| RRC ID |
28993
|
| Author |
Kim JY, Soede RD, Schaap P, Valkema R, Borleis JA, Van Haastert PJ, Devreotes PN, Hereld D.
|
| Title |
Phosphorylation of chemoattractant receptors is not essential for chemotaxis or termination of G-protein-mediated responses.
|
| Journal |
J Biol Chem
|
| Abstract |
In several G-protein-coupled signaling systems, ligand-induced receptor phosphorylation by specific kinases is suggested to lead to desensitization via mechanisms including receptor/G-protein uncoupling, receptor internalization, and receptor down-regulation. We report here that elimination of phosphorylation of a chemoattractant receptor of Dictyostelium, either by site-directed substitution of the serines or by truncation of the C-terminal cytoplasmic domain, completely prevented agonist-induced loss of ligand binding but did not impair the adaptation of several receptor-mediated responses including the activation of adenylyl and guanylyl cyclases and actin polymerization. In addition, the phosphorylation-deficient receptors were capable of mediating chemotaxis, aggregation, and differentiation. We propose that for chemoattractant receptors agonist-induced phosphorylation regulates surface binding activity but other phosphorylation-independent mechanisms mediate response adaptation.
|
| Volume |
272(43)
|
| Pages |
27313-8
|
| Published |
1997-10-24
|
| DOI |
10.1074/jbc.272.43.27313
|
| PII |
S0021-9258(18)68047-0
|
| PMID |
9341180
|
| MeSH |
Actins / metabolism
Adenylyl Cyclases / metabolism
Amino Acid Substitution
Animals
Cell Aggregation
Cell Differentiation
Chemotaxis*
Dictyostelium / physiology*
Enzyme Activation
GTP-Binding Proteins / metabolism*
Guanylate Cyclase / metabolism
Kinetics
Mutagenesis, Site-Directed
Phosphorylation
Receptors, Cyclic AMP / biosynthesis
Receptors, Cyclic AMP / physiology*
Recombinant Proteins / biosynthesis
Sequence Deletion
Serine
|
| IF |
4.238
|
| Times Cited |
75
|
|
WOS Category
|
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| Resource |
| Cellular slime molds |
S00410 |
