity

Cotter

Burke

Thomas

et al. 1999

Journal of Leukocyte Biology

View full text Add to dashboard Cite

Since the first description of Alzheimer's disease (AD) in 1907, significant progress was made into understanding disease pathophysiology. The enormous effort in AD research has translated into the discovery of genetic linkages for disease, into elucidating the structure and function of the etiologic ␤-amyloid protein, and into unraveling the seemingly complex neuroimmunological cascade that affects neuronal dysfunction. Although effective therapies do not currently exist, many are being developed. We propose that the neuropathogenesis of AD, in measure, revolves around the immunological activation of glial cells, which in turn leads to alterations in inflammatory neurotoxin production, and ultimately to neuronal injury and death. Elucidating the mechanisms involved in such glial cell immune activation should provide valuable insights into understanding the disease process and in providing effective therapeutics to prevent and/or retard the devastating neurodegeneration that afflicts so many of our elderly. J. Leukoc. Biol. 65: 416-427; 1999.

show abstract

Signaling Through G Protein-Coupled Receptors

Cited by 14 publications

References 188 publications

Cloning and transcriptional expression of a leucokinin‐like peptide receptor from the Southern cattle tick, Boophilus microplus (Acari: Ixodidae)

Cloning and transcriptional expression of a leucokinin‐like peptide receptor from the Southern cattle tick, Boophilus microplus (Acari: Ixodidae)

Functional Segregation of the Highly Conserved Basic Motifs within the Third Endoloop of the Human Secretin Receptor

Insights into the neurodegenerative process of Alzheimer's disease: a role for mononuclear phagocyte-associated inflammation and neurotoxicity

Contact Info

Product

Resources

About