The browser you are using is not supported by this website. All versions of Internet Explorer are no longer supported, either by us or Microsoft (read more here: https://www.microsoft.com/en-us/microsoft-365/windows/end-of-ie-support).

Please use a modern browser to fully experience our website, such as the newest versions of Edge, Chrome, Firefox or Safari etc.

A tyrosine residue in the juxtamembrane segment of the platelet-derived growth factor beta-receptor is critical for ligand-mediated endocytosis

På svenska

Author

Summary, in English

The importance of tyrosine residues in ligand-mediated endocytosis of the platelet-derived growth factor beta-receptor was analyzed using a series of tyrosine residue-mutated beta-receptors, which together cover all of the tyrosine residues in the juxtamembrane segment, the kinase insert, and the carboxyl-terminal tail; also certain of the tyrosine residues within the first and second parts of the kinase domain were examined. Of all of these tyrosine residues, only Tyr-579 seemed to be important for internalization, since mutation of this residue resulted in substantial reduction in the rate of ligand-induced receptor internalization (approximately 60% of the wild-type level). Replacement of Tyr-579 by either an aromatic (Phe) or a nonaromatic (Asp) residue reduced the efficiency of the mutant receptors in internalization to the same extent, suggesting that the role of Tyr-579 in the beta-receptor is different from that of the previously described tyrosine-based internalization motifs, which were first determined for the low density lipoprotein receptor. Tyr-579 has been found to be an autophosphorylation site in the beta-receptor. Moreover, the internalization rate of a kinase negative receptor mutant was not altered by the additional mutation of Tyr-579. Thus, it is likely that phosphorylation of Tyr-579 is important for ligand-induced internalization of the beta-receptor.

Publishing year

1994

Language

English

Pages

4917-4921

Publication/Series

Journal of Biological Chemistry

Volume

269

Issue

7

Document type

Journal article

Publisher

American Society for Biochemistry and Molecular Biology

Topic

  • Medicinal Chemistry

Keywords

  • Amino Acid SequenceAnimalsAortaClone Cells*EndocytosisEndothelium
  • Vascular/*metabolismHumansIodine RadioisotopesKineticsMolecular Sequence DataMutagenesis
  • IGF Type 2/chemistryReceptors
  • Site-DirectedPlatelet-Derived Growth Factor/*metabolismReceptor
  • Platelet-Derived GrowthFactor/biosynthesis/chemistry/*metabolismRecombinant Proteins/metabolismSequence Homology
  • Amino AcidSwineTransfection*Tyrosine

Status

Published

ISBN/ISSN/Other

  • ISSN: 1083-351X